|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
1-384 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 665.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 1 MIFHSSCRVLHFFTRSKRLFTASLFTFTTQQTSLRLVWILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSN 80
Cdd:cd07793 118 KALRGGSKFLHFLTRNKRFLAASVLKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 81 ASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMG 160
Cdd:cd07793 198 ASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 161 TGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAESNAGDTGTAIKWAQQLDLFTDAAETEKMAKSLEDSEGVCFVPS 240
Cdd:cd07793 278 TGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASDTGTVIDWAKSIGLFDDPSETEDIAESVEDTNGVYFVPA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 241 FSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLIN 320
Cdd:cd07793 358 FSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLG 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483672 321 ENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKLRQSEVVFKPQKKCQEYEMSLENWAKAVK 384
Cdd:cd07793 438 KPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKMDNEKREELYKNWKKAVK 501
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
35-384 |
2.53e-178 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 505.08 E-value: 2.53e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRD 114
Cdd:cd07769 136 KIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 115 TSHNFGSVDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVC 194
Cdd:cd07769 216 SSEVFGYTDPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 195 LAESNAGDTGTAIKWA-QQLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAI 273
Cdd:cd07769 296 ALEGSIFIAGAAIQWLrDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 274 LESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEEL 353
Cdd:cd07769 376 LESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDEL 455
|
330 340 350
....*....|....*....|....*....|.
gi 1370483672 354 KKLRQSEVVFKPQKKCQEYEMSLENWAKAVK 384
Cdd:cd07769 456 ASLWQVDKRFEPSMDEEERERLYRGWKKAVE 486
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
38-389 |
6.13e-143 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 415.62 E-value: 6.13e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 38 WILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSH 117
Cdd:COG0554 142 WILDNVPGARERAEAGELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 118 NFGSVDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAE 197
Cdd:COG0554 222 VFGETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 198 SNAGDTGTAIKW-AQQLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILES 276
Cdd:COG0554 302 GSIFVAGAAVQWlRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALES 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 277 IAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKL 356
Cdd:COG0554 382 IAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAAL 461
|
330 340 350
....*....|....*....|....*....|...
gi 1370483672 357 RQSEVVFKPQKKCQEYEMSLENWAKAVKRSMNW 389
Cdd:COG0554 462 WKVDRRFEPQMDEEERERLYAGWKKAVERTLGW 494
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
36-384 |
1.01e-127 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 376.45 E-value: 1.01e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 36 LVWILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDT 115
Cdd:cd07786 137 IRWILDNVPGARERAERGELAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 116 SHNFGSVDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVV-C 194
Cdd:cd07786 217 SEVFGYTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTyA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 195 LaESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAI 273
Cdd:cd07786 297 L-EGSIFIAGAAVQWLRdGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 274 LESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEEL 353
Cdd:cd07786 376 LESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDEL 455
|
330 340 350
....*....|....*....|....*....|.
gi 1370483672 354 KKLRQSEVVFKPQKKCQEYEMSLENWAKAVK 384
Cdd:cd07786 456 AKLWQVDRRFEPSMSEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
32-389 |
2.13e-120 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 358.13 E-value: 2.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 32 TSLRLVWILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPP 111
Cdd:PTZ00294 138 SAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 112 VRDTSHNFGSVDEEIFG--VPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIG 189
Cdd:PTZ00294 218 IKSSSENFGTISGEAVPllEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 190 QE--VVCLAESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSK 266
Cdd:PTZ00294 298 PNgpTVYALEGSIAVAGAGVEWLRdNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTR 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 267 YHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGF 346
Cdd:PTZ00294 378 AHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGV 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1370483672 347 WTDKEELKKL-RQSEVVFKPQKKCQEYEMSLENWAKAVKRSMNW 389
Cdd:PTZ00294 458 WKSLEEVKKLiRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKW 501
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
38-389 |
2.11e-118 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 352.97 E-value: 2.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 38 WILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSH 117
Cdd:PRK00047 144 WILDNVEGARERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 118 NFGSV-DEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLA 196
Cdd:PRK00047 224 VYGKTnPYGFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 197 ESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILE 275
Cdd:PRK00047 304 EGSIFVAGSAIQWLRdGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 276 SIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKK 355
Cdd:PRK00047 384 SIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKE 463
|
330 340 350
....*....|....*....|....*....|....
gi 1370483672 356 LRQSEVVFKPQKKCQEYEMSLENWAKAVKRSMNW 389
Cdd:PRK00047 464 QWKIDRRFEPQMDEEEREKLYAGWKKAVKRTLAW 497
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
32-386 |
2.74e-108 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 327.17 E-value: 2.74e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 32 TSLRLVWILQNLTEVQKAVEEENCCFGTIDTWLLYKLT---KGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSL 108
Cdd:cd07792 139 SAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTggkNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 109 LPPVRDTSHNFGSVDEEIF-GVPIpiVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWK 187
Cdd:cd07792 219 LPEIRSSSEVYGKIASGPLaGVPI--SGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 188 IG-QEVVCLA-ESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPST 264
Cdd:cd07792 297 LGpDAPPVYAlEGSIAIAGAAVQWLRdNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 265 SKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAV 344
Cdd:cd07792 377 TKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAV 456
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1370483672 345 GFWTDKEELKKLRQSEV-VFKPQKKCQEYEMSLENWAKAVKRS 386
Cdd:cd07792 457 GVWKSLDELKSLNEGGRtVFEPQISEEERERRYKRWKKAVERS 499
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
34-389 |
8.15e-90 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 280.05 E-value: 8.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 34 LRLVWILQNLTEVQKAVEEENCCFGTIDTWLLYKLT---KGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLP 110
Cdd:PLN02295 141 TKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTggaSGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 111 PVRDTSHNFGSVDEEIFGVPIPIVALVADQQSAMFGECCfQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQ 190
Cdd:PLN02295 221 KIVSNSEVIGTIAKGWPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 191 EVVCL--AESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKY 267
Cdd:PLN02295 300 DAPTNyaLEGSVAIAGAAVQWLRdNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 268 HLVRAILESIAFRNKQLYEMMKKEI-----HIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGL 342
Cdd:PLN02295 380 HIARAVLESMCFQVKDVLDAMRKDAgeeksHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGL 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370483672 343 AVGFWTDKEELKKLRQ-SEVVFKPQKKCQEYEMSLENWAKAVKRSMNW 389
Cdd:PLN02295 460 AVGLWTEEEIFASEKWkNTTTFRPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
29-385 |
2.87e-54 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 186.58 E-value: 2.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 29 TQQTSLRLVWILQNLTEVQKAVEeencCFGTIDTWLLYKLTkGsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSL 108
Cdd:COG1070 130 PGFTAPKLLWLKENEPEIFARIA----KVLLPKDYLRYRLT-G-EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDREL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 109 LPPVRDTSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTgNSLQQTTGGFYPL 183
Cdd:COG1070 204 LPELVPPGEVAGTLTAEAaaeTGLPagTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 184 IGWKIGQEVVCLAESNAGdtGTAIKWAQQL---DLFTDAAE-TEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMG 259
Cdd:COG1070 283 FCHAVPGRWLPMGATNNG--GSALRWFRDLfadGELDDYEElNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 260 LKPSTSKYHLVRAILESIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASL 339
Cdd:COG1070 361 LTLSHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALL 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370483672 340 AGLAVGFWTD-KEELKKLRQSEVVFKPQKKCQE-YEMSLENWAKAVKR 385
Cdd:COG1070 440 AAVGLGLYDDlEEAAAAMVRVGETIEPDPENVAaYDELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
35-345 |
3.66e-54 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 185.10 E-value: 3.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNLTEVQKAVeeenCCFGTIDTWLLYKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRD 114
Cdd:cd07773 133 KLLWLREHEPEIFAKA----AKWLSVADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVP 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 115 TSHNFGSVDEEI---FGVPIPIVALVA--DQQSAMFGECCFQTGDVKLTMGTG-TFLDINTGNSLQQTTGGFYPLIGWKI 188
Cdd:cd07773 207 SGTVIGTVTPEAaeeLGLPAGTPVVVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 189 GQEVVCLAESNAGdtGTAIKWAQQL---DLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTS 265
Cdd:cd07773 287 PGGYYYLAGSLPG--GALLEWFRDLfggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTT 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 266 KYHLVRAILESIAFRNKQLYEMMKKeIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVG 345
Cdd:cd07773 365 RADLLRAILEGLAFELRLNLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
57-368 |
2.17e-53 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 182.72 E-value: 2.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 57 FGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDEEI---FGVP--I 131
Cdd:cd07779 106 FLTVQDYLLYRLT--GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAaeeTGLPegT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 132 PIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVclaESNAGDTGTAIKWAQ 211
Cdd:cd07779 184 PVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVL---EGSINTGGSAVRWFR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 212 QLdLFTDAAETEKMAKSLED------------SEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAF 279
Cdd:cd07779 261 DE-FGQDEVAEKELGVSPYEllneeaaksppgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAF 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 280 RNKQLYEMMKKEiHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEE-LKKLRQ 358
Cdd:cd07779 340 ELRDNLEAMEKA-GVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEaVKAMVR 418
|
330
....*....|
gi 1370483672 359 SEVVFKPQKK 368
Cdd:cd07779 419 VTDTFEPDPE 428
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
56-340 |
1.35e-52 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 179.68 E-value: 1.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 56 CFGTIDTWLLYKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDEEI---FGVP-- 130
Cdd:cd00366 104 KFLQPNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAaeeTGLPag 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 131 IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGgfypLIGWKIGQEVVCLAESNAGDTGTAIKWA 210
Cdd:cd00366 182 TPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPR----LLNRCHVVPGLWLLEGAINTGGASLRWF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 211 qqLDLF----TDAAETEKM----AKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNK 282
Cdd:cd00366 258 --RDEFgeeeDSDAEYEGLdelaAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALR 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483672 283 QLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLA 340
Cdd:cd00366 336 DNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
35-372 |
6.62e-51 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 177.36 E-value: 6.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNLTEVQKAVeeenCCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRD 114
Cdd:cd07770 133 KLLWLKEERPELFAKA----AKFVSIKEYLLYRLT--GELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVD 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 115 TSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGT---------GTFLDINTGNSLQQTTGGF 180
Cdd:cd07770 207 PTEVLPGLKPEFaerLGLLagTPVVLGASDGALANLGSGALDPGRAALTVGTsgairvvsdRPVLDPPGRLWCYRLDENR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 181 YpLIGwkigqevvcLAESNAGDtgtAIKWAQQ--LDLFTDAAETEKMAKSLE-DSEGVCFVPSFSGLQAPLNDPWACASF 257
Cdd:cd07770 287 W-LVG---------GAINNGGN---VLDWLRDtlLLSGDDYEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAF 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 258 MGLKPSTSKYHLVRAILESIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAA 337
Cdd:cd07770 354 FGLTLNHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAA 432
|
330 340 350
....*....|....*....|....*....|....*
gi 1370483672 338 SLAGLAVGFWTDKEELKKLRQSEvVFKPQKKCQEY 372
Cdd:cd07770 433 LLALEALGLISSLEADELVKIGK-VVEPDPENHAI 466
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
63-373 |
1.03e-50 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 176.96 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 63 WLLYKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDEEI---FGVP--IPIVALV 137
Cdd:cd07808 158 YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAaeeLGLPegTPVVAGA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 138 ADQQSAMFGECCFQTGDVKLTMGT-GTFL------DINTGNSLQqttggFYPLI---GWKIgqevvcLAESNAGdtGTAI 207
Cdd:cd07808 236 GDNAAAALGAGVVEPGDALISLGTsGVVFaptdkpVPDPKGRLH-----TFPHAvpgKWYA------MGVTLSA--GLSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 208 KWAQQLdLFTDAAETEKM----AKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQ 283
Cdd:cd07808 303 RWLRDL-FGPDRESFDELdaeaAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRD 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 284 LYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEE-LKKLRQSEVV 362
Cdd:cd07808 382 SLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEaAAACIKIEKT 460
|
330
....*....|..
gi 1370483672 363 FKP-QKKCQEYE 373
Cdd:cd07808 461 IEPdPERHEAYD 472
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
35-373 |
2.45e-44 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 159.99 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNLTEV-QKAVeeenCCFGTIDtWLLYKLTkGsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVR 113
Cdd:cd07805 136 KILWLKENEPEIyAKTH----KFLDAKD-YLNFRLT-G-RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 114 DTSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGT----GTF-----LDINTG-NSLQQTTG 178
Cdd:cd07805 209 PSTEVVGELTPEAaaeLGLPagTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTsgwvAAHvpkpkTDPDHGiFTLASADP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 179 GFYPLIGwkigqevvclAESNAGdtgTAIKWA-----QQLDLFTDAAE--TEKMAKSLEDSEGVCFVPSFSGLQAPLNDP 251
Cdd:cd07805 289 GRYLLAA----------EQETAG---GALEWArdnlgGDEDLGADDYEllDELAAEAPPGSNGLLFLPWLNGERSPVEDP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 252 WACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHiPVRKIRADGGVCKNGFVMQMTSDLINENIDRPAD-ID 330
Cdd:cd07805 356 NARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQE 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1370483672 331 MSCLGAASLAGLAVGFWTDKEELKKLRQSEVVFKPQKKCQE-YE 373
Cdd:cd07805 435 AGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRArYD 478
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
16-345 |
2.30e-41 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 151.14 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 16 SKRLFTASLFTFTTQQTSLRLVWILQNLTEV-QKAVEeenccFGTIDTWLLYKLTkgSVYATDFSNAS-TTGLFDPYKMC 93
Cdd:cd07804 116 EDRIFEITGNPLDSQSVGPKLLWIKRNEPEVfKKTRK-----FLGAYDYIVYKLT--GEYVIDYSSAGnEGGLFDIRKRT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 94 WSGMITSLISIPLSLLPPVRDTSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDIN 168
Cdd:cd07804 189 WDEELLEALGIDPDLLPELVPSTEIVGEVTKEAaeeTGLAegTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 169 TGN--SLQQ------------------TTGGfyPLIGWKIGQevVCLAESNAGDTGTAIKWaQQLDlftdaaetEKMAKS 228
Cdd:cd07804 269 TDKlpTDPRlwldyhdipgtyvlnggmATSG--SLLRWFRDE--FAGEEVEAEKSGGDSAY-DLLD--------EEAEKI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 229 LEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKN 308
Cdd:cd07804 336 PPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVI-REAGLPIKRLVAVGGGAKS 414
|
330 340 350
....*....|....*....|....*....|....*..
gi 1370483672 309 GFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVG 345
Cdd:cd07804 415 PLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
35-344 |
4.00e-36 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 136.58 E-value: 4.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNLTEVQKAVeeenCCFGTIDTWLLYKLTkGSVYATDFSNASTTGlFDPYKMCWSGMITSLISIPLSLLPPVRD 114
Cdd:cd07783 131 KLLWLKRHEPEVLAKT----AKFLHQADWLAGRLT-GDRGVTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 115 TSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFY----PLIG 185
Cdd:cd07783 205 PGTVIGTLTAEAaeeLGLPagTPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYshrhGDGY 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 186 WKIGqevvclAESNAGdtGTAIKWAQQLDlftDAAETEKMAKSlEDSEGVCFVP-SFSGLQAPLNDPWACASFmgLKPST 264
Cdd:cd07783 285 WLVG------GASNTG--GAVLRWFFSDD---ELAELSAQADP-PGPSGLIYYPlPLRGERFPFWDPDARGFL--LPRPH 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 265 SKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINenidRP---ADIDMSCLGAASLAG 341
Cdd:cd07783 351 DRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLG----VPvviAEEEEAALGAALLAA 426
|
...
gi 1370483672 342 LAV 344
Cdd:cd07783 427 AGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
35-345 |
2.40e-31 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 123.87 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNltevQKAVEEENCCFGTIDTWLLYKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRD 114
Cdd:cd07798 135 RLLWFKEN----RPEIFERIATVLSISDWIGYRLTG--ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 115 TSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTfldintgnSLQQTTGGfyPLIG---- 185
Cdd:cd07798 209 SGTVLGTVSEEAareLGLPegTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTT--------PVQMVTDE--PIIDperr 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 186 -WkIGQEVVC---LAESNAGDTGTAIKWAQQLdLFTDAAET-EKMAKSLEDSEGVCF-VPSFSGLQAPlnDPWACA---- 255
Cdd:cd07798 279 lW-TGCHLVPgkwVLESNAGVTGLNYQWLKEL-LYGDPEDSyEVLEEEASEIPPGANgVLAFLGPQIF--DARLSGlkng 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 256 ----SFMGLKPSTSKYHLVRAILESIAF---RN-KQLYEMMKKEIhipvRKIRADGGVCKNGFVMQMTSDLINENIDRPA 327
Cdd:cd07798 355 gflfPTPLSASELTRGDFARAILENIAFairANlEQLEEVSGREI----PYIILCGGGSRSALLCQILADVLGKPVLVPE 430
|
330
....*....|....*...
gi 1370483672 328 DIDMSCLGAASLAGLAVG 345
Cdd:cd07798 431 GREASALGAAICAAVGAG 448
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
155-343 |
2.81e-31 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 117.81 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 155 VKLTMGTGTFLDINTGNSLQQTTGgFYPLIGWKIGQEVVCLAESNAgDTGTAIKWAQQLDLFTDAAETEKMAKSLE---- 230
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHG-VWGPYTNEMLPGYWGLEGGQS-AAGSLLAWLLQFHGLREELRDAGNVESLAelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 231 -----DSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGV 305
Cdd:pfam02782 79 laavaPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1370483672 306 CKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLA 343
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
15-345 |
2.78e-28 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 114.96 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 15 RSKRLFTASLFTFTTQQTSLRLVWILQNltevqkavEEENccFGTIDT------WLLYKLTkGsVYATDFSNASTtGLFD 88
Cdd:cd07802 115 TLEKVYPLTGQPLWPGQPVALLRWLKEN--------EPER--YDRIRTvlfckdWIRYRLT-G-EISTDYTDAGS-SLLD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 89 PYKMCWSGMITSLISIP--LSLLPPVRDTSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGT 161
Cdd:cd07802 182 LDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAaalTGLPegTPVAAGAFDVVASALGAGAVDEGQLCVILGT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 162 ----GTFLD-INTGNSLQQTtgGFYPLIGWKigqevvcLAESNAGDTGTAIKWAqqLDLFTDAAET----------EKMA 226
Cdd:cd07802 262 wsinEVVTDePVVPDSVGSN--SLHADPGLY-------LIVEASPTSASNLDWF--LDTLLGEEKEaggsdydeldELIA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 227 KSLEDSEGVCFVPSFSGlqAPLNdPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKeiHIPVRKIRADGGVC 306
Cdd:cd07802 331 AVPPGSSGVIFLPYLYG--SGAN-PNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLV--ARKPETIRLTGGGA 405
|
330 340 350
....*....|....*....|....*....|....*....
gi 1370483672 307 KNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVG 345
Cdd:cd07802 406 RSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
35-379 |
2.00e-23 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 101.64 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNLTEVQKAVeeenCCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRD 114
Cdd:cd07775 137 RLLWLKNNRPEIYRKA----AKITMLSDWIAYKLS--GELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 115 TSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGeccfqTGDVKLTMGT---GTFldintgnsLQQTTGGFYPLIGW 186
Cdd:cd07775 211 SGTVIGKVTKEAaeeTGLKegTPVVVGGGDVQLGCLG-----LGVVRPGQTAvlgGSF--------WQQEVNTAAPVTDP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 187 KIGQEVVC-------LAESNAGDTGTAIKWaqqldlFTDA--AETEKMAKS--------LED--------SEGVcfVPSF 241
Cdd:cd07775 278 AMNIRVNChvipdmwQAEGISFFPGLVMRW------FRDAfcAEEKEIAERlgidaydlLEEmakdvppgSYGI--MPIF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 242 SGLQAPLNDPWACASFMGL---KPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDL 318
Cdd:cd07775 350 SDVMNYKNWRHAAPSFLNLdidPEKCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADV 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483672 319 INENIDRPADIDMSCLGAASLAGLAVGFWTDKEE-LKKLRQSEVVFKPQKKCQE-YEMSLENW 379
Cdd:cd07775 430 LGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEaVESLVKWEREYLPNPENHEvYQDLYEKW 492
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
24-146 |
7.76e-22 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 93.56 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 24 LFTFTTqqtSLRLVWILQNLTEVQKAVEeencCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLIS 103
Cdd:pfam00370 127 IWPGFT---LSKLRWIKENEPEVFEKIH----KFLTIHDYLRWRLT--GVFVTDHTNASRSMMFNIHKLDWDPELLAALG 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370483672 104 IPLSLLPPVRDTSHNFGSVDEEIFG-----VPIPIVALVADQQSAMFG 146
Cdd:pfam00370 198 IPRDHLPPLVESSEIYGELNPELAAmwgldEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
63-345 |
5.45e-21 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 94.23 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 63 WLLYKLTkgSVYATDFSNASTTgLFDPYKMCWSGMITSLISIP--LSLLPPVRDTSHNFGSVDEEI---FGVP--IPIVa 135
Cdd:cd24121 159 WLFYKLT--GEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAaaaTGLPagTPVV- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 136 lvadqqSAMFgeccfqtgDVKLT-MGTGTFLDiNTGNSLQQTTG-----GFYPLIGWKIGQEVVCLAESN------AGDT 203
Cdd:cd24121 235 ------LGPF--------DVVATaLGSGAIEP-GDACSILGTTGvhevvVDEPDLEPEGVGYTICLGVPGrwlramANMA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 204 GTA-IKWAqqLDLFTDAAETEKMAKSLED--------------SEGVCFVPSFS--GLQAPLNDPWACASFMGLKPSTSK 266
Cdd:cd24121 300 GTPnLDWF--LRELGEVLKEGAEPAGSDLfqdleelaassppgAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTR 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483672 267 YHLVRAILESIAFRNKQLYEMMKkeihIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVG 345
Cdd:cd24121 378 ADLLRAVYEGVALAMRDCYEHMG----EDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
20-345 |
8.86e-21 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 93.38 E-value: 8.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 20 FTASlftfttqqtslRLVWILQNltevqkavEEENccFGTIDT------WLLYKLTKGSVyaTDFSNASTTGLFDPYKMC 93
Cdd:cd07809 131 FTAS-----------KLLWLKEN--------EPEH--YARIAKillphdYLNWKLTGEKV--TGLGDASGTFPIDPRTRD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 94 WSGMITSLIS---IPLSLLPPVRDTSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFL 165
Cdd:cd07809 188 YDAELLAAIDpsrDLRDLLPEVLPAGEVAGRLTPEGaeeLGLPagIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 166 DINTGNSLQQ----------TTGGFYPLIgwkigqevvclaeSNAGDTGTAIKWAQQLdLFTDAAETEKMA-KSLEDSEG 234
Cdd:cd07809 268 YGVSDKPVSDphgrvatfcdSTGGMLPLI-------------NTTNCLTAWTELFREL-LGVSYEELDELAaQAPPGAGG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 235 VCFVPSFSGLQAPlNDPWACASFMGLKPS-TSKYHLVRAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVCKNGFVMQ 313
Cdd:cd07809 334 LLLLPFLNGERTP-NLPHGRASLVGLTLSnFTRANLARAALEGATFGLRYGLDILREL-GVEIDEIRLIGGGSKSPVWRQ 411
|
330 340 350
....*....|....*....|....*....|..
gi 1370483672 314 MTSDLINENIDRPADIDMSCLGAASLAGLAVG 345
Cdd:cd07809 412 ILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
125-373 |
1.54e-20 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 92.98 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 125 EIFGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTfLDINTGNSLQQTTG--GFYP------LIGWKIGQevvc 194
Cdd:cd07781 232 ERLGLPagIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTST-CHLMVSPKPVDIPGicGPVPdavvpgLYGLEAGQ---- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 195 laeSNAGDTgtaIKWAQQLdLFTDAAET--------EKMAKSLE-DSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTS 265
Cdd:cd07781 307 ---SAVGDI---FAWFVRL-FVPPAEERgdsiyallSEEAAKLPpGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTT 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 266 KYHLVRAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGV-CKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAV 344
Cdd:cd07781 380 PAHIYRALLEATAFGTRAIIERFEEA-GVPVNRVVACGGIaEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAA 458
|
250 260 270
....*....|....*....|....*....|.
gi 1370483672 345 GFWTDKEEL-KKLRQSEVVFKPQKKCQE-YE 373
Cdd:cd07781 459 GVYADIEEAaDAMVRVDRVYEPDPENHAvYE 489
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
56-320 |
2.13e-18 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 86.43 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 56 CFGTIDTWLL------YKLTkGSVyATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDEEIF-- 127
Cdd:cd07771 144 LLERADKLLMlpdllnYLLT-GEK-VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAee 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 128 --GVPIPIVAlVA--DQQSAMFGECCFQTGDVKLTMGT----GTFLD--INTGNSLQ------QTTGGFYPLI----GWK 187
Cdd:cd07771 222 lgLKGIPVIA-VAshDTASAVAAVPAEDEDAAFISSGTwsliGVELDepVITEEAFEagftneGGADGTIRLLknitGLW 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 188 IGQEvvCLAEsnagdtgtaikWAQQlDLFTDAAETEKMAKSLEDSEgvCFV----PSFsglQAPLNDPWACASFM---GL 260
Cdd:cd07771 301 LLQE--CRRE-----------WEEE-GKDYSYDELVALAEEAPPFG--AFIdpddPRF---LNPGDMPEAIRAYCretGQ 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 261 KPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLIN 320
Cdd:cd07771 362 PVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
36-340 |
6.06e-18 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 84.97 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 36 LVWILQNltevqKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDT 115
Cdd:cd07777 135 LFWLLRN-----GPLPSKADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 116 SHNFGSVDEEIfGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTG---TFLDintgnSLQQTTGGF--YPLIGwkiGQ 190
Cdd:cd07777 210 GEIVGTLSSAL-PKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLT-----PKFELSGSVeiRPFFD---GR 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 191 EVVCLAESNAGDTGTAIK-----WAQQLDLFTDAAE-TEKMAKSL--EDSEGVCFVPSFSGLQaplNDPWACASFMGLKP 262
Cdd:cd07777 281 YLLVAASLPGGRALAVLVdflreWLRELGGSLSDDEiWEKLDELAesEESSDLSVDPTFFGER---HDPEGRGSITNIGE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 263 STSKY-HLVRAILESIAfrnKQLYEMMKKEI--HIPVRKIRADGGVC-KNGFVMQMTSDLINENIDRPADIDMSCLGAAS 338
Cdd:cd07777 358 SNFTLgNLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAAL 434
|
..
gi 1370483672 339 LA 340
Cdd:cd07777 435 LA 436
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
25-373 |
2.85e-13 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 70.83 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 25 FTFTTQqtsLRLVWILQNLTEVQkaveEENCCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISI 104
Cdd:PRK10331 130 FSFNTL---YKLVWLKENHPQLL----EQAHAWLFISSLINHRLT--GEFTTDITMAGTSQMLDIQQRDFSPEILQATGL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 105 PLSLLPPVRDTSHNFGSVDEEI-----FGVPIPIVALVADQQSAMFGECCFQTGDVkLTMGTGTFLDINTGN-------- 171
Cdd:PRK10331 201 SRRLFPRLVEAGEQIGTLQPSAaallgLPVGIPVISAGHDTQFALFGSGAGQNQPV-LSSGTWEILMVRSAQvdtsllsq 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 172 ------SLQQTTGGFYPLIGWkigqevvcLAesnagdTGTaIKWAQQLdLFTDAAETEKM---AKSL-EDSEGVCFVPSF 241
Cdd:PRK10331 280 yagstcELDSQSGLYNPGMQW--------LA------SGV-LEWVRKL-FWTAETPYQTMieeARAIpPGADGVKMQCDL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 242 SGLQAplndpwacASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINE 321
Cdd:PRK10331 344 LACQN--------AGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDI 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370483672 322 NIDRPADIDMSCLGAASLAGLAVGFWTDKEELK-KLRQSEVVFKPQKKCQEYE 373
Cdd:PRK10331 416 PIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARaQMKYQYRYFYPQTEPEFIE 468
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
32-345 |
9.45e-13 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 69.23 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 32 TSLRLVWILQNLTEVqkaveeenccFGTIDTWLLYK----LTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLS 107
Cdd:PRK15027 128 TAPKLLWVQRHEPEI----------FRQIDKVLLPKdylrLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 108 LLPPVRDTSHNFGSVDEEI---FGVP-IPIVALVADQQSAMFGECCFQTGDVKLTMGT-GTFLDINTG--NSLQQTTGGF 180
Cdd:PRK15027 198 QMPALYEGSEITGALLPEVakaWGMAtVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflSKPESAVHSF 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 181 -YPLIG-WKIgQEVVCLAESnagdtgtAIKWAQQLDLFTDAAETEKMAKSLEDSEG-VCFVPSFSGLQAPLNDPWACASF 257
Cdd:PRK15027 278 cHALPQrWHL-MSVMLSAAS-------CLDWAAKLTGLSNVPALIAAAQQADESAEpVWFLPYLSGERTPHNNPQAKGVF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 258 MGLKPSTSKYHLVRAILESIAFrnkQLYEMMKKeIH---IPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMS-C 333
Cdd:PRK15027 350 FGLTHQHGPNELARAVLEGVGY---ALADGMDV-VHacgIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpA 425
|
330
....*....|..
gi 1370483672 334 LGAASLAGLAVG 345
Cdd:PRK15027 426 LGAARLAQIAAN 437
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
237-372 |
6.80e-10 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 60.63 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 237 FVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVR---AILESIAFRNKQLYEMMKKEIHiPVRKIRADGGVCKNGFVMQ 313
Cdd:cd07782 383 VLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGH-KIDTIFMCGGLSKNPLFVQ 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 314 MTSDLINENIDRPADIDMSCLGAASLAGLAVG-FWTDKEELKKLRQSEVVFKPQKKCQEY 372
Cdd:cd07782 462 LHADVTGCPVVLPKEPEAVLLGAAILGAVASGdFPSLWDAMAAMSGPGKVVEPNEELKKY 521
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
35-382 |
2.32e-09 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 58.86 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 35 RLVWILQNLTEVQKAVEEenccFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRD 114
Cdd:PRK10939 140 RLLWLAHHRPDIYRQAHT----ITMISDWIAYMLS--GELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 115 TSHNFGSVDEEI-----FGVPIPIVALVADQQSAmfgecCFQTGDVKL----TMGtGTF----LDINtgnslQQTTGgfy 181
Cdd:PRK10939 214 TGTVLGHVTAKAaaetgLRAGTPVVMGGGDVQLG-----CLGLGVVRPgqtaVLG-GTFwqqvVNLP-----APVTD--- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 182 PLIGWKIGQEVV---CLAESNAGDTGTAIKWaqqldlFTDA--AETEKMAKS--------LED--------SEGVcfVPS 240
Cdd:PRK10939 280 PNMNIRINPHVIpgmVQAESISFFTGLTMRW------FRDAfcAEEKLLAERlgidayslLEEmasrvpvgSHGI--IPI 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 241 FSGLQAPLNdpW--ACASFMGLK--PSTS-KYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMT 315
Cdd:PRK10939 352 FSDVMRFKS--WyhAAPSFINLSidPEKCnKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQIL 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483672 316 SDLINENIDRPADIDMSCLGAASLAGLAVGFWTD-KEELKKLRQSEVVFKPQ-KKCQEYEMSLENWAKA 382
Cdd:PRK10939 430 ADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSlAETGERLVRWERTFEPNpENHELYQEAKEKWQAV 498
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
232-366 |
6.23e-09 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 57.63 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 232 SEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLV---RAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVCKN 308
Cdd:cd07768 360 SIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTykyIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKN 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483672 309 GFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEEL----KKLRQSEVVFKPQ 366
Cdd:cd07768 439 ERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQLADSIteadISNDRKSETFEPL 500
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
268-345 |
9.08e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 50.61 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 268 HLVRAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVC-KNGFVMQMTSDLINENIDrPADIDMSC-LGAASLAGLAVG 345
Cdd:PRK04123 412 DIYRALIEATAFGTRAIMECFEDQ-GVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQ-VVASDQCPaLGAAIFAAVAAG 489
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
242-343 |
3.52e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 39.31 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483672 242 SGLQAPLNDPWACASFMGLKPSTSKYHLVR---AILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVCKNGFVMQMTSDL 318
Cdd:cd07778 387 LGNRTPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKE-KIIIQKVVISGSQAKNARLLQLLSTV 465
|
90 100
....*....|....*....|....*..
gi 1370483672 319 INE-NIDRPA-DIDMSCLGAASLAGLA 343
Cdd:cd07778 466 LSKiHIIVPLsDSKYAVVKGAALLGKA 492
|
|
| |
