|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
40-501 |
0e+00 |
|
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: 592.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 40 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAhgKDFASRGIEMSEVRLN 119
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEA--RHAAEFGISAGAPSVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 120 LDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATkadgGTQVIDTKNILIATGSEVTPFPGITIDEDT 199
Cdd:COG1249 79 WAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT----GGETLTADHIVIATGSRPRVPPIPGLDEVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 200 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVT 279
Cdd:COG1249 155 VLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 280 GATKKSDGkidVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAG 359
Cdd:COG1249 234 SVEKTGDG---VTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 360 PMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGM 438
Cdd:COG1249 311 PQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91199540 439 VKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 501
Cdd:COG1249 391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
43-509 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 573.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET----LGGTCLNVGCIPSKALLNNSHYYHMAhGKDFASRGIEMSEV 116
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKgkpaLGGTCLNVGCIPSKALLASSEEFENA-GHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 117 RLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQV-TATKADG-GTQVIDTKNILIATGSEVTPFPGIT 194
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKTDAgYEIKVTGeDETVITAKHVIIATGSEPRHLPGVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 195 IDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGF 270
Cdd:PRK06327 165 FDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEalpaFLAAA-----DEQVAKEAAKAFTKQGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 271 KFKLNTKVtGATKKSDGKIDVSIEAASGgKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNI 350
Cdd:PRK06327 240 DIHLGVKI-GEIKTGGKGVSVAYTDADG-EAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 351 YAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAK 430
Cdd:PRK06327 318 YAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRAL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91199540 431 TNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSINF 509
Cdd:PRK06327 398 AMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD-KRPLHF 475
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
43-508 |
0e+00 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 568.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGKDFasrGIEMSEVRLNLD 121
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDeIKHAKDL---GIEVENVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 122 KMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKaDGGTQVIDTKNILIATGSEVTPFPG-ITIDEDTI 200
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTG-ENGEETLEAKNIIIATGSRPRSLPGpFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 201 VSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTG 280
Cdd:TIGR01350 158 ITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 281 ATKKSDGkidVSIEAaSGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP 360
Cdd:TIGR01350 237 VEKNDDQ---VTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 361 MLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMV 439
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91199540 440 KILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAsFGKSIN 508
Cdd:TIGR01350 393 KIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAA-LGKPIH 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
38-509 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 545.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGKDFasrGIEMSEV 116
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADeARHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 117 RLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGtQVIDTKNILIATGSEVTPFPGITID 196
Cdd:PRK06416 77 GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGE-QTYTAKNIILATGSRPRELPGIEID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 197 EDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNT 276
Cdd:PRK06416 156 GRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP-GEDKEISKLAERALKKRGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 277 KVTGATKKSDGkIDVSIEAasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDpRGRIPVNTRFQTKIPNIYAIGDV 356
Cdd:PRK06416 235 KAKKVEQTDDG-VTVTLED--GGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 357 VAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 436
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91199540 437 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSINF 509
Cdd:PRK06416 391 GFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAA-GKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
40-503 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 540.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 40 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAhgKDFASRGIEMSEVRLN 119
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEA--KHAEEFGIHADGPKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 120 LDKMMEQKSTAVKALTGGIAH-LFKQNKVVHVNGYGKITGKNQVTAtkadgGTQVIDTKNILIATGSEVTPFPGIT-IDE 197
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGVWlILG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 198 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQgFKFKLNTK 277
Cdd:PRK06292 154 DRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 278 VTGATKKSDGKIDVSIEaasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 357
Cdd:PRK06292 232 VTSVEKSGDEKVEELEK---GGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 358 AGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 436
Cdd:PRK06292 309 GKPPLLHEAADEGRIAAENAAGDvAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKND 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91199540 437 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASF 503
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
38-501 |
1.39e-106 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 325.57 E-value: 1.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKAL---------LNNSHYYHMAHGKdfas 108
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALreavlrligFNQNPLYSSYRVK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 109 RGIEMSEVRLNLDKMMeQKSTAVkaltggIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEvt 188
Cdd:PRK05249 78 LRITFADLLARADHVI-NKQVEV------RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 189 PF--PGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE-------FLghvggvgiDMEISK 259
Cdd:PRK05249 149 PYrpPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 260 NFQRILQKQGFKFKLNTKVTGATKKSDGKIdvsIEAASGGKaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPV 339
Cdd:PRK05249 221 ALSYHLRDSGVTIRHNEEVEKVEGGDDGVI---VHLKSGKK---IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 340 NTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVG 419
Cdd:PRK05249 295 NENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 420 KFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANL 499
Cdd:PRK05249 375 RARFKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAAL 454
|
..
gi 91199540 500 AA 501
Cdd:PRK05249 455 DG 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
43-507 |
2.89e-105 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 322.45 E-value: 2.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGkdfASRGIEMSEVRLNLDK 122
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERG-PLGGTCVNVGCVPSKMLLRAAEVAHYARK---PPFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 123 MMEQKSTAVKAL-TGGIAHLFKQNKVVHVNGYGKITGKNQVtatKADGGTQVIDTKNILIATGSE--VTPFPGItiDEDT 199
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTV---KVDLGREVRGAKRFLIATGARpaIPPIPGL--KEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 200 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgIDMEISKNFQRILQKQGFKFKLN 275
Cdd:TIGR02053 153 YLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLPR-----EEPEISAAVEEALAEEGIEVVTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 276 TKVTGATKKSDGKIDVSIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:TIGR02053 228 AQVKAVSVRGGGKIITVEKPGGQGEVEA---DELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 356 VVAGPMLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNAD 434
Cdd:TIGR02053 305 VTGGLQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRD 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91199540 435 TDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSI 507
Cdd:TIGR02053 385 TRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLA--AQTFYRDV 455
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
43-503 |
5.84e-103 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 316.37 E-value: 5.84e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMA-HGKDFasrGIEMS-EVRLNL 120
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSVGgPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 121 DKMMEQKSTAVKALTGGIAHLFKQNKVVHV-NGYGKITGKNQVTAtkadgGTQVIDTKNILIATGSE--VTPFPGItiDE 197
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGLEGVDVfRGHARFESPNTVRV-----GGETLRAKRIFINTGARaaIPPIPGL--DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 198 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTK 277
Cdd:PRK06370 156 VGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 278 VTGATKKSDGKIdvsIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 357
Cdd:PRK06370 235 CIRVERDGDGIA---VGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 358 AGPMLAHKAEDEGIICVEGMA-GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 436
Cdd:PRK06370 312 GRGAFTHTAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQ 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91199540 437 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFReaNLAASF 503
Cdd:PRK06370 392 GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP--TLAQAL 456
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
41-494 |
5.03e-81 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 259.32 E-value: 5.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 41 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMAH--GKDFasrGIEMSEVRL 118
Cdd:PRK06116 4 DYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHdyAPGY---GFDVTENKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 119 NLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTAtkadGGTQvIDTKNILIATGSEVTP--FPGItid 196
Cdd:PRK06116 80 DWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEV----NGER-YTADHILIATGGRPSIpdIPGA--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 197 EDTIvSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGhvggvGIDMEISKNFQRILQKQGFKF 272
Cdd:PRK06116 152 EYGI-TSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLR-----GFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 273 KLNTKVTGATKKSDGKIDVSIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYA 352
Cdd:PRK06116 226 HTNAVPKAVEKNADGSLTLTLE-----DGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 353 IGDVVAGPMLAHKAEDEGIICVEGMAGG--AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEY--KVGKFPFAANSR 428
Cdd:PRK06116 301 VGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFTPMYT 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91199540 429 AKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PRK06116 381 ALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
43-502 |
6.77e-74 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 246.36 E-value: 6.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNE-TLGGTCLNVGCIPSKALL----------NNSHYYHMA-------HGK 104
Cdd:PTZ00153 118 DVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYTYGiytnafkNGK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 105 DFASRGIEM--SEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNK-------VVHVNGYGKITGKNQVTATKADGGTQVid 175
Cdd:PTZ00153 198 NDPVERNQLvaDTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHIVDKNTIKSEKSGKEFKV-- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 176 tKNILIATGSevTPF--PGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGI 253
Cdd:PTZ00153 276 -KNIIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP-LL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 254 DMEISKNFQRILQK-QGFKFKLNTKVT-------------GATKKSDGKIDVSIEAASGGKAevITCDVLLVCIGRRPFT 319
Cdd:PTZ00153 352 DADVAKYFERVFLKsKPVRVHLNTLIEyvragkgnqpviiGHSERQTGESDGPKKNMNDIKE--TYVDSCLVATGRKPNT 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 320 KNLGLEELGIELDpRGRIPVNTRFQTK------IPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH---------- 383
Cdd:PTZ00153 430 NNLGLDKLKIQMK-RGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwa 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 384 ---IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFP--FAANSRA----------------------KTNADTD 436
Cdd:PTZ00153 509 skpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgkyNTVDNTE 588
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91199540 437 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAS 502
Cdd:PTZ00153 589 GMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIA 654
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
43-370 |
3.21e-71 |
|
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: 229.13 E-value: 3.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEknetLGGTCLNVGCIPSKALLNnshyyhmahgkdfasrGIEMSEVRLNLDK 122
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLG----------------AAEAPEIASLWAD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 123 MMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVtatkaDGGTQVIDTKNILIATGSE--VTPFPGIT---IDE 197
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARprLPPIPGVElnvGFL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 198 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTK 277
Cdd:pfam07992 137 VRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 278 VTGATKKSDGKidvsieAASGGKAEVITCDVLLVCIGRRPftKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDV- 356
Cdd:pfam07992 216 VKEIIGDGDGV------EVILKDGTEIDADLVVVAIGRRP--NTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
gi 91199540 357 VAGPMLAHKAEDEG 370
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
44-508 |
3.78e-70 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 233.89 E-value: 3.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASrGIEMSEVRLNLDKM 123
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERG-TIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 124 MEQKSTAVKALTG----GIAHLFKQNKVVHvnGYGKITGKNQVTATKADGGTQVIDTKNILIATGSE--VTPFPGITidE 197
Cdd:PRK13748 179 LAQQQARVDELRHakyeGILDGNPAITVLH--GEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASpaVPPIPGLK--E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 198 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgiDMEISKNFQRILQKQGFKFK 273
Cdd:PRK13748 255 TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE------DPAIGEAVTAAFRAEGIEVL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 274 LNTKVTgATKKSDGKIDVSIEAASggkaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAI 353
Cdd:PRK13748 329 EHTQAS-QVAHVDGEFVLTTGHGE------LRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 354 GDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 433
Cdd:PRK13748 402 GDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91199540 434 DTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSIN 508
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLA--AQTFNKDVK 554
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
46-496 |
2.94e-68 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 225.81 E-value: 2.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 46 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALLNNSHYYHmahgkDFASrgiemsevrlnldkMM 124
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ-----DFST--------------AM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 125 EQKSTAVKALTGGIAH-LFKQNKVVHVNGYGKITGKNQVTATKADgGTQVIDTKNILIATGSEVT--PFPGITIDEDtIV 201
Cdd:NF040477 69 QRKSSVVGFLRDKNYHnLADLDNVDVINGRAEFIDNHTLRVFQAD-GEQELRGEKIFINTGAQSVlpPIPGLTTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 202 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGiDMEISKNFQRILQKQGFKFKLNTKVTGA 281
Cdd:NF040477 147 DSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPRE-DRDIAQAIATILQDQGVELILNAQVQRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 282 TKKSDGkidVSIEAASGgkaeVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 361
Cdd:NF040477 226 SSHEGE---VQLETAEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 362 LAHKAEDEGIICVEGMAG-GAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMV 439
Cdd:NF040477 299 FTYISLDDFRIVRDSLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 91199540 440 KILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 496
Cdd:NF040477 379 KAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
43-494 |
2.74e-67 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 223.09 E-value: 2.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALlnnshyyhmahgkdfasrgIEMSEVRLNLD 121
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTL-------------------LVAAEKNLSFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 122 KMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGkNQVTATKADGGTQVIDTKNILIATG--SEVTPFPGITiDEDT 199
Cdd:PRK07251 66 QVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVS-NKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLA-DSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 200 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGFKFKLN 275
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDaastILPRE-----EPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 276 TKVTgATKKSDGKIDVSIEAasggkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK07251 219 AHTT-EVKNDGDQVLVVTED------ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 356 VVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 433
Cdd:PRK07251 292 VNGGPQFTYISLDDFRIVFGYLTGDGsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91199540 434 DTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PRK07251 372 DLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
43-494 |
8.97e-66 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 219.33 E-value: 8.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMAHgkDFASRGIEMS-EVRLNLD 121
Cdd:TIGR01421 4 DYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDLAERMH--DAADYGFYQNdENTFNWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 122 KMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADggtqvIDTKNILIATGSEVTPFPGITIDEDTIv 201
Cdd:TIGR01421 81 ELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPENIPGAELGT- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 202 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADvTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGA 281
Cdd:TIGR01421 155 DSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 282 TKKSDGKIDVSIEAASggkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 361
Cdd:TIGR01421 234 EKTVEGKLVIHFEDGK----SIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 362 LAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQ-LKEEGIE-YKVGKFPFAANSRAKTNADTDG 437
Cdd:TIGR01421 310 LTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEKQKC 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 91199540 438 MVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:TIGR01421 390 RMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
41-507 |
1.52e-64 |
|
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: 217.03 E-value: 1.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 41 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET--------LGGTCLNVGCIPSKALLNNSHY-YHMAHGKDFASRGI 111
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKKLMHQAALLgQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 112 EmsEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGsEVTPFP 191
Cdd:TIGR01438 82 E--TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATG-ERPRYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 192 GITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGV---GIDMEISKNFQRILQKQ 268
Cdd:TIGR01438 159 GIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-----VRSIllrGFDQDCANKVGEHMEEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 269 GFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPR-GRIPVNTRFQTKI 347
Cdd:TIGR01438 234 GVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEY---DTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 348 PNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQ----LKEEGIEYKVGKF 421
Cdd:TIGR01438 311 PYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHSYF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 422 -PFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLA 500
Cdd:TIGR01438 391 wPLEWTIPSRDNHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVT 470
|
....*..
gi 91199540 501 ASFGKSI 507
Cdd:TIGR01438 471 KRSGQDI 477
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
41-494 |
1.19e-62 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 212.37 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 41 DADVTVIGSGPGGYVAAIKAAQLG---------FKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGI 111
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGakvgicelpFHPISSESIGGVGGTCVIRGCVPKKILVYGATF--GGEFEDAKNYGW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 112 EMSE-VRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPf 190
Cdd:PLN02507 103 EINEkVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQR- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 191 PGITIDEDTIVSSTgALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeFLGHVGGVGIDMEISKNFQRILQKQGF 270
Cdd:PLN02507 182 PNIPGKELAITSDE-ALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRAVVARNLEGRGI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 271 KFKLNTKVTGATKKSDGkIDVSIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNI 350
Cdd:PLN02507 260 NLHPRTNLTQLTKTEGG-IKVITD-----HGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 351 YAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG---IEYKVGKFPFAAN 426
Cdd:PLN02507 334 WAIGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSSFNPMKN 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199540 427 SRAKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PLN02507 414 TISGRQEKT--VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
44-497 |
6.12e-58 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 198.93 E-value: 6.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEkNETLGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGIE---MSEVRLNL 120
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE-RDGLGGAAVLTDCVPSKTLIATAEV--RTELRRAAELGIRfidDGEARVDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 121 DKMMEQkstaVKALT----GGIAHLFKQNKVVHVNGYGKIT----GKNQVTATKADGGTQVIDTKNILIATGSevTP--F 190
Cdd:PRK07845 81 PAVNAR----VKALAaaqsADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGA--SPriL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 191 PGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGF 270
Cdd:PRK07845 155 PTAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLP-GEDADAAEVLEEVFARRGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 271 KFKLNTKVTGATKKSDGkidVSIEAASGGKAEVITCdvlLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNI 350
Cdd:PRK07845 234 TVLKRSRAESVERTGDG---VVVTLTDGRTVEGSHA---LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 351 YAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRA 429
Cdd:PRK07845 308 YAAGDCTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199540 430 KTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREA 497
Cdd:PRK07845 388 KMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
46-496 |
2.45e-56 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 194.46 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 46 VIGSGPGGYVAAIKAAQLGFKTVCIEK-NETLGGTCLNVGCIPSKALLNNSHyyhmAHGkDFAsrgiemsevrlnldKMM 124
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVHDAQ----QHT-DFV--------------RAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 125 EQKSTAVKALTGGIAH-LFKQNKVVHVNGYGKITGKNQVTATKADGgTQVIDTKNILIATGSE--VTPFPGITIDEDtIV 201
Cdd:PRK08010 69 QRKNEVVNFLRNKNFHnLADMPNIDVIDGQAEFINNHSLRVHRPEG-NLEIHGEKIFINTGAQtvVPPIPGITTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 202 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGFKFKLNTK 277
Cdd:PRK08010 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDIILNAH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 278 VTGATKKsDGKIDVSIEAASggkaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 357
Cdd:PRK08010 222 VERISHH-ENQVQVHSEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 358 AGPMLAHKAEDEGIICVEGMAGGAVHI--DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADT 435
Cdd:PRK08010 295 GGLQFTYISLDDYRIVRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91199540 436 DGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 496
Cdd:PRK08010 375 RGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
43-503 |
1.74e-54 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 189.39 E-value: 1.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAHGKDFASR-GIEMSEVRLNLD 121
Cdd:PRK07846 3 DLIIIGTGSGN---SILDERFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAADVARTIREAARlGVDAELDGVRWP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 122 KMMEQKSTAVKAL-TGGIAHLFKQNKVVHV-NGYGKITGknQVTATKADGGtqVIDTKNILIATGSEVTPFPGITIDEDT 199
Cdd:PRK07846 77 DIVSRVFGRIDPIaAGGEEYRGRDTPNIDVyRGHARFIG--PKTLRTGDGE--EITADQVVIAAGSRPVIPPVIADSGVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 200 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgIDMEISKNFQRILQKQgFKFKLN 275
Cdd:PRK07846 153 YHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNrsgrLLRH-----LDDDISERFTELASKR-WDVRLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 276 TKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK07846 227 RNVVGVSQDGSG---VTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 356 VVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 433
Cdd:PRK07846 301 VSSPYQLKHVANHEARVVQHNLLHPDdlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAME 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91199540 434 DTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLAASF 503
Cdd:PRK07846 381 DTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
43-492 |
7.84e-54 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 188.64 E-value: 7.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET---------LGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGIEM 113
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQY--MDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 114 --SEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNK-VVHVNGYGKITGKNQVTATK-ADGGTQV---IDTKNILIATGS- 185
Cdd:TIGR01423 83 drSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsADPKSAVkerLQAEHILLATGSw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 186 -EVTPFPGItideDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSV---WQRLGADVTaVEFLGHVGGVGIDMEISKNF 261
Cdd:TIGR01423 163 pQMLGIPGI----EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT-LCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 262 QRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEaaSGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNT 341
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNADGSKHVTFE--SGKTLDV---DVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 342 RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQL--KEEGIEYKV 418
Cdd:TIGR01423 313 FSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKVAVYE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91199540 419 GKF-PFAANSRAKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSE 492
Cdd:TIGR01423 393 SSFtPLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
389-497 |
9.22e-54 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 176.59 E-value: 9.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 389 VPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAA 468
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 91199540 469 LALEYGASCEDIARVCHAHPTLSEAFREA 497
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
41-506 |
6.74e-50 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 178.48 E-value: 6.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 41 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET------LGGTCLNVGCIPSKALlnnsHYY-HMAH--GKDFASR 109
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLM----HYAaNIGSifHHDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 110 GIEMSEVrLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVtATKADGGTQVIDTKNILIATGSEvtp 189
Cdd:PTZ00052 81 GWKTSSS-FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGR--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 190 fPGITID----EDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT-AVEflgHVGGVGIDMEISKNFQRI 264
Cdd:PTZ00052 156 -PSIPEDvpgaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTvAVR---SIPLRGFDRQCSEKVVEY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 265 LQKQGFKFKlNTKVTGATKKSDGKIDVSIeaaSGGKAEVItcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIpVNTRFQ 344
Cdd:PTZ00052 232 MKEQGTLFL-EGVVPINIEKMDDKIKVLF---SDGTTELF--DTVLYATGRKPDIKGLNLNAIGVHVNKSNKI-IAPNDC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 345 TKIPNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFP 422
Cdd:PTZ00052 305 TNIPNIFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 423 FAANS------------RAKTNA-DTD----GMVKILGQKSTD-RVLGAHILGPGAGEMVNEAALALEYGASCEDIARVC 484
Cdd:PTZ00052 385 QEFNTleiaavhrekheRARKDEyDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMI 464
|
490 500
....*....|....*....|..
gi 91199540 485 HAHPTLSEAFREANLAASFGKS 506
Cdd:PTZ00052 465 GIHPTDAEVFMNLSVTRRSGES 486
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
41-494 |
9.29e-49 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 176.61 E-value: 9.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 41 DADVTVIGSGPGG---------YVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHmahgkDF-ASRG 110
Cdd:PLN02546 79 DFDLFTIGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSH-----EFeESRG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 111 IEM---SEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTAtkaDGgtQVIDTKNILIATGSEv 187
Cdd:PLN02546 154 FGWkyeTEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG--KLYTARNILIAVGGR- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 188 tPF----PGItideDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVtaveflgHV----GGV--GIDMEI 257
Cdd:PLN02546 228 -PFipdiPGI----EHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDV-------HVfirqKKVlrGFDEEV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 258 SKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAAS-GGKAEVitcdvlLVCIGRRPFTKNLGLEELGIELDPRGR 336
Cdd:PLN02546 296 RDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTvEGFSHV------MFATGRKPNTKNLGLEEVGVKMDKNGA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 337 IPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIE 415
Cdd:PLN02546 370 IEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 416 YKVgkfpFAANSRAkTNADTDGM-----VKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTL 490
Cdd:PLN02546 450 VDV----FTANFRP-LKATLSGLpdrvfMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTA 524
|
....
gi 91199540 491 SEAF 494
Cdd:PLN02546 525 AEEF 528
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
43-500 |
1.61e-47 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 170.71 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAHGKDFASR-GIEMSEVRLNLD 121
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAAEVAQSIGESARlGIDAEIDSVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 122 KMMEQK-STAVKALTGGIAHLFKQNKVVHVNGY-GKITGKNQVTATKADGGTqvIDTKNILIATGSEVTPFPGITIDEDT 199
Cdd:TIGR03452 78 DIVSRVfGDRIDPIAAGGEDYRRGDETPNIDVYdGHARFVGPRTLRTGDGEE--ITGDQIVIAAGSRPYIPPAIADSGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 200 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGHvggvgIDMEISKNFQRILQKQgFKFKLN 275
Cdd:TIGR03452 156 YHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVnrstKLLRH-----LDEDISDRFTEIAKKK-WDIRLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 276 TKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:TIGR03452 230 RNVTAVEQDGDG---VTLTLDDG---STVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWALGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 356 VVAGPMLAHKAEDEGIICVEGMA--GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG--IEYKVGKFPFAANSRAKt 431
Cdd:TIGR03452 304 VSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYGWAM- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 432 nADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLA 500
Cdd:TIGR03452 383 -EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
21-494 |
1.52e-44 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 164.79 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 21 SHGLQGlSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHM 100
Cdd:PTZ00058 29 YHNLEA-SSAPTHLKKKPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 101 AHgkDFASRGIEMSEVrLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATK-------------- 166
Cdd:PTZ00058 107 LE--NSRHYGFDTQFS-FNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesddd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 167 ----------ADGGTQVIDTKNILIATGSEvTPFPGITIDEDTIvSSTGALSLKKvPEKMVVIGAGVIGVELGSVWQRLG 236
Cdd:PTZ00058 184 evtivsagvsQLDDGQVIEGKNILIAVGNK-PIFPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 237 ADvTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDVSIEAASGGKAEVITCdvLLVCIGRR 316
Cdd:PTZ00058 261 AE-SYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEK--VKEKNLTIYLSDGRKYEHFDY--VIYCVGRS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 317 PFTKNLGLEELGIeLDPRGRIPVNTRFQTKIPNIYAIGDVVAGP---------MLAHKAEDEGIICVEGMAGGAVH---- 383
Cdd:PTZ00058 336 PNTEDLNLKALNI-KTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnLLKLYNEEPYLKKKENTSGESYYnvql 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 384 ----------------------IDYNCVPSVIYTHPEVAWVGKSEEQL-----KEEGIEYK-------VGKFPFAANSRA 429
Cdd:PTZ00058 415 tpvainagrlladrlfgpfsrtTNYKLIPSVIFSHPPIGTIGLSEQEAidiygKENVKIYEsrftnlfFSVYDMDPAQKE 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91199540 430 KTnadtdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PTZ00058 495 KT------YLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
159-393 |
4.89e-30 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 119.53 E-value: 4.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 159 KNQVTATKADGGTQVIDTKN--------ILIATGSE--VTPFPGITIDE-DTIVSSTGALSLKKV-----PEKMVVIGAG 222
Cdd:COG0446 54 RTGTEVTAIDPEAKTVTLRDgetlsydkLVLATGARprPPPIPGLDLPGvFTLRTLDDADALREAlkefkGKRAVVIGGG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 223 VIGVELGSVWQRLGADVTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKLNTKVTGAtkksDGKIDVSIEAASGgkaE 302
Cdd:COG0446 134 PIGLELAEALRKRGLKVTLVERAPRLLGV-LDPEMAALLEEELREHGVELRLGETVVAI----DGDDKVAVTLTDG---E 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 303 VITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV----------AGPMLAHKAEDEGI 371
Cdd:COG0446 206 EIPADLVVVAPGVRP---NTELaKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtgktVYIPLASAANKQGR 282
|
250 260
....*....|....*....|..
gi 91199540 372 ICVEGMAGGAvhIDYNCVPSVI 393
Cdd:COG0446 283 VAAENILGGP--APFPGLGTFI 302
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
43-361 |
1.13e-26 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 109.82 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIpskallNNshYYHMAHGKdfasRGIEMsevrlnLDK 122
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEI------EN--YPGFPEGI----SGPEL------AER 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 123 MMEQ-KSTAVKALTGGIAHLFKQNKVVHVngygkitgknqvtatKADGGTqVIDTKNILIATGSEVT--PFPGITIDEDT 199
Cdd:COG0492 63 LREQaERFGAEILLEEVTSVDKDDGPFRV---------------TTDDGT-EYEAKAVIIATGAGPRklGLPGEEEFEGR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 200 IVSSTGALSLKKVP-EKMVVIGAGVIGVELGSVWQRLGADVTAVeflgHVGGvgiDMEISKNFQ-RILQKQGFKFKLNTK 277
Cdd:COG0492 127 GVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLI----HRRD---ELRASKILVeRLRANPKIEVLWNTE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 278 VTGAtkKSDGKID-VSIEAASGGKAEVITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:COG0492 200 VTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKP---NTELlKGLGLELDEDGYIVVDEDMETSVPGVFAAGD 274
|
....*.
gi 91199540 356 VVAGPM 361
Cdd:COG0492 275 VRDYKY 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
180-382 |
8.83e-23 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 100.22 E-value: 8.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 180 LIATGSE--VTPFPGI---------TIDE-DTIVSSTGAlslkkvPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGH 247
Cdd:COG1251 103 VLATGSRprVPPIPGAdlpgvftlrTLDDaDALRAALAP------GKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 248 VGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKidvSIEAASGgkaEVITCDVLLVCIGRRPftkNLGL-EE 326
Cdd:COG1251 177 LLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT---GVRLADG---EELPADLVVVAIGVRP---NTELaRA 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91199540 327 LGIELDpRGrIPVNTRFQTKIPNIYAIGDVVA-------GPMLAH--KAEDEGIICVEGMAGGAV 382
Cdd:COG1251 248 AGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLELvaPAYEQARVAAANLAGGPA 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
155-488 |
4.59e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 83.55 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 155 KITGKNQVTatkadgGTQVIDTKNIL-IATG--SEVTPFPGITIDE-DTIVSSTGALSLKKVPEK-----MVVIGAGVIG 225
Cdd:PRK09564 88 TITVKNLKT------GSIFNDTYDKLmIATGarPIIPPIKNINLENvYTLKSMEDGLALKELLKDeeiknIVIIGAGFIG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 226 VELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVtgatKKSDGKIDVSIEAASGGKAEVit 305
Cdd:PRK09564 162 LEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFV----KSLIGEDKVEGVVTDKGEYEA-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 306 cDVLLVCIGRRPFTKnlGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD-------VVAGPM---LAHKAEDEGIICVE 375
Cdd:PRK09564 236 -DVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 376 GMAGGAVH----IDYNCVPSVIYthpEVAWVGKSEEQLKEEGIEYKVgKFPFAANSRAKTNADTDGMVKILGQKSTDRVL 451
Cdd:PRK09564 313 NLAGRHVSfkgtLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVIL 388
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 91199540 452 GAHILGP-GAGEMVNEAALALEYGASCEDIARV--CHAHP 488
Cdd:PRK09564 389 GGQIIGKkGAVLRIDALAVAIYAKLTTQELGMMdfCYAPP 428
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
42-375 |
1.51e-16 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 81.33 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 42 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIekneTLggtclnvgcIpSKallNNSHYY-HMAHGkdFASRGIEMSEVRLNL 120
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDAEV----TL---------I-DP---NPYHLFqPLLPE--VAAGTLSPDDIAIPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 121 DKMMEQKSTAvkaltggiahlFKQNKVVHVNgygkiTGKNQVTAtkADGGTQVIDTknILIATGSEVTPF--PGI----- 193
Cdd:COG1252 63 RELLRRAGVR-----------FIQGEVTGID-----PEARTVTL--ADGRTLSYDY--LVIATGSVTNFFgiPGLaehal 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 194 ---TIDE-----DTIVSstgALSLKKVPEKM--VVIGAGVIGVEL-GSVWQRLG------------ADVTAVEFLGHVGG 250
Cdd:COG1252 123 plkTLEDalalrERLLA---AFERAERRRLLtiVVVGGGPTGVELaGELAELLRkllrypgidpdkVRITLVEAGPRILP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 251 vGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSdgkidvsIEAASGgkaEVITCDVLLVCIGRR--PFTKNLGLEelg 328
Cdd:COG1252 200 -GLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADG-------VTLEDG---EEIPADTVIWAAGVKapPLLADLGLP--- 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 91199540 329 ieLDPRGRIPVNTRFQTK-IPNIYAIGDVVAG--------PMLAHKAEDEGIICVE 375
Cdd:COG1252 266 --TDRRGRVLVDPTLQVPgHPNVFAIGDCAAVpdpdgkpvPKTAQAAVQQAKVLAK 319
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
215-288 |
2.85e-16 |
|
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: 73.39 E-value: 2.85e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91199540 215 KMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGK 288
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
170-355 |
8.96e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 75.72 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 170 GTQVIDTKNILIATGSE--VTPFPGitiDEDTIV--------SSTGALSLKKvpeKMVVIGAGVIGVELGSVWQRLGADV 239
Cdd:PRK04965 94 QGNQWQYDKLVLATGASafVPPIPG---RELMLTlnsqqeyrAAETQLRDAQ---RVLVVGGGLIGTELAMDLCRAGKAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 240 TAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPft 319
Cdd:PRK04965 168 TLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG---IRATLDSG---RSIEVDAVIAAAGLRP-- 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 91199540 320 kNLGL-EELGIELDpRGrIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK04965 240 -NTALaRRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
196-357 |
1.25e-14 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 75.97 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 196 DEDTIVSSTGALSLKKVPekmvVIGAGVIGVE-LGSVWQRlGADVTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKL 274
Cdd:PRK13512 135 DTDAIDQFIKANQVDKAL----VVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 275 NTKVTgatkksdgKIDVSIEAASGGKAEviTCDVLLVCIGRRPFTKNLglEELGIELDPRGRIPVNTRFQTKIPNIYAIG 354
Cdd:PRK13512 209 NEEID--------AINGNEVTFKSGKVE--HYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIG 276
|
...
gi 91199540 355 DVV 357
Cdd:PRK13512 277 DII 279
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
155-358 |
8.86e-12 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 67.55 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 155 KITGKNQVTATKAdGGTQVIDTknILIATGSE--VTPFPGI---------TIDE-DTIvsstgaLSLKKVPEKMVVIGAG 222
Cdd:TIGR02374 79 QIDTDQKQVITDA-GRTLSYDK--LILATGSYpfILPIPGAdkkgvyvfrTIEDlDAI------MAMAQRFKKAAVIGGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 223 VIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDvSIEAASGgkaE 302
Cdd:TIGR02374 150 LLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG--ATKAD-RIRFKDG---S 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 91199540 303 VITCDVLLVCIGRRPFTknlgleELGIE--LDPRGRIPVNTRFQTKIPNIYAIGDVVA 358
Cdd:TIGR02374 224 SLEADLIVMAAGIRPND------ELAVSagIKVNRGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
298-370 |
8.99e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 66.55 E-value: 8.99e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91199540 298 GGKAEVITCDVLLVCIGRRPfTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEG 370
Cdd:PRK12770 267 PGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
123-356 |
2.42e-11 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 65.33 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 123 MMEQKSTAVKALTGgiAHLFKQNKV-VHVNGYGKITGKNQVTATKADGGTQVIDtkNILIATGSEVTPFPGI-TIDED-- 198
Cdd:PRK09754 51 MLLEDSPQLQQVLP--ANWWQENNVhLHSGVTIKTLGRDTRELVLTNGESWHWD--QLFIATGAAARPLPLLdALGERcf 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 199 TIVSSTGALSLKKV--PEKMVVI-GAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLN 275
Cdd:PRK09754 127 TLRHAGDAARLREVlqPERSVVIvGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 276 TKVTGATKKSdgkiDVSIEAASGgkaEVITCDVLLVCIGRRpFTKNLGLEElgiELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK09754 207 NAIEHVVDGE----KVELTLQSG---ETLQADVVIYGIGIS-ANDQLAREA---NLDTANGIVIDEACRTCDPAIFAGGD 275
|
.
gi 91199540 356 V 356
Cdd:PRK09754 276 V 276
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
299-385 |
1.03e-10 |
|
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: 63.62 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 299 GKAEVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKIPNIYAIGDVVAGPMLAhkaedegiicVEGM 377
Cdd:COG0493 353 GSEFTLPADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLV----------VWAI 421
|
90
....*....|.
gi 91199540 378 AGG---AVHID 385
Cdd:COG0493 422 AEGrkaARAID 432
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
275-377 |
1.63e-07 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 53.63 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 275 NTKVTG----ATKKSDGKIDVsIEaasgGKAEVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKIPN 349
Cdd:PRK12810 359 NGKVTGvkvvRTELGEGDFEP-VE----GSEFVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNaYQTSNPK 432
|
90 100
....*....|....*....|....*...
gi 91199540 350 IYAIGDVVAGPMLAHKAEDEGIICVEGM 377
Cdd:PRK12810 433 VFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
43-78 |
5.91e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 51.77 E-value: 5.91e-07
10 20 30
....*....|....*....|....*....|....*.
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 78
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
43-79 |
7.24e-07 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 51.46 E-value: 7.24e-07
10 20 30
....*....|....*....|....*....|....*..
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
31-79 |
7.34e-07 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 51.64 E-value: 7.34e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 91199540 31 PLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK06134 2 PSAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
43-92 |
1.98e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 49.86 E-value: 1.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNetlGGTCLNVGCIPSKALL 92
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN---TDTIAELSCNPSIGGI 47
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
30-368 |
3.41e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 49.77 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 30 VPLRTY---ADQPI---DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTcLNVGcIPSKALLNNshyyhmAHG 103
Cdd:PRK13984 266 VPVEKYseiLDDEPekkNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRLPDE------ALD 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 104 KDFA---SRGIEM-SEVRLNLDKMMEQkstavkaltggiahLFKQNKVVHVNgygkiTGKNQVTATKADGGtqviDTKNI 179
Cdd:PRK13984 338 KDIAfieALGVKIhLNTRVGKDIPLEE--------------LREKHDAVFLS-----TGFTLGRSTRIPGT----DHPDV 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 180 LIAtgsevtpfpgITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLG------ADVTAVEFLGHVGGVGI 253
Cdd:PRK13984 395 IQA----------LPLLREIRDYLRGEGPKPKIPRSLVVIGGGNVAMDIARSMARLQkmeygeVNVKVTSLERTFEEMPA 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 254 DM-EISKNF------------QRIL----QKQGFKFKLNTKVTGATKKSDGKIDVSIEAasggkaeVITCDVLLVCIGRR 316
Cdd:PRK13984 465 DMeEIEEGLeegvviypgwgpMEVViendKVKGVKFKKCVEVFDEEGRFNPKFDESDQI-------IVEADMVVEAIGQA 537
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 91199540 317 PFTKNLGlEELGIELD-PRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAED 368
Cdd:PRK13984 538 PDYSYLP-EELKSKLEfVRGRILTNEYGQTSIPWLFAGGDIVHGPDIIHGVAD 589
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
39-184 |
4.37e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.09 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 39 PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGtclnvgcipsKAllnnSHYYHMAHGKDFASRGIE--MSEV 116
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG----------RA----AQLHKTFPGLDCPQCILEplIAEV 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199540 117 RLNldkmmeqkstavkaltGGIaHLFKQNKVVHVNGYGkitGKNQVTATKADGGTQVIDTKNILIATG 184
Cdd:COG1148 204 EAN----------------PNI-TVYTGAEVEEVSGYV---GNFTVTIKKGPREEIEIEVGAIVLATG 251
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
40-79 |
4.61e-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: 49.06 E-value: 4.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 91199540 40 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
38-79 |
6.17e-06 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 48.92 E-value: 6.17e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 91199540 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
43-79 |
1.07e-05 |
|
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: 47.67 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....*..
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
43-79 |
1.19e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 47.72 E-value: 1.19e-05
10 20 30
....*....|....*....|....*....|....*..
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
217-370 |
1.22e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 47.45 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 217 VVIGAGVIGVELGSVWQRLGAD--------------VTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKLNTKVTGAT 282
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLGS-FDQALRKYGQRRLRRLGVDIRTKTAVKEVL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 283 KKSdgkidvsIEAASGgkaEVITCDVLL--VCIGRRPFTKNLGleelgIELDPRGRIPVNTRFQTK-IPNIYAIGDVVAG 359
Cdd:PTZ00318 256 DKE-------VVLKDG---EVIPTGLVVwsTGVGPGPLTKQLK-----VDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320
|
170
....*....|....*.
gi 91199540 360 -----PMLAHKAEDEG 370
Cdd:PTZ00318 321 eerplPTLAQVASQQG 336
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
39-78 |
1.67e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 47.52 E-value: 1.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 91199540 39 PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 78
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
217-355 |
3.11e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.65 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 217 VVIGAGVIGVELGSVWQRLGADVTAVEF--------LGHVGG---------VGIDMEISKNFQRILQkQGfkfklntkvT 279
Cdd:PRK14989 149 AVVGGGLLGLEAAGALKNLGVETHVIEFapmlmaeqLDQMGGeqlrrkiesMGVRVHTSKNTLEIVQ-EG---------V 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91199540 280 GATKksdgkidvSIEAASGGKAEVitcDVLLVCIGRRPFTKnLGlEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK14989 219 EARK--------TMRFADGSELEV---DFIVFSTGIRPQDK-LA-TQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
44-359 |
3.53e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 46.33 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGtcLNVGCIPSkallnnshyYHMAhgKDFASRGIEM-----SEVRL 118
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPE---------FRLP--KDIVDREVERllklgVEIRT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 119 NldkmmeqksTAV-KALTggIAHLFKQNKVVHVNgygkiTGKNQVTATKADGgtqvIDTKNILIAtgsevtpfpgitIDE 197
Cdd:PRK11749 210 N---------TEVgRDIT--LDELRAGYDAVFIG-----TGAGLPRFLGIPG----ENLGGVYSA------------VDF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 198 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGA-DVTAVEFLGHVggvgiDMEISKNFQRILQKQGFKFKLNT 276
Cdd:PRK11749 258 LTRVNQAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAeSVTIVYRRGRE-----EMPASEEEVEHAKEEGVEFEWLA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199540 277 K---VTGatkksDGKIDVSIEA---------ASG-------GKAEVITCDVLLVCIGRRPFTKNLGLEElGIELDPRG-R 336
Cdd:PRK11749 333 ApveILG-----DEGRVTGVEFvrmelgepdASGrrrvpieGSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNRWGtI 406
|
330 340
....*....|....*....|...
gi 91199540 337 IPVNTRFQTKIPNIYAIGDVVAG 359
Cdd:PRK11749 407 IADDETGRTSLPGVFAGGDIVTG 429
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
46-80 |
3.69e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 41.75 E-value: 3.69e-05
10 20 30
....*....|....*....|....*....|....*
gi 91199540 46 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTC 80
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
43-79 |
3.70e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 46.27 E-value: 3.70e-05
10 20 30
....*....|....*....|....*....|....*..
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
43-86 |
6.66e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 45.57 E-value: 6.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG-TCLNVGCI 86
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
43-79 |
1.96e-04 |
|
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: 43.70 E-value: 1.96e-04
10 20 30
....*....|....*....|....*....|....*..
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
43-77 |
2.26e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.72 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....*
gi 91199540 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLG 77
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
42-79 |
2.40e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 43.59 E-value: 2.40e-04
10 20 30
....*....|....*....|....*....|....*...
gi 91199540 42 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
36-70 |
2.26e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 40.27 E-value: 2.26e-03
10 20 30
....*....|....*....|....*....|....*
gi 91199540 36 ADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCI 70
Cdd:PRK07494 2 LMEKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
324-378 |
5.12e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 39.34 E-value: 5.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 91199540 324 LEELGIELDPRGRIPVNT----RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMA 378
Cdd:PRK12769 590 LESHGVTVDKWGRIIADVesqyRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| |
