|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
1-399 |
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: 551.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 1 MNWFSYALFLLTRQSRFLAGSVLQLMNGQVTPRLLFEIMNNKKLKQALMQKKARVELLDSWILHKLRTGSsrdkdvEHIT 80
Cdd:cd07793 120 LRGGSKFLHFLTRNKRFLAASVLKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGGK------VHAT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 81 DVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGyKGFGHVHPTAFGpdwanTEIPIAASLSDQTAAIWGSQCF 160
Cdd:cd07793 194 DYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTS-GDFGSTDPSIFG-----AEIPITAVVADQQAALFGECCF 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 161 QKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAWQFKKPTrqqgaVYCIEGASHDFGTVVTWAQSCELFDSPANTSDI 240
Cdd:cd07793 268 DKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEI-----TYLAEGNASDTGTVIDWAKSIGLFDDPSETEDI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 241 AQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGV 320
Cdd:cd07793 343 AESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGV 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24656372 321 SRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDLKRFRKVARVFEPRPkEYETIANRMDKWSRTI 399
Cdd:cd07793 423 SNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKM-DNEKREELYKNWKKAV 500
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
38-397 |
4.01e-105 |
|
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: 319.03 E-value: 4.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 38 IMNNKKLKQALMQKKARVELLDSWILHKLrTGSSRdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVV 117
Cdd:cd07769 141 LDNVPGARERAERGELLFGTIDTWLIWKL-TGGKV-----HVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 118 DNGYKgFGHVHPTAFGpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAWQ 197
Cdd:cd07769 215 PSSEV-FGYTDPEGLG-----AGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 198 FKKPTrqqgaVYCIEGASHDFGTVVTWA-QSCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDyRSASG-FIGL 275
Cdd:cd07769 289 IGGKV-----TYALEGSIFIAGAAIQWLrDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWD-PDARGaIVGL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 276 TPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMA 355
Cdd:cd07769 363 TRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLA 442
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24656372 356 GINLGIWRDVNDLKRFRKVARVFEPRpKEYETIANRMDKWSR 397
Cdd:cd07769 443 GLAVGFWKDLDELASLWQVDKRFEPS-MDEEERERLYRGWKK 483
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
56-405 |
6.91e-100 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 305.83 E-value: 6.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 56 ELL----DSWILHKLrTGSSRdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGYkGFGHVHPTA 131
Cdd:COG0554 158 ELLfgtiDSWLIWKL-TGGKV-----HVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSE-VFGETDPDL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 132 FGpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAWQFK-KPTrqqgavYC 210
Cdd:COG0554 231 FG-----AEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGgKVT------YA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 211 IEGAShdF--GTVVTW-AQSCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDyRSASG-FIGLTPSTTKAHMVR 286
Cdd:COG0554 300 LEGSI--FvaGAAVQWlRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWD-PDARGaIFGLTRGTTRAHIAR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 287 ALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVN 366
Cdd:COG0554 377 AALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLE 456
|
330 340 350
....*....|....*....|....*....|....*....
gi 24656372 367 DLKRFRKVARVFEPRPKEyETIANRMDKWSRTIARFSDW 405
Cdd:COG0554 457 ELAALWKVDRRFEPQMDE-EERERLYAGWKKAVERTLGW 494
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
59-395 |
2.95e-89 |
|
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: 278.22 E-value: 2.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 59 DSWILHKLRTGSSrdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGYKgFGHVHPTAFGpdwan 138
Cdd:cd07786 162 DSWLIWKLTGGKV------HATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEV-FGYTDPDLLG----- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 139 TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAWQFKKPTrqqgaVYCIEGASHDF 218
Cdd:cd07786 230 AEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKV-----TYALEGSIFIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 219 GTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLV 297
Cdd:cd07786 305 GAAVQWLRdGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 298 QLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDLKRFRKVARV 377
Cdd:cd07786 385 DLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRR 464
|
330
....*....|....*...
gi 24656372 378 FEPRPKEyETIANRMDKW 395
Cdd:cd07786 465 FEPSMSE-EEREALYAGW 481
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
33-405 |
1.70e-84 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 266.45 E-value: 1.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 33 RLLFEimNNKKLKQALMQKKARVELLDSWILHKLRTGSSrdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKI 112
Cdd:PTZ00294 143 RWMLE--NVPAVKDAVKEGTLLFGTIDTWLIWNLTGGKS------HVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKET 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 113 LPRVVDNGYKgFGHVHPTAFGPdwaNTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYP 192
Cdd:PTZ00294 215 LPEIKSSSEN-FGTISGEAVPL---LEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 193 LVAWQFKKPTRqqgAVYCIEGASHDFGTVVTWAQS-CELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASG 271
Cdd:PTZ00294 291 TVCYQLGPNGP---TVYALEGSIAVAGAGVEWLRDnMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 272 FIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGA 351
Cdd:PTZ00294 368 IVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGA 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24656372 352 TFMAGINLGIWRDVNDLKRF-RKVARVFEPRPKEYETiANRMDKWSRTIARFSDW 405
Cdd:PTZ00294 448 ALLAGLAVGVWKSLEEVKKLiRRSNSTFSPQMSAEER-KAIYKEWNKAVERSLKW 501
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
40-401 |
5.57e-75 |
|
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: 241.66 E-value: 5.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 40 NNKKLKQALMQKKARVELLDSWILHKLrTGssRDKDVEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDN 119
Cdd:cd07792 149 NVPEVKKAVDDGRLLFGTVDSWLIWNL-TG--GKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 120 GYKgFGHVHPTAFgpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCqaVIS--GMYPLVAWQ 197
Cdd:cd07792 226 SEV-YGKIASGPL------AGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEP--VFSkhGLLTTVAYK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 198 FKkptRQQGAVYCIEGASHDFGTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPvndY-RS-ASGFI- 273
Cdd:cd07792 297 LG---PDAPPVYALEGSIAIAGAAVQWLRdNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAP---YwRPdARGTIv 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 274 GLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATF 353
Cdd:cd07792 371 GLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAI 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24656372 354 MAGINLGIWRDVNDLKRFRKVAR-VFEPRPKEYETiANRMDKWSRTIAR 401
Cdd:cd07792 451 AAGLAVGVWKSLDELKSLNEGGRtVFEPQISEEER-ERRYKRWKKAVER 498
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
50-405 |
2.27e-73 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 237.41 E-value: 2.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 50 QKKA-RVELL----DSWILHKLRTGSSrdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGyKGF 124
Cdd:PRK00047 153 RERAeKGELLfgtiDTWLVWKLTGGKV------HVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSS-EVY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 125 GHVHPTAFGpdwaNTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDrcQAVIS--GMYPLVAWQFKKPt 202
Cdd:PRK00047 226 GKTNPYGFF----GGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGE--KAVKSenGLLTTIAWGIDGK- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 203 rqqgAVYCIEGASHDFGTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDyRSASGFI-GLTPSTT 280
Cdd:PRK00047 299 ----VVYALEGSIFVAGSAIQWLRdGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWD-SDARGAIfGLTRGTT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 281 KAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLG 360
Cdd:PRK00047 374 KEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVG 453
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24656372 361 IWRDVNDLKRFRKVARVFEPRPKEyETIANRMDKWSRTIARFSDW 405
Cdd:PRK00047 454 FWKDLDELKEQWKIDRRFEPQMDE-EEREKLYAGWKKAVKRTLAW 497
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
33-405 |
2.82e-62 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 208.78 E-value: 2.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 33 RLLFEIMNNKKLKQALMQKKARVELLDSWILHKLrTGSSrdKDVEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKI 112
Cdd:PLN02295 142 KLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNL-TGGA--SGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 113 LPRVVDNGYKgFGHVhptafGPDWANTEIPIAASLSDQTAAIWGSQCfQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYP 192
Cdd:PLN02295 219 LPKIVSNSEV-IGTI-----AKGWPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 193 LVAWQF--KKPTRqqgavYCIEGASHDFGTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPvnDYRS- 268
Cdd:PLN02295 292 TVAYKLgpDAPTN-----YALEGSVAIAGAAVQWLRdNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAP--RWRDd 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 269 ASG-FIGLTPSTTKAHMVRALLESIVFRLVQLIEA-----AEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERAD 342
Cdd:PLN02295 365 ARGvCVGITRFTNKAHIARAVLESMCFQVKDVLDAmrkdaGEEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPA 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656372 343 NAESSIMGATFMAGINLGIWRDVNDLK-RFRKVARVFEPRPKEyETIANRMDKWSRTIARFSDW 405
Cdd:PLN02295 445 DIETTALGAAYAAGLAVGLWTEEEIFAsEKWKNTTTFRPKLDE-EERAKRYASWCKAVERSFDL 507
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
53-383 |
1.32e-48 |
|
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: 170.78 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 53 ARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGYKGfGHVHPTA- 131
Cdd:cd07779 104 AKFLTVQDYLLYRL-TG-------EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVI-GTLTKEAa 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 132 --FG-PdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAwqfkkptrqqgAV 208
Cdd:cd07779 175 eeTGlP----EGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPS-----------AV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 209 ---YCIEGASHDFGTVVTWAqsCELFDSPAN-------------TSDIAQSVPDTNDVFFMPAFSG-LGPPVNDYRSASg 271
Cdd:cd07779 240 pgkWVLEGSINTGGSAVRWF--RDEFGQDEVaekelgvspyellNEEAAKSPPGSDGLLFLPYLAGaGTPYWNPEARGA- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 272 FIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETsQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGA 351
Cdd:cd07779 317 FIGLTLSHTRAHLARAILEGIAFELRDNLEAMEKAG-VPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGA 395
|
330 340 350
....*....|....*....|....*....|...
gi 24656372 352 TFMAGINLGIWRDVND-LKRFRKVARVFEPRPK 383
Cdd:cd07779 396 AILAAVGAGIYPDFEEaVKAMVRVTDTFEPDPE 428
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
53-406 |
9.54e-48 |
|
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: 169.63 E-value: 9.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 53 ARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISwLFGINSKILPRVVDNGYKgFGHVHPta 131
Cdd:COG1070 152 AKVLLPKDYLRYRL-TG-------EFVTDYSDASGTGLLDVRTRDWSDeLLE-ALGIDRELLPELVPPGEV-AGTLTA-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 132 fgpDWAN-----TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgDRCQAVISGMYPLVAWQFKkptrqqG 206
Cdd:COG1070 220 ---EAAAetglpAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVP------G 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 207 AvYCIEGASHDFGTVVTWAqsCELFDSPAN------TSDIAQSVPDTNDVFFMPAFSGLGPPVNDyRSASG-FIGLTPST 279
Cdd:COG1070 290 R-WLPMGATNNGGSALRWF--RDLFADGELddyeelNALAAEVPPGADGLLFLPYLSGERTPHWD-PNARGaFFGLTLSH 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 280 TKAHMVRALLESIVFRLVQLIEAAEkETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINL 359
Cdd:COG1070 366 TRAHLARAVLEGVAFALRDGLEALE-EAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGL 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24656372 360 GIWRDVND-LKRFRKVARVFEPRPKEYETIANRMDKWSRTIARFSDWY 406
Cdd:COG1070 445 GLYDDLEEaAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKPLF 492
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
60-397 |
3.84e-42 |
|
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: 154.25 E-value: 3.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 60 SWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISWLfGINSKILPRVVDngykgFGHVHPTAfGPDWAN 138
Cdd:cd07770 156 EYLLYRL-TG-------ELVTDYSTASGTGLLNIHTLDWDEeALELL-GIDEEQLPELVD-----PTEVLPGL-KPEFAE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 139 -----TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDR---------CQAVISGMYplvawqfkkptrq 204
Cdd:cd07770 221 rlgllAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPvldppgrlwCYRLDENRW------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 205 qgavyCIEGASHDFGTVVTWAQScELFDSPANTSDI----AQSVPDTNDVFFMPAFSGLGPPV-NDYRSASgFIGLTPST 279
Cdd:cd07770 288 -----LVGGAINNGGNVLDWLRD-TLLLSGDDYEELdklaEAVPPGSHGLIFLPYLAGERAPGwNPDARGA-FFGLTLNH 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 280 TKAHMVRALLESIVFRLVQLIEAAEkETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINL 359
Cdd:cd07770 361 TRADILRAVLEGVAFNLKSIYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEAL 439
|
330 340 350
....*....|....*....|....*....|....*...
gi 24656372 360 GIWRDVnDLKRFRKVARVFEPRPKEYETIANRMDKWSR 397
Cdd:cd07770 440 GLISSL-EADELVKIGKVVEPDPENHAIYAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
51-406 |
2.49e-40 |
|
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: 149.23 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 51 KKARVELL--DsWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDnGYKGFGHVH 128
Cdd:cd07808 147 ARIRKILLpkD-YLRYRL-TG-------ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVE-STEIVGTLT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 129 PTA---FGpdwANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgDRCQAVisgmYPLVAWQFKKPTRQQ 205
Cdd:cd07808 217 PEAaeeLG---LPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPD----PKGRLHTFPHAVPGK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 206 gavYCIEGASHDFGTVVTWAqsCELFDSPANT-----SDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTT 280
Cdd:cd07808 289 ---WYAMGVTLSAGLSLRWL--RDLFGPDRESfdeldAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 281 KAHMVRALLESIVFRLVQLIEAAeKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLG 360
Cdd:cd07808 364 RAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAG 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24656372 361 IWRDVND-LKRFRKVARVFEPRPkeyetiaNRMDKWSRTIARFSDWY 406
Cdd:cd07808 443 VFDDLEEaAAACIKIEKTIEPDP-------ERHEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
57-386 |
3.84e-40 |
|
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: 148.82 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 57 LLDS--WILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISwLFGINSKILPRVVDNGYKgFGHVHPTAfg 133
Cdd:cd07805 154 FLDAkdYLNFRL-TG-------RAATDPSTASTTGLMDLRKRRWSEeLLR-AAGIDPDKLPELVPSTEV-VGELTPEA-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 134 pdwAN-----TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRC----------QAVISGMYPLVAwqf 198
Cdd:cd07805 222 ---AAelglpAGTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKtdpdhgiftlASADPGRYLLAA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 199 kkptRQQGAvycieGASHDfgtvvtWAQSCELFDSPANTSD-------IAQSVPDTNDVFFMPAFSGLGPPVNDYRSASG 271
Cdd:cd07805 296 ----EQETA-----GGALE------WARDNLGGDEDLGADDyelldelAAEAPPGSNGLLFLPWLNGERSPVEDPNARGA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 272 FIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETsQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNA-ESSIMG 350
Cdd:cd07805 361 FIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLT-RKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALG 439
|
330 340 350
....*....|....*....|....*....|....*.
gi 24656372 351 ATFMAGINLGIWRDVNDLKRFRKVARVFEPRPKEYE 386
Cdd:cd07805 440 AALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRA 475
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
49-355 |
5.68e-37 |
|
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: 138.47 E-value: 5.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 49 MQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISWlFGINSKILPRVVdNGYKGFGHV 127
Cdd:cd00366 99 LDRRAKFLQPNDYIVFRL-TG-------EFAIDYSNASGTGLYDIKTGDWSEeLLDA-LGIPREKLPPIV-ESGEVVGRV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 128 HPTAfgpdwA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgDRCQA---VISGMYPLVawqfk 199
Cdd:cd00366 169 TPEA-----AeetglPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT-DEPVPpdpRLLNRCHVV----- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 200 kptrqqGAVYCIEGASHDFGTVVTWA--QSCELFDSPAN----TSDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFI 273
Cdd:cd00366 238 ------PGLWLLEGAINTGGASLRWFrdEFGEEEDSDAEyeglDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 274 GLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSqKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATF 353
Cdd:cd00366 312 GLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGV-KIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAI 390
|
..
gi 24656372 354 MA 355
Cdd:cd00366 391 LA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
57-360 |
1.77e-36 |
|
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: 138.10 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 57 LLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGYKGfGHVHPTAFGPDW 136
Cdd:cd07773 153 SVADYIAYRL-TG-------EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVI-GTVTPEAAEELG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 137 ANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTG-AFLNLVTGDRCQAVISGMYPLVAWQFKkptrqqGAVYCIeGAS 215
Cdd:cd07773 224 LPAGTPVVVGGHDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVP------GGYYYL-AGS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 216 HDFGTVVTWAQS--CELFDSPANTSDIAQSVPDT-NDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESI 292
Cdd:cd07773 297 LPGGALLEWFRDlfGGDESDLAAADELAEAAPPGpTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGL 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24656372 293 VFRLVQLIEAAEKETsQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLG 360
Cdd:cd07773 377 AFELRLNLEALEKAG-IPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
165-359 |
9.62e-30 |
|
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: 113.96 E-value: 9.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 165 VKVTMGTGAFLnLVTGDRCQAVISGMYPLVAWQFKKPtrqqgaVYCIEGASHDFGTVVTWA----QSCELFDSPANTSDI 240
Cdd:pfam02782 1 LAISAGTSSFV-LVETPEPVLSVHGVWGPYTNEMLPG------YWGLEGGQSAAGSLLAWLlqfhGLREELRDAGNVESL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 241 AQ-----SVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIR 315
Cdd:pfam02782 74 AElaalaAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24656372 316 VDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINL 359
Cdd:pfam02782 154 VSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
48-360 |
8.37e-26 |
|
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: 108.46 E-value: 8.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 48 LMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGYKgFGHV 127
Cdd:cd07798 146 IFERIATVLSISDWIGYRL-TG-------ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTV-LGTV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 128 HPtafgpDWA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTG----DRCQAVISGMYPLvawqf 198
Cdd:cd07798 217 SE-----EAArelglPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDepiiDPERRLWTGCHLV----- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 199 kkPTRqqgavYCIEGASHDFGTVVTWAQScELFDSPANTSD-----IAQSVPDTNDVFfmpafSGLGPPVNDYRSAS--- 270
Cdd:cd07798 287 --PGK-----WVLESNAGVTGLNYQWLKE-LLYGDPEDSYEvleeeASEIPPGANGVL-----AFLGPQIFDARLSGlkn 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 271 -GFIGLTP----STTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAE 345
Cdd:cd07798 354 gGFLFPTPlsasELTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGRE 433
|
330
....*....|....*
gi 24656372 346 SSIMGATFMAGINLG 360
Cdd:cd07798 434 ASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
61-357 |
7.54e-24 |
|
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: 102.30 E-value: 7.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 61 WILHKLrTGSsrdkdvEHITDVTSSTATGlYDPFTLSWSPLISWLFGINSKILPRVVDNGYKgFGHVHPTA---FG-Pdw 136
Cdd:cd07783 155 WLAGRL-TGD------RGVTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTV-IGTLTAEAaeeLGlP-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 137 anTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMY--PLVAwqfkkptrqqgAVYCIEGA 214
Cdd:cd07783 224 --AGTPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYshRHGD-----------GYWLVGGA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 215 SHDFGTVVTWAQSCELFDspANTSDIAQSVPDtnDVFFMPaFSGLGP--PVNDyRSASGFIgLTPSTTKAHMVRALLESI 292
Cdd:cd07783 291 SNTGGAVLRWFFSDDELA--ELSAQADPPGPS--GLIYYP-LPLRGErfPFWD-PDARGFL-LPRPHDRAEFLRALLEGI 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24656372 293 VFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSiMGATFMAGI 357
Cdd:cd07783 364 AFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAA-LGAALLAAA 427
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
61-360 |
8.92e-24 |
|
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: 102.24 E-value: 8.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 61 WILHKLrTGssrdkdvEHITDVTSSTaTGLYDPFTLSWSPLISWLFGIN--SKILPRVVDNGYKGfGHVHPTAfgpdwA- 137
Cdd:cd07802 159 WIRYRL-TG-------EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIA-GRVTAEA-----Aa 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 138 ----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTgAFLNLVTGDRcqavisgmyPLVAwqfkkPTRQQGAVYCIEG 213
Cdd:cd07802 224 ltglPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGT-WSINEVVTDE---------PVVP-----DSVGSNSLHADPG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 214 ------ASHDFGTVVTWAQScELFDSP--ANTSD-------IAQSVPDTNDVFFMPAFSGlgPPVNDYRSAsGFIGLTPS 278
Cdd:cd07802 289 lyliveASPTSASNLDWFLD-TLLGEEkeAGGSDydeldelIAAVPPGSSGVIFLPYLYG--SGANPNARG-GFFGLTAW 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 279 TTKAHMVRALLESIVFRLVQLIEAAEKETsqKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGIN 358
Cdd:cd07802 365 HTRAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVA 442
|
..
gi 24656372 359 LG 360
Cdd:cd07802 443 AG 444
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
59-360 |
7.27e-23 |
|
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: 99.91 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 59 DSWILHKLrTGssrdkdvEHITDVTS-STATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGyKGFGHVHPtafgpDWA 137
Cdd:cd07804 157 YDYIVYKL-TG-------EYVIDYSSaGNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPST-EIVGEVTK-----EAA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 138 -----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVIsgmYPLVAWQFKKPtrqqgavYCIE 212
Cdd:cd07804 223 eetglAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPR---LWLDYHDIPGT-------YVLN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 213 GASHDFGTVVTW-------AQSCELFDSPANTSDI----AQSVPDTND-VFFMPAFSGLGPPVNDyRSASG-FIGLTPST 279
Cdd:cd07804 293 GGMATSGSLLRWfrdefagEEVEAEKSGGDSAYDLldeeAEKIPPGSDgLIVLPYFMGERTPIWD-PDARGvIFGLTLSH 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 280 TKAHMVRALLESIVFRLVQLIEAAEkETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINL 359
Cdd:cd07804 372 TRAHLYRALLEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGV 450
|
.
gi 24656372 360 G 360
Cdd:cd07804 451 G 451
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
53-360 |
1.26e-17 |
|
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: 84.14 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 53 ARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLF---GINSKILPRVVDNGYKGfGHVHP 129
Cdd:cd07809 151 AKILLPHDYLNWKL-TG-------EKVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVA-GRLTP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 130 TA---FGpdwANTEIPIAASLSDQ-TAAIwGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYP----LVAWqfkkp 201
Cdd:cd07809 222 EGaeeLG---LPAGIPVAPGEGDNmTGAL-GTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATfcdsTGGM----- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 202 trqqgaVYCIEGAShDFGTVVTWAqsCELFDSPANTSD--IAQSVPDTNDVFFMPAFSGlgPPVNDYRSASG-FIGLTPS 278
Cdd:cd07809 293 ------LPLINTTN-CLTAWTELF--RELLGVSYEELDelAAQAPPGAGGLLLLPFLNG--ERTPNLPHGRAsLVGLTLS 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 279 -TTKAHMVRALLESIVFRL---VQLIEAAEKETSQklhmIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFM 354
Cdd:cd07809 362 nFTRANLARAALEGATFGLrygLDILRELGVEIDE----IRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQ 437
|
....*.
gi 24656372 355 AGINLG 360
Cdd:cd07809 438 AAWGAG 443
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
32-395 |
3.22e-17 |
|
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: 83.15 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 32 PRLLFeIMNNKKlkqALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSK 111
Cdd:cd07775 136 PRLLW-LKNNRP---EIYRKAAKITMLSDWIAYKL-SG-------ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 112 ILPRVVDNGYKgFGHVHPTAFGPDWANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTgaF----LNL---VTGDRCQ 184
Cdd:cd07775 204 ILPPVVESGTV-IGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGS--FwqqeVNTaapVTDPAMN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 185 -----AVISGMyplvaWQFkkptrqqgavyciEGASHDFGTVVTW---AQSCEL--------FDSPANTSDIAQSVPdTN 248
Cdd:cd07775 281 irvncHVIPDM-----WQA-------------EGISFFPGLVMRWfrdAFCAEEkeiaerlgIDAYDLLEEMAKDVP-PG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 249 DVFFMPAFSGLGPPVNDYRSASGFIGLT---PSTTKAHMVRALLES--IVFRL-VQLIEAAekeTSQKLHMIRVDGGVSR 322
Cdd:cd07775 342 SYGIMPIFSDVMNYKNWRHAAPSFLNLDidpEKCNKATFFRAIMENaaIVSAGnLERIAEF---SGIFPDSLVFAGGASK 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656372 323 NDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVND-LKRFRKVARVFEPRPKEYETIANRMDKW 395
Cdd:cd07775 419 GKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEaVESLVKWEREYLPNPENHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
80-376 |
1.51e-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: 81.04 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 80 TDVTSSTATGLYDPFTLSWS-PLISWLfGINSKILPRVVDNGyKGFGHVHPTaFGPDWANTEIPIAASLSDQTA-AIWGS 157
Cdd:cd07771 168 AEYTIASTTQLLDPRTKDWSeELLEKL-GLPRDLFPPIVPPG-TVLGTLKPE-VAEELGLKGIPVIAVASHDTAsAVAAV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 158 QCFQKNDVKVTMGT----GAFLN--LVTGDRCQA----------------VISGMYPL----VAWQfkkptrqqgavycI 211
Cdd:cd07771 245 PAEDEDAAFISSGTwsliGVELDepVITEEAFEAgftneggadgtirllkNITGLWLLqecrREWE-------------E 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 212 EGASHDFGTVVTWAQSCELFDSPANTSDiaqsvpdtnDVFF----MPAFsglgppVNDYrsaSGFIGLTPSTTKAHMVRA 287
Cdd:cd07771 312 EGKDYSYDELVALAEEAPPFGAFIDPDD---------PRFLnpgdMPEA------IRAY---CRETGQPVPESPGEIARC 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 288 LLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVeRADNAESSIMGATFMAGINLGiwrDVND 367
Cdd:cd07771 374 IYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPV-IAGPVEATAIGNLLVQLIALG---EIKS 449
|
....*....
gi 24656372 368 LKRFRKVAR 376
Cdd:cd07771 450 LEEGRELVR 458
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
238-360 |
2.11e-15 |
|
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: 77.66 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 238 SDIAQSVPDTNDVFFMPAFSGLG---PPVNDYRSASgFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAeketSQKLHMI 314
Cdd:cd24121 332 ELAASSPPGAEGVLYHPYLSPAGeraPFVNPNARAQ-FTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGEL 406
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24656372 315 RVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLG 360
Cdd:cd24121 407 RLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
55-388 |
2.00e-14 |
|
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: 74.88 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 55 VELLDsWILHKLrTGssrdkdvehiTDVTSSTATG---LYDPFTLSWS--------PLiswLFGINSKILPRVVDNGyKG 123
Cdd:cd07781 159 VEACD-WINARL-TG----------RWVRSRCAAGhkwMYNEWGGGPPreflaaldPG---LLKLREKLPGEVVPVG-EP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 124 FGHVHPtafgpDWA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTgAFLNLVTGDRCQAV--ISGMYPlvaw 196
Cdd:cd07781 223 AGTLTA-----EAAerlglPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGT-STCHLMVSPKPVDIpgICGPVP---- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 197 qfkkptrqqGAV----YCIEGASHDFGTVVTWAqsCELFDSPANT---------SDIAQSV-PDTNDVFFMPAFSGLGPP 262
Cdd:cd07781 293 ---------DAVvpglYGLEAGQSAVGDIFAWF--VRLFVPPAEErgdsiyallSEEAAKLpPGESGLVALDWFNGNRTP 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 263 VNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSqKLHMIRVDGGVS-RNDFVCQFLADLSRLRVERA 341
Cdd:cd07781 362 LVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGV-PVNRVVACGGIAeKNPLWMQIYADVLGRPIKVP 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24656372 342 DNAESSIMGATFMAGINLGIWRDVNDL-KRFRKVARVFEPRP---KEYETI 388
Cdd:cd07781 441 KSDQAPALGAAILAAVAAGVYADIEEAaDAMVRVDRVYEPDPenhAVYEEL 491
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
60-355 |
6.45e-13 |
|
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: 69.94 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 60 SWILHKLrTGSSrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISWLfGINSKILPRVVDNGyKGFGHVHPTAfgpdwaN 138
Cdd:cd07777 156 DYIVARL-TGLP-----KPVMHPTNAASWGLFDLETGTWNKdLLEAL-GLPVILLPEIVPSG-EIVGTLSSAL------P 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 139 TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgdrCQAVISGMY---PlvawqFKKPTrqqgavYCIEGAS 215
Cdd:cd07777 222 KGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLT---PKFELSGSVeirP-----FFDGR------YLLVAAS 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 216 --------HDFGTVVTWAQscELFDSPANT---SDIAQSVP--DTNDVFFMPAFSGlgpPVNDYRSASGFIGLTPSTTK- 281
Cdd:cd07777 288 lpggralaVLVDFLREWLR--ELGGSLSDDeiwEKLDELAEseESSDLSVDPTFFG---ERHDPEGRGSITNIGESNFTl 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24656372 282 AHMVRALLESIVfrlVQLIEAAEKETSQKLHM--IRVDGGVSR-NDFVCQFLADLSRLRVERADNAESSIMGATFMA 355
Cdd:cd07777 363 GNLFRALCRGIA---ENLHEMLPRLDLDLSGIerIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
15-380 |
3.59e-10 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 61.58 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 15 SRFLAGSVLQLMNG--QVTPRLLFEIMNNKKLKQALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYD 92
Cdd:PRK10331 113 ERYISAQQLQQISGvgAFSFNTLYKLVWLKENHPQLLEQAHAWLFISSLINHRL-TG-------EFTTDITMAGTSQMLD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 93 PFTLSWSPLISWLFGINSKILPRVVDNGYKgFGHVHPTAFGPDWANTEIPIAASLSDQTAAIWGSQCfQKNDVKVTMGTG 172
Cdd:PRK10331 185 IQQRDFSPEILQATGLSRRLFPRLVEAGEQ-IGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSGA-GQNQPVLSSGTW 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 173 AFLNLvtgdRCQAVISgmyplvAWQFkkptRQQGAVYCIEGASHDFGTVVTWAQSC------ELFDSPANTSDI----AQ 242
Cdd:PRK10331 263 EILMV----RSAQVDT------SLLS----QYAGSTCELDSQSGLYNPGMQWLASGvlewvrKLFWTAETPYQTmieeAR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 243 SVPD-TNDVFFMPAFSGLGppvndyrsASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVS 321
Cdd:PRK10331 329 AIPPgADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGS 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 322 RNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDLK-RFRKVARVFEP 380
Cdd:PRK10331 401 RNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARaQMKYQYRYFYP 460
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
32-401 |
4.28e-09 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 58.09 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 32 PRLLFEimnnKKLKQALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSK 111
Cdd:PRK10939 139 PRLLWL----AHHRPDIYRQAHTITMISDWIAYML-SG-------ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRAD 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 112 ILPRVVDNGYKgFGHVHPTAFGPDWANTEIPIAASLSD--------------QTAAIWGSqcFQKNDVKVTMG-TGAFLN 176
Cdd:PRK10939 207 ILPPVKETGTV-LGHVTAKAAAETGLRAGTPVVMGGGDvqlgclglgvvrpgQTAVLGGT--FWQQVVNLPAPvTDPNMN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 177 LvtgdRCQA-VISGMyplvaWQFkkptrqqgavyciEGASHDFGTVVTWAQS--CEL---------FDSPANTSDIAQSV 244
Cdd:PRK10939 284 I----RINPhVIPGM-----VQA-------------ESISFFTGLTMRWFRDafCAEekllaerlgIDAYSLLEEMASRV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 245 P-DTNDVffMPAFSGLGPPVNDYRSASGFIGLT--PS-TTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGV 320
Cdd:PRK10939 342 PvGSHGI--IPIFSDVMRFKSWYHAAPSFINLSidPEkCNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 321 SRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDL-KRFRKVARVFEPRPKEYETIANRMDKWSRTI 399
Cdd:PRK10939 420 SKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETgERLVRWERTFEPNPENHELYQEAKEKWQAVY 499
|
..
gi 24656372 400 AR 401
Cdd:PRK10939 500 AD 501
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
50-156 |
3.08e-08 |
|
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: 54.27 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 50 QKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGYKgFGHVHP 129
Cdd:pfam00370 148 EKIHKFLTIHDYLRWRL-TG-------VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEI-YGELNP 218
|
90 100
....*....|....*....|....*..
gi 24656372 130 TAFGPDWANTEIPIAASLSDQTAAIWG 156
Cdd:pfam00370 219 ELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
14-368 |
3.56e-08 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 55.36 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 14 QSRFLAGSVLqlMNGQVTPRLLFEimnnKKLKQALMQKKARVELLDSWIlhKLR-TGssrdkdvEHITDVTSSTATGLYD 92
Cdd:PRK15027 114 QSRVITGNLM--MPGFTAPKLLWV----QRHEPEIFRQIDKVLLPKDYL--RLRmTG-------EFASDMSDAAGTMWLD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 93 PFTLSWSPLISWLFGINSKILPRVVDnGYKGFGHVHPtAFGPDWANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTg 172
Cdd:PRK15027 179 VAKRDWSDVMLQACHLSRDQMPALYE-GSEITGALLP-EVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 173 aflnlvtgdrcqaviSGMYPLVAWQF-KKPtrqqgavyciEGASHDFG----------TVVTWAQSC--------ELFDS 233
Cdd:PRK15027 256 ---------------SGVYFAVSEGFlSKP----------ESAVHSFChalpqrwhlmSVMLSAASCldwaakltGLSNV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 234 PANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEkETSQKLHM 313
Cdd:PRK15027 311 PALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQS 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24656372 314 IRVDGGVSRNDFVCQFLADLSRLRVE-RADNAESSIMGATFMAGINLGIWRDVNDL 368
Cdd:PRK15027 390 VTLIGGGARSEYWRQMLADISGQQLDyRTGGDVGPALGAARLAQIAANPEKSLIEL 445
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
247-386 |
2.43e-05 |
|
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: 46.37 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 247 TNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVR---ALLESIVFRLVQLIEAAEKEtSQKLHMIRVDGGVSRN 323
Cdd:cd07782 378 TRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAA-GHKIDTIFMCGGLSKN 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656372 324 DFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVND-LKRFRKVARVFEPRPKEYE 386
Cdd:cd07782 457 PLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDaMAAMSGPGKVVEPNEELKK 520
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
238-394 |
4.59e-05 |
|
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: 45.31 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 238 SDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTK---AHMVRALLESIVFRLVQLIEAAEKETSQkLHMI 314
Cdd:cd07768 351 RQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMlnlTYKYIAILEALAFGTRLIIDTFQNEGIH-IKEL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656372 315 RVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDL----KRFRKVARVFEPRPKEYETIAN 390
Cdd:cd07768 430 RASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQLADSIteadISNDRKSETFEPLAYRLGADYI 509
|
....
gi 24656372 391 RMDK 394
Cdd:cd07768 510 LLYK 513
|
|
| |
