|
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 ... |
15-422 |
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: 643.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 15 CRGADEsnCRSWhiNTEshfhYMEQLLHGATRVLHFFSRSKVMLTVSRFNFSTQHATLRLTWILQNLSEVKRAVEEDNCC 94
Cdd:cd07793 102 LRAAEL--CESW--NRS----LLLKALRGGSKFLHFLTRNKRFLAASVLKFSTAHVSIRLLWILQNNPELKEAAEKGELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 95 FGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIFGVPIPVVAL 174
Cdd:cd07793 174 FGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAEIPITAV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 175 VGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELVCLAEGNAGDTGTAIMWAQKLDLF 254
Cdd:cd07793 254 VADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASDTGTVIDWAKSIGLF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 255 TDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYDMLQREIQIPV 334
Cdd:cd07793 334 DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 335 TNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKLRQSEMVFKPQKKWQEYEVNM 414
Cdd:cd07793 414 SSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKMDNEKREELY 493
|
....*...
gi 568961414 415 ENWVKAVK 422
Cdd:cd07793 494 KNWKKAVK 501
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
65-422 |
2.30e-164 |
|
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: 471.18 E-value: 2.30e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 65 FStqhATlRLTWILQNLSEVKRAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPL 144
Cdd:cd07769 132 FS---AT-KIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 145 SILPPVKDTSYNFGSVDEKIFGVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGW 224
Cdd:cd07769 208 SMLPEVRPSSEVFGYTDPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAW 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 225 KIGQELVCLAEGNAGDTGTAIMWA-QKLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTN 303
Cdd:cd07769 288 QIGGKVTYALEGSIFIAGAAIQWLrDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 304 KYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 383
Cdd:cd07769 368 KAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG 447
|
330 340 350
....*....|....*....|....*....|....*....
gi 568961414 384 FWADKEELQKLRQSEMVFKPQKKWQEYEVNMENWVKAVK 422
Cdd:cd07769 448 FWKDLDELASLWQVDKRFEPSMDEEERERLYRGWKKAVE 486
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
65-427 |
2.75e-140 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 410.22 E-value: 2.75e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 65 FStqhATlRLTWILQNLSEVKRAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPL 144
Cdd:COG0554 135 FS---AT-KIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 145 SILPPVKDTSYNFGSVDEKIFGVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGW 224
Cdd:COG0554 211 SMLPEVRPSSEVFGETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAW 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 225 KIGQELVCLAEGNAGDTGTAIMW-AQKLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTN 303
Cdd:COG0554 291 GLGGKVTYALEGSIFVAGAAVQWlRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 304 KYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 383
Cdd:COG0554 371 RAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVG 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568961414 384 FWADKEELQKLRQSEMVFKPQKKWQEYEVNMENWVKAVKRSMNW 427
Cdd:COG0554 451 FWKSLEELAALWKVDRRFEPQMDEEERERLYAGWKKAVERTLGW 494
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
65-422 |
4.82e-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: 376.06 E-value: 4.82e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 65 FStqhATlRLTWILQNLSEVKRAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPL 144
Cdd:cd07786 132 FS---AT-KIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 145 SILPPVKDTSYNFGSVDEKIFGVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGW 224
Cdd:cd07786 208 SMLPEVKPSSEVFGYTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAW 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 225 KIGQELV-CLaEGNAGDTGTAIMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHST 302
Cdd:cd07786 288 QLGGKVTyAL-EGSIFIAGAAVQWLRdGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGT 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 303 NKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAV 382
Cdd:cd07786 367 TRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAV 446
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568961414 383 GFWADKEELQKLRQSEMVFKPQKKWQEYEVNMENWVKAVK 422
Cdd:cd07786 447 GLWKSLDELAKLWQVDRRFEPSMSEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
65-427 |
5.81e-117 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 350.81 E-value: 5.81e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 65 FSTQHATLRLTWILQNLSEVKRAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPL 144
Cdd:PTZ00294 133 ISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 145 SILPPVKDTSYNFGSVDEKIFG--VPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLI 222
Cdd:PTZ00294 213 ETLPEIKSSSENFGTISGEAVPllEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 223 GWKIGQELVCL--AEGNAGDTGTAIMWAQK-LDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLK 299
Cdd:PTZ00294 293 CYQLGPNGPTVyaLEGSIAVAGAGVEWLRDnMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMT 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 300 HSTNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAG 379
Cdd:PTZ00294 373 LKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAG 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568961414 380 LAVGFWADKEELQKL-RQSEMVFKPQKKWQEYEVNMENWVKAVKRSMNW 427
Cdd:PTZ00294 453 LAVGVWKSLEEVKKLiRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKW 501
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
76-427 |
1.04e-115 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 347.58 E-value: 1.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 76 WILQNLSEVKRAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSY 155
Cdd:PRK00047 144 WILDNVEGARERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 156 NFGSV-DEKIFGVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELVCLA 234
Cdd:PRK00047 224 VYGKTnPYGFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 235 EGNAGDTGTAIMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILE 313
Cdd:PRK00047 304 EGSIFVAGSAIQWLRdGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 314 SIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQK 393
Cdd:PRK00047 384 SIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKE 463
|
330 340 350
....*....|....*....|....*....|....*.
gi 568961414 394 LRQSEMVFKPQkkWQEYEVN--MENWVKAVKRSMNW 427
Cdd:PRK00047 464 QWKIDRRFEPQ--MDEEEREklYAGWKKAVKRTLAW 497
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
65-424 |
8.86e-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: 8.86e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 65 FSTQHATLRLTWILQNLSEVKRAVEEDNCCFGTIDTWLLYKLT---KGSSYATDYSNASTTGFFDPYAMRWSRLITTMVS 141
Cdd:cd07792 134 ISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTggkNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 142 IPLSILPPVKDTSYNFGSVDEKIF-GVPIpvVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYP 220
Cdd:cd07792 214 IPMSILPEIRSSSEVYGKIASGPLaGVPI--SGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 221 LIGWKIG-QELVCLA-EGNAGDTGTAIMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMG 297
Cdd:cd07792 292 TVAYKLGpDAPPVYAlEGSIAIAGAAVQWLRdNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 298 LKHSTNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASL 377
Cdd:cd07792 372 LTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIA 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568961414 378 AGLAVGFWADKEELQKLRQSEM-VFKPQKKWQEYEVNMENWVKAVKRS 424
Cdd:cd07792 452 AGLAVGVWKSLDELKSLNEGGRtVFEPQISEEERERRYKRWKKAVERS 499
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
66-427 |
1.89e-88 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 277.74 E-value: 1.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 66 STQHATLRLTWILQNLSEVKRAVEEDNCCFGTIDTWLLYKLT---KGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSI 142
Cdd:PLN02295 135 STYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTggaSGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 143 PLSILPPVKDTSYNFGSVDEKIFGVPIPVVALVGDQQSAMFGECCfETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLI 222
Cdd:PLN02295 215 PAEILPKIVSNSEVIGTIAKGWPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 223 GWKIGQELVCL--AEGNAGDTGTAIMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLK 299
Cdd:PLN02295 294 AYKLGPDAPTNyaLEGSVAIAGAAVQWLRdNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGIT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 300 HSTNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTN-----IRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGA 374
Cdd:PLN02295 374 RFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGA 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568961414 375 ASLAGLAVGFWADKEEL-QKLRQSEMVFKPQKKWQEYEVNMENWVKAVKRSMNW 427
Cdd:PLN02295 454 AYAAGLAVGLWTEEEIFaSEKWKNTTTFRPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
73-423 |
1.75e-53 |
|
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: 185.81 E-value: 1.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNLSEVKRAVEedncCFGTIDTWLLYKLTkGSsYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 152
Cdd:COG1070 136 KLLWLKENEPEIFARIA----KVLLPKDYLRYRLT-GE-FVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 153 TSYNFGSVDEKI---FGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNG---GFYPLIGW 224
Cdd:COG1070 210 PGEVAGTLTAEAaaeTGLPagTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGrvhTFCHAVPG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 225 KIGQELVCLAegnagdTGTAIMWAQKL---DLFTDAAETEKMALSLE-DSEGVYFVPSFSGLQAPLNDPCACASFMGLKH 300
Cdd:COG1070 290 RWLPMGATNN------GGSALRWFRDLfadGELDDYEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 301 STNKYHLVRAILESIAFRNKQLYDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGL 380
Cdd:COG1070 364 SHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAV 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568961414 381 AVGFWAD-KEELQKLRQSEMVFKPQKKWQE-YEVNMENWVKAVKR 423
Cdd:COG1070 443 GLGLYDDlEEAAAAMVRVGETIEPDPENVAaYDELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
94-378 |
4.40e-53 |
|
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: 181.99 E-value: 4.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 94 CFGTIDTWLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP-- 168
Cdd:cd00366 104 KFLQPNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAaeeTGLPag 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 169 IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGK---------NLQHVNGGFYpligwkigqelvcLAEGNAG 239
Cdd:cd00366 182 TPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEpvppdprllNRCHVVPGLW-------------LLEGAIN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 240 DTGTAIMWAqkLDLFTDAAETEKMALSLED--------SEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAI 311
Cdd:cd00366 249 TGGASLRWF--RDEFGEEEDSDAEYEGLDElaaevppgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAV 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961414 312 LESIAFrnkQLYDMLQ--REIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLA 378
Cdd:cd00366 327 LEGVAY---ALRDNLEilEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
95-409 |
1.04e-50 |
|
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: 176.94 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 95 FGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--I 169
Cdd:cd07779 106 FLTVQDYLLYRLT--GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAaeeTGLPegT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 170 PVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIG-----WkigqelvcLAEGNAGDTGTA 244
Cdd:cd07779 184 PVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSavpgkW--------VLEGSINTGGSA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 245 IMWAQKLdLFTDAAETEKMALSLED------------SEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAIL 312
Cdd:cd07779 256 VRWFRDE-FGQDEVAEKELGVSPYEllneeaaksppgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAIL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 313 ESIAFrnkQLYDMLQ--REIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEE 390
Cdd:cd07779 335 EGIAF---ELRDNLEamEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEE 411
|
330 340
....*....|....*....|
gi 568961414 391 -LQKLRQSEMVFKPQKKWQE 409
Cdd:cd07779 412 aVKAMVRVTDTFEPDPENVA 431
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
101-411 |
4.81e-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: 176.19 E-value: 4.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 101 WLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--IPVVALV 175
Cdd:cd07808 158 YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAaeeLGLPegTPVVAGA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 176 GDQQSAMFGECCFETGDVKLTMGT-GTFL------DINTGKNLQ---HVNGGFYPLIGwkigqelVCLAegnagdTGTAI 245
Cdd:cd07808 236 GDNAAAALGAGVVEPGDALISLGTsGVVFaptdkpVPDPKGRLHtfpHAVPGKWYAMG-------VTLS------AGLSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 246 MWAQKL--DLFTDAAETEKMAL-SLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQL 322
Cdd:cd07808 303 RWLRDLfgPDRESFDELDAEAAkVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 323 YDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQK-LRQSEMVF 401
Cdd:cd07808 383 LEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAaCIKIEKTI 461
|
330
....*....|.
gi 568961414 402 KPQKKWQE-YE 411
Cdd:cd07808 462 EPDPERHEaYD 472
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
73-383 |
1.96e-47 |
|
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: 168.53 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNLSEVKRAVeednCCFGTIDTWLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 152
Cdd:cd07773 133 KLLWLREHEPEIFAKA----AKWLSVADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVP 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 153 TSYNFGSVDEKI---FGVP--IPVValVG--DQQSAMFGECCFETGDVKLTMGTG-TFLDINTGKNLQHVNGGFYPLIGW 224
Cdd:cd07773 207 SGTVIGTVTPEAaeeLGLPagTPVV--VGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGH 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 225 KIGQELVCLAEGNAGdtGTAIMWAQKL---DLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHS 301
Cdd:cd07773 285 HVPGGYYYLAGSLPG--GALLEWFRDLfggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 302 TNKYHLVRAILESIAFRNKQLYDMLQReIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLA 381
Cdd:cd07773 363 TTRADLLRAILEGLAFELRLNLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVG 441
|
..
gi 568961414 382 VG 383
Cdd:cd07773 442 AG 443
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
73-410 |
1.68e-46 |
|
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: 166.58 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNLSEVKRAVeednCCFGTIDTWLLYKLTKGssYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 152
Cdd:cd07770 133 KLLWLKEERPELFAKA----AKFVSIKEYLLYRLTGE--LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVD 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 153 TSYNFGSVDEKI---FGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGF--YPLIG-- 223
Cdd:cd07770 207 PTEVLPGLKPEFaerLGLLagTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLwcYRLDEnr 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 224 WKIGqelvclaeG---NAGDtgtAIMWAQK--LDLFTDAAETEKMALSLE-DSEGVYFVPSFSGLQAPLNDPCACASFMG 297
Cdd:cd07770 287 WLVG--------GainNGGN---VLDWLRDtlLLSGDDYEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFG 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 298 LKHSTNKYHLVRAILESIAFRNKQLYDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASL 377
Cdd:cd07770 356 LTLNHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALL 434
|
330 340 350
....*....|....*....|....*....|...
gi 568961414 378 AGLAVGFWADKeELQKLRQSEMVFKPQKKWQEY 410
Cdd:cd07770 435 ALEALGLISSL-EADELVKIGKVVEPDPENHAI 466
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
76-411 |
1.22e-45 |
|
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: 164.62 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 76 WILQNLSEV-KRAVeednCCFGTIDtWLLYKLTkGSsYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTS 154
Cdd:cd07805 139 WLKENEPEIyAKTH----KFLDAKD-YLNFRLT-GR-AATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPST 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 155 YNFGSVDEKI---FGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGK----------NLQHVNGGFY 219
Cdd:cd07805 212 EVVGELTPEAaaeLGLPagTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKpktdpdhgifTLASADPGRY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 220 pligwkigqeLVCLAEGNAGdtgTAIMWA-----QKLDLFTDAAE--TEKMALSLEDSEGVYFVPSFSGLQAPLNDPCAC 292
Cdd:cd07805 292 ----------LLAAEQETAG---GALEWArdnlgGDEDLGADDYEllDELAAEAPPGSNGLLFLPWLNGERSPVEDPNAR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 293 ASFMGLKHSTNKYHLVRAILESIAFRNKQLYDMLQREIQiPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAH-FDMSC 371
Cdd:cd07805 359 GAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGA 437
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568961414 372 LGAASLAGLAVGFWADKEELQKLRQSEMVFKPQKKWQE-YE 411
Cdd:cd07805 438 LGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRArYD 478
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
65-383 |
2.00e-38 |
|
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: 144.21 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 65 FSTQHATLRLTWILQNLSEV-KRAVEednccFGTIDTWLLYKLTkgSSYATDYSNAS-TTGFFDPYAMRWSRLITTMVSI 142
Cdd:cd07804 127 LDSQSVGPKLLWIKRNEPEVfKKTRK-----FLGAYDYIVYKLT--GEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 143 PLSILPPVKDTSYNFGSVDEKI---FGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQ----- 212
Cdd:cd07804 200 DPDLLPELVPSTEIVGEVTKEAaeeTGLAegTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTdprlw 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 213 ---HVNGGFY----------PLIGW---KIGQELVClAEGNAGDTGtaimwaqkLDLFTDAAETekmalSLEDSEGVYFV 276
Cdd:cd07804 280 ldyHDIPGTYvlnggmatsgSLLRWfrdEFAGEEVE-AEKSGGDSA--------YDLLDEEAEK-----IPPGSDGLIVL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 277 PSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDL 356
Cdd:cd07804 346 PYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADV 424
|
330 340
....*....|....*....|....*..
gi 568961414 357 INEKIDRPAHFDMSCLGAASLAGLAVG 383
Cdd:cd07804 425 TGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
101-382 |
2.39e-33 |
|
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: 129.65 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 101 WLLYKLTkGSSYATDYSNASTTGFfDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--IPVVALV 175
Cdd:cd07783 155 WLAGRLT-GDRGVTDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAaeeLGLPagTPVVAGT 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 176 GDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFY--PLIgwkIGQELVclaeGNAGDTGTAImwaqkLDL 253
Cdd:cd07783 233 TDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYshRHG---DGYWLV----GGASNTGGAV-----LRW 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 254 FTDAAETEKMA--LSLEDSEGVYFVP-SFSGLQAPLNDPCACASFMGLKHstNKYHLVRAILESIAFRNKQLYDMLQREI 330
Cdd:cd07783 301 FFSDDELAELSaqADPPGPSGLIYYPlPLRGERFPFWDPDARGFLLPRPH--DRAEFLRALLEGIAFIERLGYERLEELG 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568961414 331 QIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHfDMSCLGAASLAGLAV 382
Cdd:cd07783 379 APPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
97-383 |
1.18e-30 |
|
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: 122.72 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 97 TIDTWLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--IPV 171
Cdd:cd07798 155 SISDWIGYRLTG--ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAareLGLPegTPV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 172 VALVGDQQSAMFGECCFETGDVKLTMGTGT---------FLDIN----TGKnlqHVNGGFYPLigwkigqelvclaEGNA 238
Cdd:cd07798 233 VVGGADTQCALLGSGAIEPGDIGIVAGTTTpvqmvtdepIIDPErrlwTGC---HLVPGKWVL-------------ESNA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 239 GDTGTAIMWAQKLdLFTDAAET-----EKMALSLEDSEGVYfvpSFSGLQAPlnDPCACA--------SFMGLKHSTNKY 305
Cdd:cd07798 297 GVTGLNYQWLKEL-LYGDPEDSyevleEEASEIPPGANGVL---AFLGPQIF--DARLSGlknggflfPTPLSASELTRG 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961414 306 HLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 383
Cdd:cd07798 371 DFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
193-381 |
7.72e-29 |
|
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: 112.03 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 193 VKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELvcLAEGNAGDTGTAIMW----------AQKLDLFTDAAETEK 262
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEMLPGYW--GLEGGQSAAGSLLAWllqfhglreeLRDAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 263 MALSLeDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGG 342
Cdd:pfam02782 79 LAAVA-PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 568961414 343 VCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLA 381
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
101-383 |
1.48e-27 |
|
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: 113.80 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 101 WLLYKLTkGSsYATDYSNASTtGFFDPYAMRWSRLITTMVSIP--LSILPPVKDTSYNFGSVDEKI---FGVP--IPVVA 173
Cdd:cd07802 159 WIRYRLT-GE-ISTDYTDAGS-SLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAaalTGLPegTPVAA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 174 LVGDQQSAMFGECCFETGDVKLTMGTGTfldINTG--KNLQHVNGGF----YPLIGWKIgqelvcLAEGNAgdTGTAIM- 246
Cdd:cd07802 236 GAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGsnslHADPGLYL------IVEASP--TSASNLd 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 247 WAqkLDLFTDAAET----------EKMALSLEDSEGVYFVPSFSGlqAPLNdPCACASFMGLKHSTNKYHLVRAILESIA 316
Cdd:cd07802 305 WF--LDTLLGEEKEaggsdydeldELIAAVPPGSSGVIFLPYLYG--SGAN-PNARGGFFGLTAWHTRAHLLRAVYEGIA 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961414 317 FRNKQLYDMLQREiqIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 383
Cdd:cd07802 380 FSHRDHLERLLVA--RKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
73-383 |
1.40e-23 |
|
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: 102.24 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNlsevkravEEDNccFGTIDT------WLLYKLTKGssYATDYSNASTTGFFDPYAMRWSRLIT---TMVSIP 143
Cdd:cd07809 135 KLLWLKEN--------EPEH--YARIAKillphdYLNWKLTGE--KVTGLGDASGTFPIDPRTRDYDAELLaaiDPSRDL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 144 LSILPPVKDTSYNFGSVDEKI---FGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQ------ 212
Cdd:cd07809 203 RDLLPEVLPAGEVAGRLTPEGaeeLGLPagIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSdphgrv 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 213 ----HVNGGFYPLIgwkigqelvClaegNAGDTGTAIMWAQKLdLFTDAAETEKMALSLE-DSEGVYFVPSFSGLQAPlN 287
Cdd:cd07809 283 atfcDSTGGMLPLI---------N----TTNCLTAWTELFREL-LGVSYEELDELAAQAPpGAGGLLLLPFLNGERTP-N 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 288 DPCACASFMGLKHS-TNKYHLVRAILESIAFrnkQLYDMLQ--REIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRP 364
Cdd:cd07809 348 LPHGRASLVGLTLSnFTRANLARAALEGATF---GLRYGLDilRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVP 424
|
330
....*....|....*....
gi 568961414 365 AHFDMSCLGAASLAGLAVG 383
Cdd:cd07809 425 ETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
73-417 |
1.08e-22 |
|
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: 100.10 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNLSEVKRAVeednCCFGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 152
Cdd:cd07775 137 RLLWLKNNRPEIYRKA----AKITMLSDWIAYKLS--GELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 153 TSYNFGSVDEKI---FGVP--IPVVALVGDQQSAMFGeccfeTGDVKLTMGT---GTF--LDINTG-------------- 208
Cdd:cd07775 211 SGTVIGKVTKEAaeeTGLKegTPVVVGGGDVQLGCLG-----LGVVRPGQTAvlgGSFwqQEVNTAapvtdpamnirvnc 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 209 ---KNLQHVNG-GFYP--LIGW---KIGQELVCLAEGNAGDTgtaimwaqkLDLFTDAAetekmALSLEDSEGVyfVPSF 279
Cdd:cd07775 286 hviPDMWQAEGiSFFPglVMRWfrdAFCAEEKEIAERLGIDA---------YDLLEEMA-----KDVPPGSYGI--MPIF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 280 SGLQAPLNDPCACASFMGL---KHSTNKYHLVRAILESIAFRNKQLYDMLQReiqipVTNIRAD-----GGVCNNAFVMQ 351
Cdd:cd07775 350 SDVMNYKNWRHAAPSFLNLdidPEKCNKATFFRAIMENAAIVSAGNLERIAE-----FSGIFPDslvfaGGASKGKLWCQ 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961414 352 MTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEE-LQKLRQSEMVFKPQKKWQE-YEVNMENW 417
Cdd:cd07775 425 ILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEaVESLVKWEREYLPNPENHEvYQDLYEKW 492
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
73-184 |
2.54e-20 |
|
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: 89.70 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNLSEVKRAVEedncCFGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 152
Cdd:pfam00370 135 KLRWIKENEPEVFEKIH----KFLTIHDYLRWRLT--GVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVE 208
|
90 100 110
....*....|....*....|....*....|....*..
gi 568961414 153 TSYNFGSVDEKIFG-----VPIPVVALVGDQQSAMFG 184
Cdd:pfam00370 209 SSEIYGELNPELAAmwgldEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
76-378 |
5.02e-20 |
|
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: 91.51 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 76 WILQNlsevkRAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSY 155
Cdd:cd07777 137 WLLRN-----GPLPSKADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 156 NFGSVDEKIfGVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHvnGGF--YPLIGwkiGQELVCL 233
Cdd:cd07777 212 IVGTLSSAL-PKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELS--GSVeiRPFFD---GRYLLVA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 234 AEGNAGDTGTAIM-----WAQKLDLFTDAAE-TEKM--ALSLEDSEGVYFVPSFSGLQaplNDPCACASFMGLKHSTNKY 305
Cdd:cd07777 286 ASLPGGRALAVLVdflreWLRELGGSLSDDEiWEKLdeLAESEESSDLSVDPTFFGER---HDPEGRGSITNIGESNFTL 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961414 306 -HLVRAILESIAfrnKQLYDMLQREI--QIPVTNIRADGGVCN-NAFVMQMTSDLINEKIDRPAHFDMSCLGAASLA 378
Cdd:cd07777 363 gNLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
101-383 |
7.30e-19 |
|
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: 88.45 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 101 WLLYKLTkGSSyATDYSNASTTgFFDPYAMRWSRLITTMVSIP--LSILPPVKDTSYNFGSVDEKI---FGVP--IPVVA 173
Cdd:cd24121 159 WLFYKLT-GEI-ATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAaaaTGLPagTPVVL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 174 LVGDQQSAMFGECCFETGDVKLTMGT----GTFLD------INTGKNLQHVNGGFY----------PLIGWKIGQelvcl 233
Cdd:cd24121 236 GPFDVVATALGSGAIEPGDACSILGTtgvhEVVVDepdlepEGVGYTICLGVPGRWlramanmagtPNLDWFLRE----- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 234 aegnAGDTGTAIMWAQKLDLFTDAaetEKMALSLE-DSEGVYFVPSFS--GLQAPLNDPCACASFMGLKHSTNKYHLVRA 310
Cdd:cd24121 311 ----LGEVLKEGAEPAGSDLFQDL---EELAASSPpGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRA 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961414 311 ILESIAFRNKQLYdmlqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 383
Cdd:cd24121 384 VYEGVALAMRDCY----EHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
163-416 |
3.35e-18 |
|
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: 86.44 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 163 KIFGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTfLDINTGKNLQHVNG--GFYP------LIGWKIGQ---- 228
Cdd:cd07781 232 ERLGLPagIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTST-CHLMVSPKPVDIPGicGPVPdavvpgLYGLEAGQsavg 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 229 -------ELVCLAEGNAGDTgtaimwaqKLDLFTDAAETEKMalsleDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHS 301
Cdd:cd07781 311 difawfvRLFVPPAEERGDS--------IYALLSEEAAKLPP-----GESGLVALDWFNGNRTPLVDPRLRGAIVGLTLG 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 302 TNKYHLVRAILESIAFRNKQLYDMLQREiQIPVTNIRADGGV-CNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGL 380
Cdd:cd07781 378 TTPAHIYRALLEATAFGTRAIIERFEEA-GVPVNRVVACGGIaEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAV 456
|
250 260 270
....*....|....*....|....*....|....*.
gi 568961414 381 AVGFWADKEELQKlrqsemVFKPQKKwqEYEVNMEN 416
Cdd:cd07781 457 AAGVYADIEEAAD------AMVRVDR--VYEPDPEN 484
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
94-358 |
2.85e-16 |
|
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: 80.65 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 94 CFGTIDTWLL------YKLTkgSSYATDYSNASTTGFFDPYAMRWSR-LITTMvSIPLSILPPVKDTSYNFGSVDEKIF- 165
Cdd:cd07771 144 LLERADKLLMlpdllnYLLT--GEKVAEYTIASTTQLLDPRTKDWSEeLLEKL-GLPRDLFPPIVPPGTVLGTLKPEVAe 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 166 ---GVPIPVVALVG-DQQSAMFGECCFETGDVKLTMGT----GTFLD--INTGK-------NLQHVNGGFYPL---IGWK 225
Cdd:cd07771 221 elgLKGIPVIAVAShDTASAVAAVPAEDEDAAFISSGTwsliGVELDepVITEEafeagftNEGGADGTIRLLkniTGLW 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 226 IGQElvCLAEgnagdtgtaimWAQKlDLFTDAAETEKMALSLEDSEGVYFV--PSFsglQAPLNDPCACASFM---GLKH 300
Cdd:cd07771 301 LLQE--CRRE-----------WEEE-GKDYSYDELVALAEEAPPFGAFIDPddPRF---LNPGDMPEAIRAYCretGQPV 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961414 301 STNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLIN 358
Cdd:cd07771 364 PESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
73-391 |
2.74e-15 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 77.70 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNLSEVkraveednccFGTIDTWLLYK----LTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILP 148
Cdd:PRK15027 131 KLLWVQRHEPEI----------FRQIDKVLLPKdylrLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 149 PVKDTSYNFGSVDEKI---FGVP-IPVVALVGDQQSAMFGECCFETGDVKLTMGT-GTFLDINTG---KNLQHVNGGFYP 220
Cdd:PRK15027 201 ALYEGSEITGALLPEVakaWGMAtVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflsKPESAVHSFCHA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 221 LIG-WKIGQELVCLAegnagdtgTAIMWAQKLDLFTDAAETEKMALSLEDSEG-VYFVPSFSGLQAPLNDPCACASFMGL 298
Cdd:PRK15027 281 LPQrWHLMSVMLSAA--------SCLDWAAKLTGLSNVPALIAAAQQADESAEpVWFLPYLSGERTPHNNPQAKGVFFGL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 299 KHSTNKYHLVRAILESIAFRNKQLYDMLQrEIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMS-CLGAASL 377
Cdd:PRK15027 353 THQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARL 431
|
330
....*....|....
gi 568961414 378 AGLAVGFWADKEEL 391
Cdd:PRK15027 432 AQIAANPEKSLIEL 445
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
60-411 |
1.15e-12 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 69.29 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 60 VSRFNFSTQHatlRLTWILQNLSEVKraveEDNCCFGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTM 139
Cdd:PRK10331 127 VGAFSFNTLY---KLVWLKENHPQLL----EQAHAWLFISSLINHRLT--GEFTTDITMAGTSQMLDIQQRDFSPEILQA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 140 VSIPLSILPPVKDTSYNFGSVDEKI-----FGVPIPVVALVGDQQSAMFGECCFETGDVkLTMGTGTFLDINTgknlQHV 214
Cdd:PRK10331 198 TGLSRRLFPRLVEAGEQIGTLQPSAaallgLPVGIPVISAGHDTQFALFGSGAGQNQPV-LSSGTWEILMVRS----AQV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 215 N------------------GGFYPLIGWkigqelvcLAEGnagdtgtAIMWAQKLdLFTDAAETEKM---ALSL-EDSEG 272
Cdd:PRK10331 273 DtsllsqyagstceldsqsGLYNPGMQW--------LASG-------VLEWVRKL-FWTAETPYQTMieeARAIpPGADG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 273 VYFVPSFSGlqaplndpCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQM 352
Cdd:PRK10331 337 VKMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQI 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 353 TSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQ-KLRQSEMVFKPQKKWQEYE 411
Cdd:PRK10331 409 KANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARaQMKYQYRYFYPQTEPEFIE 468
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
73-420 |
4.14e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 67.72 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 73 RLTWILQNLSEVKRAVEEdnccFGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 152
Cdd:PRK10939 140 RLLWLAHHRPDIYRQAHT----ITMISDWIAYMLS--GELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 153 TSYNFGSVDEKI-----FGVPIPVVALVGDQQSAMFGECCFETGDVkLTMGtGTFL-------------DINTGKNLQHV 214
Cdd:PRK10939 214 TGTVLGHVTAKAaaetgLRAGTPVVMGGGDVQLGCLGLGVVRPGQT-AVLG-GTFWqqvvnlpapvtdpNMNIRINPHVI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 215 NG-------GFYP--LIGW---KIGQELVCLAEGNAGDTGTAImwaqkldlftdaaetEKMALSLE-DSEGVyfVPSFSG 281
Cdd:PRK10939 292 PGmvqaesiSFFTglTMRWfrdAFCAEEKLLAERLGIDAYSLL---------------EEMASRVPvGSHGI--IPIFSD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 282 LQ--------AP--LN---DPCACasfmglkhstNKYHLVRAILESIAFRNKQLYDMLQReiqipVTNIRAD-----GGV 343
Cdd:PRK10939 355 VMrfkswyhaAPsfINlsiDPEKC----------NKATLFRALEENAAIVSACNLQQIAA-----FSGVFPSslvfaGGG 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961414 344 CNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWAD-KEELQKLRQSEMVFKPQ-KKWQEYEVNMENWVKA 420
Cdd:PRK10939 420 SKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSlAETGERLVRWERTFEPNpENHELYQEAKEKWQAV 498
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
270-383 |
3.21e-08 |
|
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: 55.71 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 270 SEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLV---RAILESIAFRNKQLYDMLQREiQIPVTNIRADGGVCNN 346
Cdd:cd07768 360 SIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTykyIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKN 438
|
90 100 110
....*....|....*....|....*....|....*..
gi 568961414 347 AFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 383
Cdd:cd07768 439 ERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAG 475
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
306-411 |
5.83e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 48.30 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 306 HLVRAILESIAFRNKQLYDMLQREiQIPVTNIRADGGVC-NNAFVMQMTSDLINEKIDRPAhFDMSC-LGAASLAGLAVG 383
Cdd:PRK04123 412 DIYRALIEATAFGTRAIMECFEDQ-GVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVA-SDQCPaLGAAIFAAVAAG 489
|
90 100 110
....*....|....*....|....*....|.
gi 568961414 384 FWADKEELQKLRQS--EMVFKPQ-KKWQEYE 411
Cdd:PRK04123 490 AYPDIPEAQQAMASpvEKTYQPDpENVARYE 520
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
273-410 |
6.67e-06 |
|
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: 48.30 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 273 VYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVR---AILESIAFRNKQLYDMLQrEIQIPVTNIRADGGVCNNAFV 349
Cdd:cd07782 381 LHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMN-AAGHKIDTIFMCGGLSKNPLF 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961414 350 MQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWAD-KEELQKLRQSEMVFKPQKKWQEY 410
Cdd:cd07782 460 VQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSlWDAMAAMSGPGKVVEPNEELKKY 521
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
280-381 |
7.90e-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: 38.54 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961414 280 SGLQAPLNDPCACASFMGLKHSTNKYHLVR---AILESIAFRNKQLYDMLQREiQIPVTNIRADGGVCNNAFVMQMTSDL 356
Cdd:cd07778 387 LGNRTPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKE-KIIIQKVVISGSQAKNARLLQLLSTV 465
|
90 100
....*....|....*....|....*..
gi 568961414 357 INE-KIDRPA-HFDMSCLGAASLAGLA 381
Cdd:cd07778 466 LSKiHIIVPLsDSKYAVVKGAALLGKA 492
|
|
| |
