|
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 ... |
14-428 |
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: 705.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 14 RKTGHHFHNFISWQDLRAAELVKSWNNSLIMKLLHGATRVLHFFSRSKVMLTVSRFNFSTQHATLRLTWILQNLSEVKRA 93
Cdd:cd07793 87 KKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLHFLTRNKRFLAASVLKFSTAHVSIRLLWILQNNPELKEA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 94 VEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIFGV 173
Cdd:cd07793 167 AEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 174 PIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELVCLAEGNAGDTGTAIMW 253
Cdd:cd07793 247 EIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASDTGTVIDW 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 254 AQKLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYDMLQ 333
Cdd:cd07793 327 AKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETME 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 334 REIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKLRQSEMVFKPQKKW 413
Cdd:cd07793 407 KETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKMDN 486
|
410
....*....|....*
gi 568961412 414 QEYEVNMENWVKAVK 428
Cdd:cd07793 487 EKREELYKNWKKAVK 501
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
14-428 |
3.33e-176 |
|
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: 501.61 E-value: 3.33e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 14 RKTGHHFHNFISWQDLRAAELVKSWNNSLIMKLLHGAT-RVLH-FFSRSKVMltvsrfnfstqhatlrltWILQNLSEVK 91
Cdd:cd07769 87 KKTGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTgLPLDpYFSATKIK------------------WILDNVPGAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 92 RAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIF 171
Cdd:cd07769 149 ERAERGELLFGTIDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 172 GVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELVCLAEGNAGDTGTAI 251
Cdd:cd07769 229 GAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFIAGAAI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 252 MWA-QKLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYD 330
Cdd:cd07769 309 QWLrDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 331 MLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKLRQSEMVFKPQ 410
Cdd:cd07769 389 AMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPS 468
|
410
....*....|....*...
gi 568961412 411 KKWQEYEVNMENWVKAVK 428
Cdd:cd07769 469 MDEEERERLYRGWKKAVE 486
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
14-433 |
5.97e-147 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 427.56 E-value: 5.97e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 14 RKTGHHFHNFISWQDLRAAELVKSWNNSlimkllHGATRVlhffsRSKVMLTVSRFnFStqhATlRLTWILQNLSEVKRA 93
Cdd:COG0554 90 RKTGKPLYNAIVWQDRRTADICEELKAD------GLEDLI-----REKTGLVLDPY-FS---AT-KIKWILDNVPGARER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 94 VEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIFGV 173
Cdd:COG0554 154 AEAGELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 174 PIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELVCLAEGNAGDTGTAIMW 253
Cdd:COG0554 234 EIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIFVAGAAVQW 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 254 -AQKLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYDML 332
Cdd:COG0554 314 lRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAM 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 333 QREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKLRQSEMVFKPQKK 412
Cdd:COG0554 394 EADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMD 473
|
410 420
....*....|....*....|.
gi 568961412 413 WQEYEVNMENWVKAVKRSMNW 433
Cdd:COG0554 474 EEERERLYAGWKKAVERTLGW 494
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
14-428 |
3.56e-132 |
|
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: 389.54 E-value: 3.56e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 14 RKTGHHFHNFISWQDLRAAELVKSWNNSLIMKLLHGAT-RVLH-FFSRSKVMltvsrfnfstqhatlrltWILQNLSEVK 91
Cdd:cd07786 87 RETGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTgLVLDpYFSATKIR------------------WILDNVPGAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 92 RAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIF 171
Cdd:cd07786 149 ERAERGELAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 172 GVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELV-CLaEGNAGDTGTA 250
Cdd:cd07786 229 GAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTyAL-EGSIFIAGAA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 251 IMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLY 329
Cdd:cd07786 308 VQWLRdGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 330 DMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKLRQSEMVFKP 409
Cdd:cd07786 388 EAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEP 467
|
410
....*....|....*....
gi 568961412 410 QKKWQEYEVNMENWVKAVK 428
Cdd:cd07786 468 SMSEEEREALYAGWKKAVK 486
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
14-433 |
2.23e-122 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 365.07 E-value: 2.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 14 RKTGHHFHNFISWQDLRAAELVKSWNNSlimkllHGATRvlHFfsRSKVMLTVSRFnFSTqhatLRLTWILQNLSEVKRA 93
Cdd:PTZ00294 91 KVTGKPLYNAIVWLDTRTYDIVNELTKK------YGGSN--FF--QKITGLPISTY-FSA----FKIRWMLENVPAVKDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 94 VEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIFG- 172
Cdd:PTZ00294 156 VKEGTLLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPl 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 173 -VPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELVCL--AEGNAGDTGT 249
Cdd:PTZ00294 236 lEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVyaLEGSIAVAGA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 250 AIMWAQK-LDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQL 328
Cdd:PTZ00294 316 GVEWLRDnMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDV 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 329 YDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKL-RQSEMVF 407
Cdd:PTZ00294 396 IESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLiRRSNSTF 475
|
410 420
....*....|....*....|....*.
gi 568961412 408 KPQKKWQEYEVNMENWVKAVKRSMNW 433
Cdd:PTZ00294 476 SPQMSAEERKAIYKEWNKAVERSLKW 501
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
14-433 |
6.63e-119 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 356.06 E-value: 6.63e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 14 RKTGHHFHNFISWQDLRAAELVKSWNNSLIMKLLHGATRVL--HFFSRSKVMltvsrfnfstqhatlrltWILQNLSEVK 91
Cdd:PRK00047 92 KETGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVidPYFSGTKIK------------------WILDNVEGAR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 92 RAVEEDNCCFGTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSV-DEKI 170
Cdd:PRK00047 154 ERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTnPYGF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 171 FGVPIPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELVCLAEGNAGDTGTA 250
Cdd:PRK00047 234 FGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFVAGSA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 251 IMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLY 329
Cdd:PRK00047 314 IQWLRdGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 330 DMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKLRQSEMVFKP 409
Cdd:PRK00047 394 DAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEP 473
|
410 420
....*....|....*....|....*.
gi 568961412 410 QkkWQEYEVN--MENWVKAVKRSMNW 433
Cdd:PRK00047 474 Q--MDEEEREklYAGWKKAVKRTLAW 497
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
14-430 |
3.86e-115 |
|
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: 346.43 E-value: 3.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 14 RKTGHHFHNFISWQDLRAAELVKSwnnsLIMKLLHGATRVlhffsRSKVMLTVSRFnFSTqhatLRLTWILQNLSEVKRA 93
Cdd:cd07792 91 KSTGKPLYNAIVWLDTRTSDTVEE----LSAKTPGGKDHF-----RKKTGLPISTY-FSA----VKLRWLLDNVPEVKKA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 94 VEEDNCCFGTIDTWLLYKLTKG---SSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI 170
Cdd:cd07792 157 VDDGRLLFGTVDSWLIWNLTGGkngGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 171 F-GVPIpvVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIG-QELVCLA-EGNAGDT 247
Cdd:cd07792 237 LaGVPI--SGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGpDAPPVYAlEGSIAIA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 248 GTAIMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNK 326
Cdd:cd07792 315 GAAVQWLRdNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 327 QLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQKLRQSEM- 405
Cdd:cd07792 395 EILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRt 474
|
410 420
....*....|....*....|....*
gi 568961412 406 VFKPQKKWQEYEVNMENWVKAVKRS 430
Cdd:cd07792 475 VFEPQISEEERERRYKRWKKAVERS 499
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
1-433 |
2.66e-94 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 293.14 E-value: 2.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 1 MTRRRECEApARRRKTGHHFHNFISWQDLRAAELVKSwnnslIMKLLHGATRvlHFfsRSKVMLTVSRFnFSTqhatLRL 80
Cdd:PLN02295 79 ITNQRETTV-AWSKSTGRPLYNAIVWMDSRTSSICRR-----LEKELSGGRK--HF--VETCGLPISTY-FSA----TKL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 81 TWILQNLSEVKRAVEEDNCCFGTIDTWLLYKLT---KGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVK 157
Cdd:PLN02295 144 LWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTggaSGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 158 DTSYNFGSVDEKIFGVPIPVVALVGDQQSAMFGECCfETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELV 237
Cdd:PLN02295 224 SNSEVIGTIAKGWPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAP 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 238 CL--AEGNAGDTGTAIMWAQ-KLDLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLV 314
Cdd:PLN02295 303 TNyaLEGSVAIAGAAVQWLRdNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 315 RAILESIAFRNKQLYDMLQREIQIPVTN-----IRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 389
Cdd:PLN02295 383 RAVLESMCFQVKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVG 462
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 568961412 390 FWADKEEL-QKLRQSEMVFKPQKKWQEYEVNMENWVKAVKRSMNW 433
Cdd:PLN02295 463 LWTEEEIFaSEKWKNTTTFRPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
21-429 |
1.68e-57 |
|
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: 196.59 E-value: 1.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 21 HNFISWQDLRAAELVKSWNNSLIMKLLHGAT--RVLHFFSRSKVMltvsrfnfstqhatlrltWILQNLSEVKRAVEedn 98
Cdd:COG1070 94 RPAILWNDTRAAAEAAELREELGEEALYEITgnPLHPGFTAPKLL------------------WLKENEPEIFARIA--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 99 cCFGTIDTWLLYKLTkGSsYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP- 174
Cdd:COG1070 153 -KVLLPKDYLRYRLT-GE-FVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAaaeTGLPa 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 175 -IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNG---GFYPLIGWKIGQELVCLAegnagdTGTA 250
Cdd:COG1070 230 gTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGrvhTFCHAVPGRWLPMGATNN------GGSA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 251 IMWAQKL---DLFTDAAETEKMALSLE-DSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNK 326
Cdd:COG1070 304 LRWFRDLfadGELDDYEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 327 QLYDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWAD-KEELQKLRQSEM 405
Cdd:COG1070 384 DGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDlEEAAAAMVRVGE 462
|
410 420
....*....|....*....|....*
gi 568961412 406 VFKPQKKWQE-YEVNMENWVKAVKR 429
Cdd:COG1070 463 TIEPDPENVAaYDELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
100-384 |
5.10e-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: 5.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 100 CFGTIDTWLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP-- 174
Cdd:cd00366 104 KFLQPNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAaeeTGLPag 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 175 IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGK---------NLQHVNGGFYpligwkigqelvcLAEGNAG 245
Cdd:cd00366 182 TPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEpvppdprllNRCHVVPGLW-------------LLEGAIN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 246 DTGTAIMWAqkLDLFTDAAETEKMALSLED--------SEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAI 317
Cdd:cd00366 249 TGGASLRWF--RDEFGEEEDSDAEYEGLDElaaevppgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAV 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961412 318 LESIAFrnkQLYDMLQ--REIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLA 384
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; ... |
101-415 |
1.20e-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: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 101 FGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--I 175
Cdd:cd07779 106 FLTVQDYLLYRLT--GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAaeeTGLPegT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 176 PVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFYPLIG-----WkigqelvcLAEGNAGDTGTA 250
Cdd:cd07779 184 PVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSavpgkW--------VLEGSINTGGSA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 251 IMWAQKLdLFTDAAETEKMALSLED------------SEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAIL 318
Cdd:cd07779 256 VRWFRDE-FGQDEVAEKELGVSPYEllneeaaksppgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAIL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 319 ESIAFrnkQLYDMLQ--REIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEE 396
Cdd:cd07779 335 EGIAF---ELRDNLEamEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEE 411
|
330 340
....*....|....*....|
gi 568961412 397 -LQKLRQSEMVFKPQKKWQE 415
Cdd:cd07779 412 aVKAMVRVTDTFEPDPENVA 431
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
21-389 |
1.53e-50 |
|
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: 177.01 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 21 HNFISWQDLRAAELVKSWNNSLIMKLLHGAT--RVLHFFSRSKVMltvsrfnfstqhatlrltWILQNLSEVKRAVeedn 98
Cdd:cd07773 91 GPAIVWFDPRGKEEAEELAERIGAEELYRITglPPSPMYSLAKLL------------------WLREHEPEIFAKA---- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 99 CCFGTIDTWLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP- 174
Cdd:cd07773 149 AKWLSVADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAaeeLGLPa 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 175 -IPVValVG--DQQSAMFGECCFETGDVKLTMGTG-TFLDINTGKNLQHVNGGFYPLIGWKIGQELVCLAEGNAGdtGTA 250
Cdd:cd07773 227 gTPVV--VGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGGYYYLAGSLPG--GAL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 251 IMWAQKL---DLFTDAAETEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQ 327
Cdd:cd07773 303 LEWFRDLfggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRL 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961412 328 LYDMLQReIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 389
Cdd:cd07773 383 NLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
107-417 |
5.55e-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: 5.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 107 WLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--IPVVALV 181
Cdd:cd07808 158 YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAaeeLGLPegTPVVAGA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 182 GDQQSAMFGECCFETGDVKLTMGT-GTFL------DINTGKNLQ---HVNGGFYPLIGwkigqelVCLAegnagdTGTAI 251
Cdd:cd07808 236 GDNAAAALGAGVVEPGDALISLGTsGVVFaptdkpVPDPKGRLHtfpHAVPGKWYAMG-------VTLS------AGLSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 252 MWAQKL--DLFTDAAETEKMAL-SLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQL 328
Cdd:cd07808 303 RWLRDLfgPDRESFDELDAEAAkVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 329 YDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEELQK-LRQSEMVF 407
Cdd:cd07808 383 LEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAaCIKIEKTI 461
|
330
....*....|.
gi 568961412 408 KPQKKWQE-YE 417
Cdd:cd07808 462 EPDPERHEaYD 472
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-417 |
5.46e-48 |
|
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: 171.16 E-value: 5.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 15 KTGHHFHNFISWQDLRAAELVKSwnnslIMKllhgatrvlHFFSRSKVMLTvSRFNFSTQHATLRLTWILQNLSEV-KRA 93
Cdd:cd07805 87 KDGNPLRNAIIWSDTRAAEEAEE-----IAG---------GLGGIEGYRLG-GGNPPSGKDPLAKILWLKENEPEIyAKT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 94 VeednCCFGTIDtWLLYKLTkGSsYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI--- 170
Cdd:cd07805 152 H----KFLDAKD-YLNFRLT-GR-AATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAaae 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 171 FGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGK----------NLQHVNGGFYpligwkigqeLVC 238
Cdd:cd07805 225 LGLPagTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKpktdpdhgifTLASADPGRY----------LLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 239 LAEGNAGdtgTAIMWA-----QKLDLFTDAAE--TEKMALSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKY 311
Cdd:cd07805 295 AEQETAG---GALEWArdnlgGDEDLGADDYEllDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 312 HLVRAILESIAFRNKQLYDMLQREIQiPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAH-FDMSCLGAASLAGLAVGF 390
Cdd:cd07805 372 DLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGL 450
|
410 420
....*....|....*....|....*...
gi 568961412 391 WADKEELQKLRQSEMVFKPQKKWQE-YE 417
Cdd:cd07805 451 LKSFDEAKALVKVEKVFEPDPENRArYD 478
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
24-416 |
2.31e-47 |
|
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: 169.27 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 24 ISWQDLRAAElvkswnnslIMKLLHGATRVLHFFSRSKVMLtvsrfnfstqHAT---LRLTWILQNLSEVKRAVeednCC 100
Cdd:cd07770 94 ITWADTRAAE---------EAERLRKEGDGSELYRRTGCPI----------HPMyplAKLLWLKEERPELFAKA----AK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 101 FGTIDTWLLYKLTKGssYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--I 175
Cdd:cd07770 151 FVSIKEYLLYRLTGE--LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFaerLGLLagT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 176 PVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGF--YPLIG--WKIGqelvclaeG---NAGDtg 248
Cdd:cd07770 229 PVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLwcYRLDEnrWLVG--------GainNGGN-- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 249 tAIMWAQK--LDLFTDAAETEKMALSLE-DSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRN 325
Cdd:cd07770 299 -VLDWLRDtlLLSGDDYEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 326 KQLYDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKeELQKLRQSEM 405
Cdd:cd07770 378 KSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL-EADELVKIGK 455
|
410
....*....|.
gi 568961412 406 VFKPQKKWQEY 416
Cdd:cd07770 456 VVEPDPENHAI 466
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
21-389 |
1.99e-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: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 21 HNFISWQDLRAAELVKsWNNSLImkllhGATRVLHffsrskvmLTVSRFNfsTQHATLRLTWILQNLSEV-KRAVEednc 99
Cdd:cd07804 93 RPAILYGDRRATEEIE-WLNENI-----GEDRIFE--------ITGNPLD--SQSVGPKLLWIKRNEPEVfKKTRK---- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 100 cFGTIDTWLLYKLTkgSSYATDYSNAS-TTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP- 174
Cdd:cd07804 153 -FLGAYDYIVYKLT--GEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAaeeTGLAe 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 175 -IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQ--------HVNGGFY----------PLIGW---KI 232
Cdd:cd07804 230 gTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTdprlwldyHDIPGTYvlnggmatsgSLLRWfrdEF 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 233 GQELVClAEGNAGDTGtaimwaqkLDLFTDAAETekmalSLEDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYH 312
Cdd:cd07804 310 AGEEVE-AEKSGGDSA--------YDLLDEEAEK-----IPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAH 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961412 313 LVRAILESIAFRNKQLYDMLqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 389
Cdd:cd07804 376 LYRALLEGVAYGLRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
21-388 |
1.91e-34 |
|
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: 133.12 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 21 HNFISWQDLRAAELVKSWNNSLIMKLLHGATRVLHFFSRSKVMltvsrfnfstqhatlrltWILQNLSEVKRAVeednCC 100
Cdd:cd07783 91 RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLL------------------WLKRHEPEVLAKT----AK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 101 FGTIDTWLLYKLTkGSSYATDYSNASTTGFfDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--I 175
Cdd:cd07783 149 FLHQADWLAGRLT-GDRGVTDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAaeeLGLPagT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 176 PVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHVNGGFY--PLIgwkIGQELVclaeGNAGDTGTAImw 253
Cdd:cd07783 227 PVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYshRHG---DGYWLV----GGASNTGGAV-- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 254 aqkLDLFTDAAETEKMA--LSLEDSEGVYFVP-SFSGLQAPLNDPCACASFMGLKHstNKYHLVRAILESIAFRNKQLYD 330
Cdd:cd07783 298 ---LRWFFSDDELAELSaqADPPGPSGLIYYPlPLRGERFPFWDPDARGFLLPRPH--DRAEFLRALLEGIAFIERLGYE 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961412 331 MLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHfDMSCLGAASLAGLAV 388
Cdd:cd07783 373 RLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
24-389 |
2.63e-31 |
|
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: 124.59 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 24 ISWQDLRAAELVKSWNNSLIMKLLHGATRvLHFFSRSKVMLtvsrfnfstqhatlrLTWILQNLSEV-KRAveednccfG 102
Cdd:cd07802 96 ILSNDSRAADIVDRWEEDGTLEKVYPLTG-QPLWPGQPVAL---------------LRWLKENEPERyDRI--------R 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 103 TI----DtWLLYKLTkGSsYATDYSNASTtGFFDPYAMRWSRLITTMVSIP--LSILPPVKDTSYNFGSVDEKI---FGV 173
Cdd:cd07802 152 TVlfckD-WIRYRLT-GE-ISTDYTDAGS-SLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAaalTGL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 174 P--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTfldINTG--KNLQHVNGGF----YPLIGWKIgqelvcLAEGNAg 245
Cdd:cd07802 228 PegTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGsnslHADPGLYL------IVEASP- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 246 dTGTAIM-WAqkLDLFTDAAET----------EKMALSLEDSEGVYFVPSFSGlqAPLNdPCACASFMGLKHSTNKYHLV 314
Cdd:cd07802 298 -TSASNLdWF--LDTLLGEEKEaggsdydeldELIAAVPPGSSGVIFLPYLYG--SGAN-PNARGGFFGLTAWHTRAHLL 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961412 315 RAILESIAFRNKQLYDMLQREiqIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 389
Cdd:cd07802 372 RAVYEGIAFSHRDHLERLLVA--RKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
103-389 |
1.30e-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: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 103 TIDTWLLYKLTKgsSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI---FGVP--IPV 177
Cdd:cd07798 155 SISDWIGYRLTG--ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAareLGLPegTPV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 178 VALVGDQQSAMFGECCFETGDVKLTMGTGT---------FLDIN----TGKnlqHVNGGFYPLigwkigqelvclaEGNA 244
Cdd:cd07798 233 VVGGADTQCALLGSGAIEPGDIGIVAGTTTpvqmvtdepIIDPErrlwTGC---HLVPGKWVL-------------ESNA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 245 GDTGTAIMWAQKLdLFTDAAET-----EKMALSLEDSEGVYfvpSFSGLQAPlnDPCACA--------SFMGLKHSTNKY 311
Cdd:cd07798 297 GVTGLNYQWLKEL-LYGDPEDSyevleEEASEIPPGANGVL---AFLGPQIF--DARLSGlknggflfPTPLSASELTRG 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961412 312 HLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 389
Cdd:cd07798 371 DFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
199-387 |
8.33e-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: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 199 VKLTMGTGTFLDINTGKNLQHVNGGFYPLIGWKIGQELvcLAEGNAGDTGTAIMW----------AQKLDLFTDAAETEK 268
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEMLPGYW--GLEGGQSAAGSLLAWllqfhglreeLRDAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 269 MALSLeDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGG 348
Cdd:pfam02782 79 LAAVA-PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 568961412 349 VCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLA 387
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
22-190 |
7.09e-25 |
|
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: 102.42 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 22 NFISWQDLRAAELVKSWNNSLIMKLLHGATRVL--HFFSRSKvmltvsrfnfstqhatlrLTWILQNLSEVKRAVEednc 99
Cdd:pfam00370 94 NAILWKDRRTAEIVENLKEEGNNQKLYEITGLPiwPGFTLSK------------------LRWIKENEPEVFEKIH---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 100 CFGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIFG-----VP 174
Cdd:pfam00370 152 KFLTIHDYLRWRLT--GVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAmwgldEG 229
|
170
....*....|....*.
gi 568961412 175 IPVVALVGDQQSAMFG 190
Cdd:pfam00370 230 VPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
22-389 |
7.72e-25 |
|
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: 106.10 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 22 NFISWQDLRAAELvkswnNSLIMKLLHGATRVLHffsrskvmLTVSRFNFStqhATlRLTWILQNlsevkravEEDNccF 101
Cdd:cd07809 95 PAKLWCDTRTAPE-----AEELTEALGGKKCLLV--------GLNIPARFT---AS-KLLWLKEN--------EPEH--Y 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 102 GTIDT------WLLYKLTKGssYATDYSNASTTGFFDPYAMRWSRLIT---TMVSIPLSILPPVKDTSYNFGSVDEKI-- 170
Cdd:cd07809 148 ARIAKillphdYLNWKLTGE--KVTGLGDASGTFPIDPRTRDYDAELLaaiDPSRDLRDLLPEVLPAGEVAGRLTPEGae 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 171 -FGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQ----------HVNGGFYPLIgwkigqelv 237
Cdd:cd07809 226 eLGLPagIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSdphgrvatfcDSTGGMLPLI--------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 238 ClaegNAGDTGTAIMWAQKLdLFTDAAETEKMALSLE-DSEGVYFVPSFSGLQAPlNDPCACASFMGLKHS-TNKYHLVR 315
Cdd:cd07809 297 N----TTNCLTAWTELFREL-LGVSYEELDELAAQAPpGAGGLLLLPFLNGERTP-NLPHGRASLVGLTLSnFTRANLAR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961412 316 AILESIAFrnkQLYDMLQ--REIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 389
Cdd:cd07809 371 AALEGATF---GLRYGLDilRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
17-389 |
2.72e-23 |
|
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: 101.55 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 17 GHHFHNFISWQDLRAAELVKSWNNSLImkllhgATRVlhfFSRSKVMLtvsrfNFSTQHATLRltWILQNLSEVKRAVEE 96
Cdd:cd24121 89 GRPVRDAILWLDGRAADIVERWQADGI------AEAV---FEITGTGL-----FPGSQAAQLA--WLKENEPERLERART 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 97 DNCCFGtidtWLLYKLTkGSSyATDYSNASTTgFFDPYAMRWSRLITTMVSIP--LSILPPVKDTSYNFGSVDEKI---F 171
Cdd:cd24121 153 ALHCKD----WLFYKLT-GEI-ATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAaaaT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 172 GVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGT----GTFLD------INTGKNLQHVNGGFY----------PLIG 229
Cdd:cd24121 226 GLPagTPVVLGPFDVVATALGSGAIEPGDACSILGTtgvhEVVVDepdlepEGVGYTICLGVPGRWlramanmagtPNLD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 230 WKIGQelvclaegnAGDTGTAIMWAQKLDLFTDAaetEKMALSLE-DSEGVYFVPSFS--GLQAPLNDPCACASFMGLKH 306
Cdd:cd24121 306 WFLRE---------LGEVLKEGAEPAGSDLFQDL---EELAASSPpGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSL 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 307 STNKYHLVRAILESIAFRNKQLYdmlqREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGL 386
Cdd:cd24121 374 EHTRADLLRAVYEGVALAMRDCY----EHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAV 449
|
...
gi 568961412 387 AVG 389
Cdd:cd24121 450 ALG 452
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
22-384 |
1.02e-22 |
|
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: 99.60 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 22 NFISWQDLRAAElvkswnnsliMKLLHGATRVLHFFSRSKVMLtvsrfnfSTQHATLRLTWILQNlsevkRAVEEDNCCF 101
Cdd:cd07777 94 PLITWQDQRCSE----------EFLGGLSTYGEELLPKSGMRL-------KPGYGLATLFWLLRN-----GPLPSKADRA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 102 GTIDTWLLYKLTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKIfGVPIPVVALV 181
Cdd:cd07777 152 GTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSAL-PKGIPVYVAL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 182 GDQQSAMFGECCFETGDVKLTMGTGTFLDINTGKNLQHvnGGF--YPLIGwkiGQELVCLAEGNAGDTGTAIM-----WA 254
Cdd:cd07777 231 GDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELS--GSVeiRPFFD---GRYLLVAASLPGGRALAVLVdflreWL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 255 QKLDLFTDAAE-TEKM--ALSLEDSEGVYFVPSFSGLQaplNDPCACASFMGLKHSTNKY-HLVRAILESIAfrnKQLYD 330
Cdd:cd07777 306 RELGGSLSDDEiWEKLdeLAESEESSDLSVDPTFFGER---HDPEGRGSITNIGESNFTLgNLFRALCRGIA---ENLHE 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 568961412 331 MLQREI--QIPVTNIRADGGVCN-NAFVMQMTSDLINEKIDRPAHFDMSCLGAASLA 384
Cdd:cd07777 380 MLPRLDldLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
79-423 |
1.68e-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: 99.71 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 79 RLTWILQNLSEVKRAVeednCCFGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 158
Cdd:cd07775 137 RLLWLKNNRPEIYRKA----AKITMLSDWIAYKLS--GELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 159 TSYNFGSVDEKI---FGVP--IPVVALVGDQQSAMFGeccfeTGDVKLTMGT---GTF--LDINTG-------------- 214
Cdd:cd07775 211 SGTVIGKVTKEAaeeTGLKegTPVVVGGGDVQLGCLG-----LGVVRPGQTAvlgGSFwqQEVNTAapvtdpamnirvnc 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 215 ---KNLQHVNG-GFYP--LIGW---KIGQELVCLAEGNAGDTgtaimwaqkLDLFTDAAetekmALSLEDSEGVyfVPSF 285
Cdd:cd07775 286 hviPDMWQAEGiSFFPglVMRWfrdAFCAEEKEIAERLGIDA---------YDLLEEMA-----KDVPPGSYGI--MPIF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 286 SGLQAPLNDPCACASFMGL---KHSTNKYHLVRAILESIAFRNKQLYDMLQReiqipVTNIRAD-----GGVCNNAFVMQ 357
Cdd:cd07775 350 SDVMNYKNWRHAAPSFLNLdidPEKCNKATFFRAIMENAAIVSAGNLERIAE-----FSGIFPDslvfaGGASKGKLWCQ 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961412 358 MTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEE-LQKLRQSEMVFKPQKKWQE-YEVNMENW 423
Cdd:cd07775 425 ILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEaVESLVKWEREYLPNPENHEvYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
169-422 |
3.53e-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: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 169 KIFGVP--IPVVALVGDQQSAMFGECCFETGDVKLTMGTGTfLDINTGKNLQHVNG--GFYP------LIGWKIGQ---- 234
Cdd:cd07781 232 ERLGLPagIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTST-CHLMVSPKPVDIPGicGPVPdavvpgLYGLEAGQsavg 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 235 -------ELVCLAEGNAGDTgtaimwaqKLDLFTDAAETEKMalsleDSEGVYFVPSFSGLQAPLNDPCACASFMGLKHS 307
Cdd:cd07781 311 difawfvRLFVPPAEERGDS--------IYALLSEEAAKLPP-----GESGLVALDWFNGNRTPLVDPRLRGAIVGLTLG 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 308 TNKYHLVRAILESIAFRNKQLYDMLQREiQIPVTNIRADGGV-CNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGL 386
Cdd:cd07781 378 TTPAHIYRALLEATAFGTRAIIERFEEA-GVPVNRVVACGGIaEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAV 456
|
250 260 270
....*....|....*....|....*....|....*.
gi 568961412 387 AVGFWADKEELQKlrqsemVFKPQKKwqEYEVNMEN 422
Cdd:cd07781 457 AAGVYADIEEAAD------AMVRVDR--VYEPDPEN 484
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
100-364 |
2.98e-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: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 100 CFGTIDTWLL------YKLTkgSSYATDYSNASTTGFFDPYAMRWSR-LITTMvSIPLSILPPVKDTSYNFGSVDEKIF- 171
Cdd:cd07771 144 LLERADKLLMlpdllnYLLT--GEKVAEYTIASTTQLLDPRTKDWSEeLLEKL-GLPRDLFPPIVPPGTVLGTLKPEVAe 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 172 ---GVPIPVVALVG-DQQSAMFGECCFETGDVKLTMGT----GTFLD--INTGK-------NLQHVNGGFYPL---IGWK 231
Cdd:cd07771 221 elgLKGIPVIAVAShDTASAVAAVPAEDEDAAFISSGTwsliGVELDepVITEEafeagftNEGGADGTIRLLkniTGLW 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 232 IGQElvCLAEgnagdtgtaimWAQKlDLFTDAAETEKMALSLEDSEGVYFV--PSFsglQAPLNDPCACASFM---GLKH 306
Cdd:cd07771 301 LLQE--CRRE-----------WEEE-GKDYSYDELVALAEEAPPFGAFIDPddPRF---LNPGDMPEAIRAYCretGQPV 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961412 307 STNKYHLVRAILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLIN 364
Cdd:cd07771 364 PESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
79-397 |
2.86e-15 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 77.70 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 79 RLTWILQNLSEVkraveednccFGTIDTWLLYK----LTKGSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILP 154
Cdd:PRK15027 131 KLLWVQRHEPEI----------FRQIDKVLLPKdylrLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 155 PVKDTSYNFGSVDEKI---FGVP-IPVVALVGDQQSAMFGECCFETGDVKLTMGT-GTFLDINTG---KNLQHVNGGFYP 226
Cdd:PRK15027 201 ALYEGSEITGALLPEVakaWGMAtVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflsKPESAVHSFCHA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 227 LIG-WKIGQELVCLAegnagdtgTAIMWAQKLDLFTDAAETEKMALSLEDSEG-VYFVPSFSGLQAPLNDPCACASFMGL 304
Cdd:PRK15027 281 LPQrWHLMSVMLSAA--------SCLDWAAKLTGLSNVPALIAAAQQADESAEpVWFLPYLSGERTPHNNPQAKGVFFGL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 305 KHSTNKYHLVRAILESIAFRNKQLYDMLQrEIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMS-CLGAASL 383
Cdd:PRK15027 353 THQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARL 431
|
330
....*....|....
gi 568961412 384 AGLAVGFWADKEEL 397
Cdd:PRK15027 432 AQIAANPEKSLIEL 445
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
24-417 |
6.47e-13 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 70.06 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 24 ISWQDLRAAElvkswnnslIMKLLHGATRVLHFFSRSKVmltvSRFNFSTQHatlRLTWILQNLSEVKraveEDNCCFGT 103
Cdd:PRK10331 98 ISWKCPRTAA---------VMENIERYISAQQLQQISGV----GAFSFNTLY---KLVWLKENHPQLL----EQAHAWLF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 104 IDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKDTSYNFGSVDEKI-----FGVPIPVV 178
Cdd:PRK10331 158 ISSLINHRLT--GEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAaallgLPVGIPVI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 179 ALVGDQQSAMFGECCFETGDVkLTMGTGTFLDINTgknlQHVN------------------GGFYPLIGWkigqelvcLA 240
Cdd:PRK10331 236 SAGHDTQFALFGSGAGQNQPV-LSSGTWEILMVRS----AQVDtsllsqyagstceldsqsGLYNPGMQW--------LA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 241 EGnagdtgtAIMWAQKLdLFTDAAETEKM---ALSL-EDSEGVYFVPSFSGlqaplndpCACASFMGLKHSTNKYHLVRA 316
Cdd:PRK10331 303 SG-------VLEWVRKL-FWTAETPYQTMieeARAIpPGADGVKMQCDLLA--------CQNAGWQGVTLNTTRGHFYRA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 317 ILESIAFRNKQLYDMLQREIQIPVTNIRADGGVCNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWADKEE 396
Cdd:PRK10331 367 ALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQ 446
|
410 420
....*....|....*....|..
gi 568961412 397 LQ-KLRQSEMVFKPQKKWQEYE 417
Cdd:PRK10331 447 ARaQMKYQYRYFYPQTEPEFIE 468
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
79-426 |
4.52e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 67.72 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 79 RLTWILQNLSEVKRAVEEdnccFGTIDTWLLYKLTkgSSYATDYSNASTTGFFDPYAMRWSRLITTMVSIPLSILPPVKD 158
Cdd:PRK10939 140 RLLWLAHHRPDIYRQAHT----ITMISDWIAYMLS--GELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 159 TSYNFGSVDEKI-----FGVPIPVVALVGDQQSAMFGECCFETGDVkLTMGtGTFL-------------DINTGKNLQHV 220
Cdd:PRK10939 214 TGTVLGHVTAKAaaetgLRAGTPVVMGGGDVQLGCLGLGVVRPGQT-AVLG-GTFWqqvvnlpapvtdpNMNIRINPHVI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 221 NG-------GFYP--LIGW---KIGQELVCLAEGNAGDTGTAImwaqkldlftdaaetEKMALSLE-DSEGVyfVPSFSG 287
Cdd:PRK10939 292 PGmvqaesiSFFTglTMRWfrdAFCAEEKLLAERLGIDAYSLL---------------EEMASRVPvGSHGI--IPIFSD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 288 LQ--------AP--LN---DPCACasfmglkhstNKYHLVRAILESIAFRNKQLYDMLQReiqipVTNIRAD-----GGV 349
Cdd:PRK10939 355 VMrfkswyhaAPsfINlsiDPEKC----------NKATLFRALEENAAIVSACNLQQIAA-----FSGVFPSslvfaGGG 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961412 350 CNNAFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWAD-KEELQKLRQSEMVFKPQ-KKWQEYEVNMENWVKA 426
Cdd:PRK10939 420 SKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSlAETGERLVRWERTFEPNpENHELYQEAKEKWQAV 498
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
276-389 |
3.29e-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: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 276 SEGVYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLV---RAILESIAFRNKQLYDMLQREiQIPVTNIRADGGVCNN 352
Cdd:cd07768 360 SIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTykyIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKN 438
|
90 100 110
....*....|....*....|....*....|....*..
gi 568961412 353 AFVMQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVG 389
Cdd:cd07768 439 ERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAG 475
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
312-417 |
5.97e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 48.30 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 312 HLVRAILESIAFRNKQLYDMLQREiQIPVTNIRADGGVC-NNAFVMQMTSDLINEKIDRPAhFDMSC-LGAASLAGLAVG 389
Cdd:PRK04123 412 DIYRALIEATAFGTRAIMECFEDQ-GVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVA-SDQCPaLGAAIFAAVAAG 489
|
90 100 110
....*....|....*....|....*....|.
gi 568961412 390 FWADKEELQKLRQS--EMVFKPQ-KKWQEYE 417
Cdd:PRK04123 490 AYPDIPEAQQAMASpvEKTYQPDpENVARYE 520
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
279-416 |
6.83e-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: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 279 VYFVPSFSGLQAPLNDPCACASFMGLKHSTNKYHLVR---AILESIAFRNKQLYDMLQrEIQIPVTNIRADGGVCNNAFV 355
Cdd:cd07782 381 LHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMN-AAGHKIDTIFMCGGLSKNPLF 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961412 356 MQMTSDLINEKIDRPAHFDMSCLGAASLAGLAVGFWAD-KEELQKLRQSEMVFKPQKKWQEY 416
Cdd:cd07782 460 VQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSlWDAMAAMSGPGKVVEPNEELKKY 521
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
286-387 |
8.06e-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: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961412 286 SGLQAPLNDPCACASFMGLKHSTNKYHLVR---AILESIAFRNKQLYDMLQREiQIPVTNIRADGGVCNNAFVMQMTSDL 362
Cdd:cd07778 387 LGNRTPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKE-KIIIQKVVISGSQAKNARLLQLLSTV 465
|
90 100
....*....|....*....|....*..
gi 568961412 363 INE-KIDRPA-HFDMSCLGAASLAGLA 387
Cdd:cd07778 466 LSKiHIIVPLsDSKYAVVKGAALLGKA 492
|
|
| |
