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Conserved domains on  [gi|171848964|pdb|2Z5Y|A]
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Chain A, Amine oxidase [flavin-containing] A

Protein Classification

flavin monoamine oxidase family protein( domain architecture ID 11440890)

flavin monoamine oxidase family protein functions as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60|1.10.405.10
EC:  1.-.-.-
Gene Ontology:  GO:0000166|GO:0016491
SCOP:  4000128

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-453 1.69e-135

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 399.30  E-value: 1.69e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD-YVDVGGAYVGPTQNRILRLSKELGIETYK 79
Cdd:COG1231   6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGlYAELGAMRIPPSHTNLLALARELGLPLEP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       80 -VNVSERLVQYVKGKTYPFRAAfppvwnPIAYLDYNNLWRTIDN-MGKEIPtdaPWEAQhADKWDKMTMKELIDKICWTK 157
Cdd:COG1231  86 fPNENGNALLYLGGKRVRAGEI------AADLRGVAELLAKLLRaLAAALD---PWAHP-AAELDRESLAEWLRRNGASP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      158 TARRFAYLFVNINVTSEPHEVSALWFLWYvkqcggttrIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVD 237
Cdd:COG1231 156 SARRLLGLLGAGEYGADPDELSLLDLLRY---------AASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIR 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      238 QSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIED 317
Cdd:COG1231 227 QDGDGVTVTTDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGISLTD 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      318 EdaPISITLDDTKP-DGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSqEALHPVHYEEKNWCEEQYSGGCY 396
Cdd:COG1231 307 L--PIRQTWYPSNGpDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGV-YAAEPVDYVSTDWGRDPWSRGAY 383

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
2Z5Y_A      397 tAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLG 453
Cdd:COG1231 384 -AAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEWPGWVEGALESGERAAAEILARLG 439
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-453 1.69e-135

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 399.30  E-value: 1.69e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD-YVDVGGAYVGPTQNRILRLSKELGIETYK 79
Cdd:COG1231   6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGlYAELGAMRIPPSHTNLLALARELGLPLEP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       80 -VNVSERLVQYVKGKTYPFRAAfppvwnPIAYLDYNNLWRTIDN-MGKEIPtdaPWEAQhADKWDKMTMKELIDKICWTK 157
Cdd:COG1231  86 fPNENGNALLYLGGKRVRAGEI------AADLRGVAELLAKLLRaLAAALD---PWAHP-AAELDRESLAEWLRRNGASP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      158 TARRFAYLFVNINVTSEPHEVSALWFLWYvkqcggttrIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVD 237
Cdd:COG1231 156 SARRLLGLLGAGEYGADPDELSLLDLLRY---------AASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIR 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      238 QSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIED 317
Cdd:COG1231 227 QDGDGVTVTTDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGISLTD 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      318 EdaPISITLDDTKP-DGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSqEALHPVHYEEKNWCEEQYSGGCY 396
Cdd:COG1231 307 L--PIRQTWYPSNGpDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGV-YAAEPVDYVSTDWGRDPWSRGAY 383

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
2Z5Y_A      397 tAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLG 453
Cdd:COG1231 384 -AAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEWPGWVEGALESGERAAAEILARLG 439
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 12-449 1.44e-85

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 271.29  E-value: 1.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         12 ISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGGAYVGPTQNRILRLSKELGIET---YKVNVSERLVQ 88
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGF-LIELGAMWFHGAQPPLLALLKELGLEDrlvLPDPAPFYTVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         89 YVKGKTYPFR-----AAFPPVWNPIAYLDYN---------NLWRTIDNMGKEIPTDAPWEAQHADKwdkmtmkELIDKIC 154
Cdd:pfam01593  80 FAGGRRYPGDfrrvpAGWEGLLEFGRLLSIPeklrlglaaLASDALDEFDLDDFSLAESLLFLGRR-------GPGDVEV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        155 WTKTARRFAYLFVNINVT------SEPHEVSALWFLWYVKQcggttrifsvtNGGQERKFVGGSGQVSERI-MDLLGDQV 227
Cdd:pfam01593 153 WDRLIDPELFAALPFASGafagdpSELSAGLALPLLWALLG-----------EGGSLLLPRGGLGALPDALaAQLLGGDV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        228 KLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKK 307
Cdd:pfam01593 222 RLNTRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        308 DYCG--CMIIEDEDAP-ISITLDDTKPDGSLPAIMGFI-LARKADRLAKLHKEIRKKKICELYAKVLGsQEALHPVHYEE 383
Cdd:pfam01593 302 GLLGllSELLTGLGTAfSWLTFPNRAPPGKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFG-EEAPEPLRVLV 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2Z5Y_A        384 KNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVL 449
Cdd:pfam01593 381 SDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAVL 446
PLN02268 PLN02268
probable polyamine oxidase
 5-447 4.39e-23

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 101.69  E-value: 4.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTirnehvDY-----VDVGGAYV-GPTQ-NRILRLSKELGIET 77
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT------DYsfgfpVDMGASWLhGVCNeNPLAPLIGRLGLPL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        78 YKVNVSERLVQYVKGKTYpfrAAFppvwnpiayldynnlwrtiDNMGKEIPTDAPWEAQHA-DKWDKMTMK---ELIDKI 153
Cdd:PLN02268  77 YRTSGDNSVLYDHDLESY---ALF-------------------DMDGNQVPQELVTKVGETfERILEETEKvrdEHEEDM 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       154 CWTKTarrfaylfVNINVTSEP--------HEVsalwFLWYVKQCGG-----TTRIfSVTNGGQERKFVGGSGQVS---E 217
Cdd:PLN02268 135 SLLQA--------ISIVLERHPelrleglaHEV----LQWYLCRMEGwfaadADTI-SLKSWDQEELLEGGHGLMVrgyD 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       218 RIMDLL--GDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIP-PTLTAK-IHFRPELPAERNQLIQRLPMGAVI 293
Cdd:PLN02268 202 PVINTLakGLDIRLNHRVTKIVRRYNGVKVTVEDGTTFVADAAIIAVPlGVLKANiIKFEPELPEWKEEAISDLGVGIEN 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       294 KCMMYYKEAFWKKKDYCGCMiiededAPISIT----LDDTKPDGSlPAIMGFILARKADRLAKLHKEIRKKKICELYAKV 369
Cdd:PLN02268 282 KIALHFDSVFWPNVEFLGVV------APTSYGcsyfLNLHKATGH-PVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKM 354

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2Z5Y_A       370 LgsQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRvIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAARE 447
Cdd:PLN02268 355 L--PDATEPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYER-LRAPVDNLFFAGEATSSDFPGSVHGAYSTGVMAAEE 429
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 2-81 2.32e-10

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 62.55  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A          2 MFDVVVIGGGISGLSAA----KLLTEYGVSVLVLEARDRVGGRTYTiRNEHVDYVDVGGAYVGPTQNRILRLSKELGIET 77
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQT-VKEDGYLIERGPDSFLERKKSAPDLVKDLGLEH 80


                  ....
2Z5Y_A         78 YKVN 81
Cdd:TIGR00562  81 VLVS 84
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 5-59 3.04e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 38.26  E-value: 3.04e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2Z5Y_A           5 VVVIGGGISGLSAAKLLTEYGVSVLVL--------EARDRVGGRTYTIR------NEHVDYVD--VGGAYV 59
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTLYsqaellEEAVKEADlvIGAVLI 93
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 4-35 4.06e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 39.31  E-value: 4.06e-03
                        10        20        30
                ....*....|....*....|....*....|..
2Z5Y_A        4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARD 35
Cdd:cd01620 164 KVLIIGAGVVGLGAAKIAKKLGANVLVYDIKE 195
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-453 1.69e-135

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 399.30  E-value: 1.69e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD-YVDVGGAYVGPTQNRILRLSKELGIETYK 79
Cdd:COG1231   6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGlYAELGAMRIPPSHTNLLALARELGLPLEP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       80 -VNVSERLVQYVKGKTYPFRAAfppvwnPIAYLDYNNLWRTIDN-MGKEIPtdaPWEAQhADKWDKMTMKELIDKICWTK 157
Cdd:COG1231  86 fPNENGNALLYLGGKRVRAGEI------AADLRGVAELLAKLLRaLAAALD---PWAHP-AAELDRESLAEWLRRNGASP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      158 TARRFAYLFVNINVTSEPHEVSALWFLWYvkqcggttrIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVD 237
Cdd:COG1231 156 SARRLLGLLGAGEYGADPDELSLLDLLRY---------AASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIR 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      238 QSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIED 317
Cdd:COG1231 227 QDGDGVTVTTDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGISLTD 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      318 EdaPISITLDDTKP-DGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSqEALHPVHYEEKNWCEEQYSGGCY 396
Cdd:COG1231 307 L--PIRQTWYPSNGpDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGV-YAAEPVDYVSTDWGRDPWSRGAY 383

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
2Z5Y_A      397 tAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLG 453
Cdd:COG1231 384 -AAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEWPGWVEGALESGERAAAEILARLG 439
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 12-449 1.44e-85

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 271.29  E-value: 1.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         12 ISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGGAYVGPTQNRILRLSKELGIET---YKVNVSERLVQ 88
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGF-LIELGAMWFHGAQPPLLALLKELGLEDrlvLPDPAPFYTVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         89 YVKGKTYPFR-----AAFPPVWNPIAYLDYN---------NLWRTIDNMGKEIPTDAPWEAQHADKwdkmtmkELIDKIC 154
Cdd:pfam01593  80 FAGGRRYPGDfrrvpAGWEGLLEFGRLLSIPeklrlglaaLASDALDEFDLDDFSLAESLLFLGRR-------GPGDVEV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        155 WTKTARRFAYLFVNINVT------SEPHEVSALWFLWYVKQcggttrifsvtNGGQERKFVGGSGQVSERI-MDLLGDQV 227
Cdd:pfam01593 153 WDRLIDPELFAALPFASGafagdpSELSAGLALPLLWALLG-----------EGGSLLLPRGGLGALPDALaAQLLGGDV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        228 KLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKK 307
Cdd:pfam01593 222 RLNTRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        308 DYCG--CMIIEDEDAP-ISITLDDTKPDGSLPAIMGFI-LARKADRLAKLHKEIRKKKICELYAKVLGsQEALHPVHYEE 383
Cdd:pfam01593 302 GLLGllSELLTGLGTAfSWLTFPNRAPPGKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFG-EEAPEPLRVLV 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2Z5Y_A        384 KNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVL 449
Cdd:pfam01593 381 SDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAVL 446
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 2-452 5.96e-24

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 104.14  E-value: 5.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        2 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEhvDY-VDVGG-AYVgPTQNRILRLSKELGIET-- 77
Cdd:COG1232   1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVD--GFrIDRGPhSFL-TRDPEVLELLRELGLGDel 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       78 YKVNVSERLVqYVKGKTYP-------------------FRAAFPPVWNPIAYLDYNNL--WrTIDNMGKEIptdapweaq 136
Cdd:COG1232  78 VWPNTRKSYI-YYGGKLHPlpqgplallrspllslagkLRALLELLAPRRPPGEDESLaeF-VRRRFGREV--------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      137 hadkWDKMtMKELIDKIcwtktarrFAYlfvninvtsEPHEVSALWFLWYVKQ---------CGGTTRIFSVTNGGQERK 207
Cdd:COG1232 147 ----YERL-VEPLLEGV--------YAG---------DPDELSADWAFPRLKRlelehgsliKGALALRKGAKAGEVFGY 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      208 FVGGSGQVSERIMDLLGD-QVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIhFRPeLPAERNQLIQR 286
Cdd:COG1232 205 LRGGLGTLVEALAEALEAgEIRLGTRVTAIEREGGGWRVTTSDGETIEADAVVSATPAPALARL-LAP-LPPEVAAALAG 282

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      287 LPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPIS-ITLDDTK-----PDG--SLPAIMGFilARKADRLAKLHKEIR 358
Cdd:COG1232 283 IPYASVAVVALGFDRPDLPPPDGFGWLVPRDEGVPILaVTFSSNKwphraPDGkvLLRLEVGG--AGDPELWQLSDEELV 360

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      359 KKKICELyAKVLGSQEAlhPVHYEEKNWcEE---QYSGGcYTAYFPPgimtqygrvIRQPVGR---IFFAGtetatkwSG 432
Cdd:COG1232 361 ALALADL-RKLLGIDAE--PVDTRVVRW-PKaypQYTVG-HLERVAA---------IREALAAlpgLYLAG-------RA 419

                       490       500
                ....*....|....*....|....
2Z5Y_A      433 Y----MEGAVEAGERAAREVLNGL 452
Cdd:COG1232 420 YdgvgLPDCIRSGREAAERILAEL 443
PLN02268 PLN02268
probable polyamine oxidase
 5-447 4.39e-23

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 101.69  E-value: 4.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTirnehvDY-----VDVGGAYV-GPTQ-NRILRLSKELGIET 77
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT------DYsfgfpVDMGASWLhGVCNeNPLAPLIGRLGLPL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        78 YKVNVSERLVQYVKGKTYpfrAAFppvwnpiayldynnlwrtiDNMGKEIPTDAPWEAQHA-DKWDKMTMK---ELIDKI 153
Cdd:PLN02268  77 YRTSGDNSVLYDHDLESY---ALF-------------------DMDGNQVPQELVTKVGETfERILEETEKvrdEHEEDM 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       154 CWTKTarrfaylfVNINVTSEP--------HEVsalwFLWYVKQCGG-----TTRIfSVTNGGQERKFVGGSGQVS---E 217
Cdd:PLN02268 135 SLLQA--------ISIVLERHPelrleglaHEV----LQWYLCRMEGwfaadADTI-SLKSWDQEELLEGGHGLMVrgyD 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       218 RIMDLL--GDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIP-PTLTAK-IHFRPELPAERNQLIQRLPMGAVI 293
Cdd:PLN02268 202 PVINTLakGLDIRLNHRVTKIVRRYNGVKVTVEDGTTFVADAAIIAVPlGVLKANiIKFEPELPEWKEEAISDLGVGIEN 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       294 KCMMYYKEAFWKKKDYCGCMiiededAPISIT----LDDTKPDGSlPAIMGFILARKADRLAKLHKEIRKKKICELYAKV 369
Cdd:PLN02268 282 KIALHFDSVFWPNVEFLGVV------APTSYGcsyfLNLHKATGH-PVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKM 354

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2Z5Y_A       370 LgsQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRvIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAARE 447
Cdd:PLN02268 355 L--PDATEPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYER-LRAPVDNLFFAGEATSSDFPGSVHGAYSTGVMAAEE 429
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 2-290 7.97e-22

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 98.38  E-value: 7.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        2 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTI-RNEHVdyVDVGGAYVGPTQ--NRILRlskELGIETY 78
Cdd:COG1233   3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFeRPGFR--FDVGPSVLTMPGvlERLFR---ELGLEDY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       79 kVNVSERLVQYV----KGKTYP-----------FRAAFPPVWNpiAYLDYNNLWRTIDNMGKE----IPTDAPWEAQHAD 139
Cdd:COG1233  78 -LELVPLDPAYRvpfpDGRALDlprdlertaaeLERLFPGDAE--AYRRFLAELRRLYDALLEdllyRPLLSLRDLLRPL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      140 KWDKM------TMKELIDKicWTKTAR-RFAYLFVNINVTSEPHEVSAL-WFLWYVKQCGGTTRIfsvtnggqerkfVGG 211
Cdd:COG1233 155 ALARLlrlllrSLRDLLRR--YFKDPRlRALLAGQALYLGLSPDRTPALyALIAYLEYAGGVWYP------------KGG 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      212 SGQVSERIMDL---LGDQVKLNHPVTHVDQSSDNII-IETLNHEHYECKYVI-NAIPPTLTAKIHFRPELPAERNQLIQR 286
Cdd:COG1233 221 MGALADALARLaeeLGGEIRTGAEVERILVEGGRATgVRLADGEEIRADAVVsNADPAHTYLRLLGEEALPARYRRRLER 300


                ....
2Z5Y_A      287 LPMG 290
Cdd:COG1233 301 FRYS 304
PLN02676 PLN02676
polyamine oxidase
 3-459 1.72e-17

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 85.15  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         3 FDVVVIGGGISGLSAAKLLTEYGVS-VLVLEARDRVGGRTYTIRNEHVDyVDVGGAYV----GPTQNRILRLSKELGIET 77
Cdd:PLN02676  27 PSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRMRKANFAGVS-VELGANWVegvgGPESNPIWELANKLKLRT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        78 YkvnvserlvqyvkgktypfraafppvwnpiaYLDYNNLWRTI-DNMGKEIPTDapwEAQHADKwDKMTMKELIDKICWT 156
Cdd:PLN02676 106 F-------------------------------YSDFDNLSSNIyKQDGGLYPKK---VVQKSMK-VADASDEFGENLSIS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       157 KTARR------FAYLFVNINVTSEPHEVsALWFLWY---------VKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMD 221
Cdd:PLN02676 151 LSAKKavdisiLTAQRLFGQVPKTPLEM-VIDYYNYdyefaepprVTSLKNTEPNPTFVDFGEDEYFVADPRGYESLVYY 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       222 LLGD------------QVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVInaIPPTL----TAKIHFRPELPAERNQLIQ 285
Cdd:PLN02676 230 LAEQflstksgkitdpRLKLNKVVREISYSKNGVTVKTEDGSVYRAKYVI--VSVSLgvlqSDLIKFKPPLPDWKIEAIY 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       286 RLPMGAVIKCMMYYKEAFWKkkdyCG----CMIIEDEDA---PISITLDDTKPDGSLpaIMGFILARKADRLAKLHKEIR 358
Cdd:PLN02676 308 QFDMAVYTKIFLKFPYKFWP----SGpgteFFLYAHERRgyyPFWQHLENEYPGSNV--LFVTVTDEESRRIEQQPDSET 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       359 KKKICELYAKVLGSQ-----EALHPvhyeekNWCEEQYSGGCYTAYfPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGY 433
Cdd:PLN02676 382 KAEIMEVLRKMFGPNipeatDILVP------RWWSNRFFKGSYSNW-PIGVSRYEFDQIRAPVGRVYFTGEHTSEKYNGY 454

                        490       500
                 ....*....|....*....|....*.
2Z5Y_A       434 MEGAVEAGERAAREVLNGLGKVTEKD 459
Cdd:PLN02676 455 VHGAYLAGIDTANDLLECIKKKKCRK 480
PRK07233 PRK07233
hypothetical protein; Provisional
 5-296 2.34e-16

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 81.09  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVD---YvdvggaY--VGPTQNRILRLSKELGIEtyk 79
Cdd:PRK07233   2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLPierF------YhhIFKSDEALLELLDELGLE--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        80 vnvsERLV-------QYVKGKTYPFRaafppvwNPIAYLDYNNLwRTIDN--MGkeiptdapWEAQHADK---W---DKM 144
Cdd:PRK07233  73 ----DKLRwretktgYYVDGKLYPLG-------TPLELLRFPHL-SLIDKfrLG--------LLTLLARRikdWralDKV 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       145 TMKELIDKICWTKTARRFaylFvninvtsEP----------HEVSALWFLWYVKQcggttRIFSVTNGGQERK--FVGGS 212
Cdd:PRK07233 133 PAEEWLRRWSGEGVYEVF---W-------EPlleskfgdyaDDVSAAWLWSRIKR-----RGNRRYSLFGEKLgyLEGGF 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       213 GQVSERIMDLL---GDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIhfRPELPAERNQLIQRLP- 288
Cdd:PRK07233 198 ATLIDALAEAIearGGEIRLGTPVTSVVIDGGGVTGVEVDGEEEDFDAVISTAPPPILARL--VPDLPADVLARLRRIDy 275


                 ....*...
2Z5Y_A       289 MGAVikCM 296
Cdd:PRK07233 276 QGVV--CM 281
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 4-449 2.81e-14

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 75.80  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEH---VDYVDVGGAYV-GPTQNRILRLSKELGIETYK 79
Cdd:PLN02328 240 NVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGdgvVAAADLGGSVLtGINGNPLGVLARQLGLPLHK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        80 VNvserlvqyvkgktypfraAFPPVWNPiayldynnlwrtiDNMGKEIPTDAPWEAqhadkwdkmTMKELIDKICWTKTA 159
Cdd:PLN02328 320 VR------------------DICPLYLP-------------DGKAVDAEIDSKIEA---------SFNKLLDRVCKLRQA 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       160 RRFAYLFVNIN-------------VTSEPHEVSAL-WFLWYVKQCGGTTrifsVTN-------------GGQERKFVGGS 212
Cdd:PLN02328 360 MIEEVKSVDVNlgtaleafrhvykVAEDPQERMLLnWHLANLEYANASL----MSNlsmaywdqddpyeMGGDHCFIPGG 435

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       213 GQ--VSERIMDLlgdQVKLNHPVTHVDQSSDNIIIETLNHEhYECKYVINAIPPTLTAK--IHFRPELPAERNQLIQRLP 288
Cdd:PLN02328 436 NDtfVRELAKDL---PIFYERTVESIRYGVDGVIVYAGGQE-FHGDMVLCTVPLGVLKKgsIEFYPELPQRKKDAIQRLG 511

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       289 MGAVIKCMMYYKEAFWKKK-DYCGcMIIEDEDAPISITLDDTKPDGS-LPAIMGFILARKADRLAKLHKEIRKKKICELY 366
Cdd:PLN02328 512 YGLLNKVALLFPYNFWGGEiDTFG-HLTEDPSMRGEFFLFYSYSSVSgGPLLIALVAGDAAVKFETLSPVESVKRVLQIL 590

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       367 AKVLGSQEAL--HPVHYEEKNWCEEQYSGGCYTaYFPPGIMTQYGRVIRQPV--GRIFFAGTETATKWSGYMEGAVEAGE 442
Cdd:PLN02328 591 RGIFHPKGIVvpDPVQAVCTRWGKDCFTYGSYS-YVAVGSSGDDYDILAESVgdGRVFFAGEATNKQYPATMHGAFLSGM 669


                 ....*..
2Z5Y_A       443 RAAREVL 449
Cdd:PLN02328 670 REAANIL 676
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
7-73 2.92e-14

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 67.56  E-value: 2.92e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2Z5Y_A          7 VIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR-NEHVdyVDVGG-AYVGPTQNRILRLSKEL 73
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRvPGYV--FDYGAhIFHGSDEPNVRDLLDEL 67
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 2-453 2.90e-13

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 71.81  E-value: 2.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        2 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR----NEHVDYvdvG-----GAYvgptQNrILRLSKE 72
Cdd:COG3349   3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPdpdtGLPIDN---GqhvllGCY----RN-TLDLLRR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       73 LGIETYKVNVSERLVQYVKGKTYPFRAA--FPPVWNPIAYL--------DYNNLWRTIdnmgkeiptdAPWEAQHADKWD 142
Cdd:COG3349  75 IGAADNLVGPEPLQFPLPGGRRWTLRAPrlPAPLHLLRALLrapglslaDRLALLRLL----------TACRERRWRELD 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      143 KMTMKELIDKICWT-KTARRFAYLF----VNInvtsEPHEVSALWFLwyvkqcggttRIFsvtnggqeRKFVGGSGQVSE 217
Cdd:COG3349 145 DISVADWLRRHGQSpRLIRRLWEPLllaaLNT----PPEQASARLAL----------TVL--------RETLLAGPAASD 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      218 -RIM-----DLLGD-----------QVKLNHPVTHVDQSSDNI-IIETLNHEHYECKYVINAIPPTLTAKIhfrpeLPAE 279
Cdd:COG3349 203 lLVPrgplsELFVDpalaylearggEVRLGTRVRALEFDGGRVtGLVLADGETVPADAVVLAVPPEVAARL-----LPEL 277

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      280 RN----QLIQRLPMGAVIKCMMYYKEAF-WKKKDYCGcMIiedeDAPISITLDDTKPDGSLPAIMGFILArKADRLAKL- 353
Cdd:COG3349 278 ARlpelGLLAPLEYSPIVNVHLWLDRPVtLGPPPFAG-LV----GSTSQWVFDRGAGDGGQGGVLSVVIS-AADRLLDLs 351

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A      354 HKEIRKKKICELyAKVLGSQEALHPVHYE---EKnwceeqysggcyTAYF---P------PGIMTqygrvirqPVGRIFF 421
Cdd:COG3349 352 REELAAEVWAEL-AALLPAAREALPVWSRvvrEK------------RATFaatPgsdrlrPGART--------PIPNLFL 410

                       490       500       510
                ....*....|....*....|....*....|..
2Z5Y_A      422 AGTETATKWSGYMEGAVEAGERAAREVLNGLG 453
Cdd:COG3349 411 AGDWTATGLPATMEGAVRSGRRAANAILARLG 442
PLN03000 PLN03000
amine oxidase
 4-445 1.92e-12

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 70.05  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR---NEHVDYVDVGGAYV-GPTQNRILRLSKELGIETYK 79
Cdd:PLN03000 186 SVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKmeaNRVGAAADLGGSVLtGTLGNPLGIIARQLGSSLYK 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        80 vnvserlvqyVKGKTYPFRAAFPPVwNPIAYL----DYNNLwrtIDNMGK------EIPTDAPWEAQHAdkwdkmTMKEL 149
Cdd:PLN03000 266 ----------VRDKCPLYRVDGKPV-DPDVDLkvevAFNQL---LDKASKlrqlmgDVSMDVSLGAALE------TFRQV 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       150 IDKICWTKTARRFAYLFVNINVtSEPHEVSALWFLWYVKQCggttrifSVTNGGQERKFVGGSGqvseRIMDLLGDQVKL 229
Cdd:PLN03000 326 SGNDVATEEMGLFNWHLANLEY-ANAGLVSKLSLAFWDQDD-------PYDMGGDHCFLPGGNG----RLVQALAENVPI 393

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       230 NHPVT-HVDQSSDNIIIETLNHEHYECKYVINAIPPTL--TAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKK 306
Cdd:PLN03000 394 LYEKTvQTIRYGSNGVKVIAGNQVYEGDMVLCTVPLGVlkNGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYVFWST 473

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       307 K-DYCGcMIIEDEDAPISITL-DDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQ--EALHPVHYE 382
Cdd:PLN03000 474 DlDTFG-HLTEDPNYRGEFFLfYSYAPVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYEPQgiNVPDPLQTV 552

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
2Z5Y_A       383 EKNWCEEQYSGGCYTAYFPPGIMTQYGrVIRQPV--GRIFFAGTETATKWSGYMEGAVEAGERAA 445
Cdd:PLN03000 553 CTRWGGDPFSLGSYSNVAVGASGDDYD-ILAESVgdGRLFFAGEATTRRYPATMHGAFVTGLREA 616
PLN02529 PLN02529
lysine-specific histone demethylase 1
 5-449 6.55e-12

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 67.99  E-value: 6.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTI---RNEHVDYVDVGGAYV-GPTQNRILRLSKELGIETYKV 80
Cdd:PLN02529 163 VIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQkmgRKGQFAAVDLGGSVItGIHANPLGVLARQLSIPLHKV 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        81 NVSerlvqyvkgktypfraafPPVWNPIAYLdynnlwrtidnMGKEIptDAPWEAQHADKWDKMT-----MKELIDKICW 155
Cdd:PLN02529 243 RDN------------------CPLYKPDGAL-----------VDKEI--DSNIEFIFNKLLDKVTelrqiMGGFANDISL 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       156 TKTARRFAYLFVNINVTSEPHEVSalWFLWYVKQC-GGTTRIFSVTNGGQERKFVGGSGQV-----SERIMDLLGDQVKL 229
Cdd:PLN02529 292 GSVLERLRQLYGVARSTEERQLLD--WHLANLEYAnAGCLSDLSAAYWDQDDPYEMGGDHCflaggNWRLINALCEGVPI 369

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       230 NHPVT-HVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAK--IHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKK 306
Cdd:PLN02529 370 FYGKTvDTIKYGNDGVEVIAGSQVFQADMVLCTVPLGVLKKrtIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWGE 449

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       307 K-DYCGCMiIEDEDAPISITL---DDTKPDGslPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQ--EALHPVH 380
Cdd:PLN02529 450 ElDTFGCL-NESSNKRGEFFLfygYHTVSGG--PALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNPKgiNVPDPIQ 526

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2Z5Y_A       381 YEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVL 449
Cdd:PLN02529 527 TICTRWGSDPLSYGSYSHVRVQSSGSDYDILAESVSGRLFFAGEATTRQYPATMHGAFLSGLREASRIL 595
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 1-42 1.72e-11

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 66.04  E-value: 1.72e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG----RTY 42
Cdd:COG2072   5 EHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdNRY 50
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-59 3.88e-11

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 64.51  E-value: 3.88e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGGAYV 59
Cdd:COG3380   2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGG-RFDHGAQYF 59
PLN02976 PLN02976
amine oxidase
 5-311 1.48e-10

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 64.12  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A          5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVG------PTQNRILRLS---KELGI 75
Cdd:PLN02976  696 IIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVPVDLGASIITgveadvATERRPDPSSlicAQLGL 775

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         76 ETYKVNVSERLVQYVKGKTYPfraafppvwnpiAYLD------YNNLwrtIDNMGKEIptdapweAQHADKWDKMTMKel 149
Cdd:PLN02976  776 ELTVLNSDCPLYDVVTGEKVP------------ADLDealeaeYNSL---LDDMVLLV-------AQKGEHAMKMSLE-- 831

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        150 iDKICWTKTARRFAYLFVNINVTSEPHEVSALW-------------------FL---------WYVKQ----CGGTTRIF 197
Cdd:PLN02976  832 -DGLEYALKRRRMPRPGVDIDETELGNAADDLYdsastgvdgghcekeskedVLsplerrvmnWHFAHleygCAALLKEV 910

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        198 SVTNGGQErKFVGGSGQVS-------ERIMDLLGD--QVKLNHPVTHV----------DQSSDNIIIETLNHEHYECKYV 258
Cdd:PLN02976  911 SLPYWNQD-DVYGGFGGAHcmikggySNVVESLAEglDIHLNHVVTDVsygskdagasGSSRKKVKVSTSNGSEFLGDAV 989

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
2Z5Y_A        259 INAIP-PTLTAK-IHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKK-DYCG 311
Cdd:PLN02976  990 LITVPlGCLKAEtIKFSPPLPDWKYSSIQRLGFGVLNKVVLEFPEVFWDDSvDYFG 1045
PLN02576 PLN02576
protoporphyrinogen oxidase
 4-76 2.19e-10

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 62.72  E-value: 2.19e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2Z5Y_A         4 DVVVIGGGISGLSAA-KLLTEYGVSVLVLEARDRVGGRTYTIrnEHVDYVDVGGAYVGPTQNRILRLSKELGIE 76
Cdd:PLN02576  14 DVAVVGAGVSGLAAAyALASKHGVNVLVTEARDRVGGNITSV--SEDGFIWEEGPNSFQPSDPELTSAVDSGLR 85
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 2-81 2.32e-10

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 62.55  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A          2 MFDVVVIGGGISGLSAA----KLLTEYGVSVLVLEARDRVGGRTYTiRNEHVDYVDVGGAYVGPTQNRILRLSKELGIET 77
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQT-VKEDGYLIERGPDSFLERKKSAPDLVKDLGLEH 80


                  ....
2Z5Y_A         78 YKVN 81
Cdd:TIGR00562  81 VLVS 84
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 4-41 1.27e-08

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 56.64  E-value: 1.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
2Z5Y_A          4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 41
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGA 38
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 5-45 1.62e-08

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 56.90  E-value: 1.62e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
2Z5Y_A          5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIR 45
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLE 41
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-79 2.27e-08

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 56.07  E-value: 2.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGGRTyTIRNehvdyvdvGG----AYVGPTQNRILRLSKElGIE 76
Cdd:COG0665   1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSGA-SGRN--------AGqlrpGLAALADRALVRLARE-ALD 69


                ...
2Z5Y_A       77 TYK 79
Cdd:COG0665  70 LWR 72
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-44 2.29e-08

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 55.71  E-value: 2.29e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARD--RVGGRTYTI 44
Cdd:COG0654   2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPppRPDGRGIAL 47
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 5-96 4.61e-08

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 55.24  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYG--VSVLVLEARDRVGGRTYTIRNEhvDYV-DVGG-AYVGptqnR---ILRLSKELGIEt 77
Cdd:PRK11883   3 VAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKD--GFPiELGPeSFLA----RkpsAPALVKELGLE- 75

                         90       100
                 ....*....|....*....|....*..
2Z5Y_A        78 ykvnvsERLVQ--------YVKGKTYP 96
Cdd:PRK11883  76 ------DELVAnttgqsyiYVNGKLHP 96
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
2-38 6.71e-08

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 54.77  E-value: 6.71e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
2Z5Y_A        2 MFDVVVIGGGISGLSAAKLLTEY-GVSVLVLEARDRVG 38
Cdd:COG0579   4 MYDVVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVA 41
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-46 1.16e-07

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 54.11  E-value: 1.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
2Z5Y_A         1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEA--RDRVGGRTYTIRN 46
Cdd:PRK08274   3 SMVDVLVIGGGNAALCAALAAREAGASVLLLEAapREWRGGNSRHTRN 50
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
7-83 2.08e-07

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 53.20  E-value: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A        7 VIGGGISGLSAAKLL-TEYgvSVLVLEARDRVGGRTYTirnehVDyVDVGGAYVG----------PTQNRILRLSKELGI 75
Cdd:COG2907   8 VIGSGISGLTAAWLLsRRH--DVTLFEANDRLGGHTHT-----VD-VDLDGRTVPvdtgfivfneRTYPNLTALFAELGV 79


                ....*...
2Z5Y_A       76 ETYKVNVS 83
Cdd:COG2907  80 PTQPSDMS 87
PLN02612 PLN02612
phytoene desaturase
 5-76 6.18e-07

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 52.15  E-value: 6.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVG-----GAYVGpTQNrilrLSKELGIE 76
Cdd:PLN02612  96 VVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDGDWYETGlhiffGAYPN-VQN----LFGELGIN 167
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
1-37 9.00e-07

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 51.45  E-value: 9.00e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
2Z5Y_A         1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRV 37
Cdd:PRK06183   9 HDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-39 1.55e-06

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 50.60  E-value: 1.55e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 39
Cdd:COG1053   2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PRK07208 PRK07208
hypothetical protein; Provisional
 1-56 1.78e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 50.27  E-value: 1.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
2Z5Y_A         1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVdYVDVGG 56
Cdd:PRK07208   3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKGN-RFDIGG 57
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 4-36 1.65e-05

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 46.93  E-value: 1.65e-05
                          10        20        30
                  ....*....|....*....|....*....|...
2Z5Y_A          4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDR 36
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 5-52 1.84e-05

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 47.00  E-value: 1.84e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
2Z5Y_A        5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYV 52
Cdd:COG0771   7 VLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEVV 54
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-39 1.91e-05

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 47.00  E-value: 1.91e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGG 39
Cdd:COG1249   2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 5-39 2.39e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 46.71  E-value: 2.39e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 39
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 4-39 2.70e-05

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 46.45  E-value: 2.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
2Z5Y_A          4 DVVVIGGGISG----LSAAKLlteyGVSVLVLEARDRVGG 39
Cdd:pfam12831   1 DVVVVGGGPAGvaaaIAAARA----GAKVLLVERRGFLGG 36
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
2-31 2.79e-05

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 46.38  E-value: 2.79e-05
                         10        20        30
                 ....*....|....*....|....*....|
2Z5Y_A         2 MFDVVVIGGGISGLSAAKLLTEYGVSVLVL 31
Cdd:PRK05329   2 KFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
PRK12843 PRK12843
FAD-dependent oxidoreductase;
3-43 2.81e-05

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 46.65  E-value: 2.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
2Z5Y_A         3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYT 43
Cdd:PRK12843  17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
3-46 6.77e-05

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 44.73  E-value: 6.77e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
2Z5Y_A        3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGGR---TYTIRN 46
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQlatTKEIEN 46
HI0933_like pfam03486
HI0933-like protein;
3-38 7.48e-05

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 45.26  E-value: 7.48e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
2Z5Y_A          3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 38
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
2-38 8.65e-05

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 44.81  E-value: 8.65e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
2Z5Y_A         2 MFDVVVIGGGISGLSAAKLLTEY--GVSVLVLEARDRVG 38
Cdd:PRK11728   2 MYDFVIIGGGIVGLSTAMQLQERypGARIAVLEKESGPA 40
PLN02568 PLN02568
polyamine oxidase
 5-43 1.09e-04

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 44.82  E-value: 1.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVS-----VLVLEARDRVGGRTYT 43
Cdd:PLN02568   8 IVIIGAGMAGLTAANKLYTSSAAndmfeLTVVEGGDRIGGRINT 51
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 5-39 1.15e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 44.77  E-value: 1.15e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 39
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 3-38 1.21e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 44.23  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
2Z5Y_A          3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 38
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-37 1.43e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 40.27  E-value: 1.43e-04
                          10        20        30
                  ....*....|....*....|....*....|...
2Z5Y_A          5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRV 37
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
PRK12839 PRK12839
FAD-dependent oxidoreductase;
1-41 1.58e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 44.43  E-value: 1.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
2Z5Y_A         1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 41
Cdd:PRK12839   7 HTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGAT 47
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 1-31 1.70e-04

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 44.33  E-value: 1.70e-04
                        10        20        30
                ....*....|....*....|....*....|.
2Z5Y_A        1 HMFDVVVIGGGISGLSAAKLLTEYGvSVLVL 31
Cdd:COG0029   3 LKTDVLVIGSGIAGLSAALKLAERG-RVTLL 32
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 5-39 1.73e-04

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 43.97  E-value: 1.73e-04
                        10        20        30
                ....*....|....*....|....*....|....*
2Z5Y_A        5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 39
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 4-41 2.01e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 43.82  E-value: 2.01e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
2Z5Y_A          4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 41
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
4-40 2.02e-04

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.08  E-value: 2.02e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
2Z5Y_A        4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGR 40
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGR 178
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 5-38 2.22e-04

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 43.70  E-value: 2.22e-04
                         10        20        30
                 ....*....|....*....|....*....|....
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 38
Cdd:PRK08132  26 VVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
4-39 3.26e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 43.24  E-value: 3.26e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
2Z5Y_A        4 DVVVIGGGISGLSAAKLLTEYGVSVLVL--EARDRVGG 39
Cdd:COG3573   7 DVIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGG 44
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
3-31 3.77e-04

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 42.86  E-value: 3.77e-04
                        10        20
                ....*....|....*....|....*....
2Z5Y_A        3 FDVVVIGGGISGLSAAKLLTEYGVSVLVL 31
Cdd:COG3075   3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
1-34 4.02e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 42.63  E-value: 4.02e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
2Z5Y_A         1 HM-FDVVVIGGGISGLSAAKLLTEYGVSVLVLEAR 34
Cdd:PRK07608   3 HMkFDVVVVGGGLVGASLALALAQSGLRVALLAPR 37
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 2-51 5.00e-04

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 42.51  E-value: 5.00e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
2Z5Y_A        2 MFDVVVIGGGISGLSAAKLLTEY-GVSVLVLEA--RDRV------GGRTYTIRNEHVDY 51
Cdd:COG2303   4 EYDYVIVGAGSAGCVLANRLSEDaGLRVLLLEAggRDDDplirmpAGYAKLLGNPRYDW 62
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 3-78 5.03e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 42.31  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A          3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEA-RDRVGGR---TYTIRN--EHVDYVDVGGAYVGPTQNRILRLSKelGIE 76
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGGcvlSKALLGaaEAPEIASLWADLYKRKEEVVKKLNN--GIE 78


                  ..
2Z5Y_A         77 TY 78
Cdd:pfam07992  79 VL 80
PRK06847 PRK06847
hypothetical protein; Provisional
 4-39 8.74e-04

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 41.78  E-value: 8.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARD--RVGG 39
Cdd:PRK06847   6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
3-39 9.85e-04

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 41.68  E-value: 9.85e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
2Z5Y_A         3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 39
Cdd:PRK05249   6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 4-41 1.40e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 41.24  E-value: 1.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 41
Cdd:PRK06134  14 DVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTT 51
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-37 1.41e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 40.76  E-value: 1.41e-03
                          10        20        30
                  ....*....|....*....|....*....|...
2Z5Y_A          5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRV 37
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 4-39 1.76e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 40.15  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
2Z5Y_A          4 DVVVIGGGISGLSAAKLL-TEYGVSVLVLEARDRVGG 39
Cdd:pfam01946  19 DVVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPGG 55
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 5-39 1.83e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 41.01  E-value: 1.83e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 39
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
5-38 1.84e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 40.79  E-value: 1.84e-03
                         10        20        30
                 ....*....|....*....|....*....|....
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVG 38
Cdd:PRK08163   7 VLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 5-45 1.86e-03

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 40.55  E-value: 1.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDR--VGGRtytIR 45
Cdd:PRK08243   5 VAIIGAGPAGLLLGQLLHLAGIDSVVLERRSReyVEGR---IR 44
PRK06370 PRK06370
FAD-containing oxidoreductase;
3-39 2.93e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.19  E-value: 2.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
2Z5Y_A         3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGG 39
Cdd:PRK06370   6 YDAIVIGAGQAGPPLAARAAGLGMKVALIE-RGLLGG 41
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 5-59 3.04e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 38.26  E-value: 3.04e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2Z5Y_A           5 VVVIGGGISGLSAAKLLTEYGVSVLVL--------EARDRVGGRTYTIR------NEHVDYVD--VGGAYV 59
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTLYsqaellEEAVKEADlvIGAVLI 93
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
10-40 3.30e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.57  E-value: 3.30e-03
                        10        20        30
                ....*....|....*....|....*....|.
2Z5Y_A       10 GGISGLSAAKLLTEYGVSVLVLEARDRVGGR 40
Cdd:COG0644   1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDK 31
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 4-42 3.56e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 39.88  E-value: 3.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVL--EARDRVGGRTY 42
Cdd:PRK12834   6 DVIVVGAGLAGLVAAAELADAGKRVLLLdqENEANLGGQAF 46
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 1-41 3.72e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 39.74  E-value: 3.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
2Z5Y_A         1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 41
Cdd:PRK12844   5 ETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGST 45
PRK12416 PRK12416
protoporphyrinogen oxidase; Provisional
 2-76 4.06e-03

protoporphyrinogen oxidase; Provisional


Pssm-ID: 183516  Cd Length: 463  Bit Score: 39.81  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A         2 MFDVVVIGGGISGLSA----AKLLTEYGV--SVLVLEARDRVGGRTYTIRNEhvDYVDVGGA--YVGPTQNrILRLSKEL 73
Cdd:PRK12416   1 MKTVVVIGGGITGLSTmfylEKLKKDYNIdlNLILVEKEEYLGGKIHSVEEK--DFIMESGAdsIVARNEH-VMPLVKDL 77


                 ...
2Z5Y_A        74 GIE 76
Cdd:PRK12416  78 NLE 80
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 4-35 4.06e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 39.31  E-value: 4.06e-03
                        10        20        30
                ....*....|....*....|....*....|..
2Z5Y_A        4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARD 35
Cdd:cd01620 164 KVLIIGAGVVGLGAAKIAKKLGANVLVYDIKE 195
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 5-39 4.31e-03

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 39.76  E-value: 4.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
2Z5Y_A          5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGG 39
Cdd:PTZ00306  412 VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 4-41 4.31e-03

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 39.68  E-value: 4.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 41
Cdd:PRK12842  11 DVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTT 48
PRK07364 PRK07364
FAD-dependent hydroxylase;
3-34 4.68e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 39.23  E-value: 4.68e-03
                         10        20        30
                 ....*....|....*....|....*....|..
2Z5Y_A         3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEAR 34
Cdd:PRK07364  19 YDVAIVGGGIVGLTLAAALKDSGLRIALIEAQ 50
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
5-40 5.02e-03

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 39.35  E-value: 5.02e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
2Z5Y_A        5 VVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGR 40
Cdd:COG1251 145 VVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPR 180
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 4-31 5.37e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 39.18  E-value: 5.37e-03
                         10        20
                 ....*....|....*....|....*...
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVL 31
Cdd:PRK07804  18 DVVVVGSGVAGLTAALAARRAGRRVLVV 45
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 3-33 6.11e-03

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 39.23  E-value: 6.11e-03
                          10        20        30
                  ....*....|....*....|....*....|.
2Z5Y_A          3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEA 33
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAA 31
PRK09126 PRK09126
FAD-dependent hydroxylase;
1-32 6.61e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 38.77  E-value: 6.61e-03
                         10        20        30
                 ....*....|....*....|....*....|..
2Z5Y_A         1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLE 32
Cdd:PRK09126   2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIE 33
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 3-45 6.93e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 38.66  E-value: 6.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
2Z5Y_A          3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLE------ARDRVGGRTYTIR 45
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLLEqfdlphSRGSSHGQSRIIR 49
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 3-33 7.38e-03

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 39.06  E-value: 7.38e-03
                          10        20        30
                  ....*....|....*....|....*....|.
2Z5Y_A          3 FDVVVIGGGISGLSAAKLLTEYGVSVLVLEA 33
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDF 33
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
213-287 7.78e-03

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 38.65  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z5Y_A       213 GQVSERIMDLL---GDQVKLNHPVTHVDQSSDNIIIETlNHEHYECKYVIN-------------AIPPtlTAKI-HFRPE 275
Cdd:PRK11728 149 RAVAEAMAELIqarGGEIRLGAEVTALDEHANGVVVRT-TQGEYEARTLINcaglmsdrlakmaGLEP--DFRIvPFRGE 225

                         90
                 ....*....|....*
2Z5Y_A       276 ---LPAERNQLIQRL 287
Cdd:PRK11728 226 yyrLAPEKNQLVNHL 240
PRK06753 PRK06753
hypothetical protein; Provisional
 5-34 7.82e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 38.52  E-value: 7.82e-03
                         10        20        30
                 ....*....|....*....|....*....|
2Z5Y_A         5 VVVIGGGISGLSAAKLLTEYGVSVLVLEAR 34
Cdd:PRK06753   3 IAIIGAGIGGLTAAALLQEQGHEVKVFEKN 32
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 2-39 8.12e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 38.59  E-value: 8.12e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
2Z5Y_A         2 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLEaRDRVGG 39
Cdd:PRK06416   4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE-KEKLGG 40
PRK07121 PRK07121
FAD-binding protein;
1-41 8.25e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 38.71  E-value: 8.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
2Z5Y_A         1 HMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRT 41
Cdd:PRK07121  19 DEADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGAT 59
PRK07538 PRK07538
hypothetical protein; Provisional
 4-33 8.64e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 38.72  E-value: 8.64e-03
                         10        20        30
                 ....*....|....*....|....*....|
2Z5Y_A         4 DVVVIGGGISGLSAAKLLTEYGVSVLVLEA 33
Cdd:PRK07538   2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEA 31
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 2-49 8.80e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 38.74  E-value: 8.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
2Z5Y_A         2 MFDVVVIGGGISGLSAAKLLTEYGVSVLVLE------ARDRVGGRTYTIRNEHV 49
Cdd:PRK10157   5 IFDAIIVGAGLAGSVAALVLAREGAQVLVIErgnsagAKNVTGGRLYAHSLEHI 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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