|
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 ... |
32-549 |
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: 750.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRSGEYYHNFITWKDLRADELVDQWNASWTKSSMNWFSYALFLLTRQSRFLAGSVLQLMNGQVTPRLLFEIMNN 191
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLHFLTRNKRFLAASVLKFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 KKLKQALMQKKARVELLDSWILHKLRTGSsrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGy 271
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGK------VHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTS- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 272 KGFGHVHPTAFGpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAWQFKKP 351
Cdd:cd07793 234 GDFGSTDPSIFG-----AEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 352 TrqqgaVYCIEGASHDFGTVVTWAQSCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTK 431
Cdd:cd07793 309 I-----TYLAEGNASDTGTVIDWAKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 432 AHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGI 511
Cdd:cd07793 384 AHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGI 463
|
490 500 510
....*....|....*....|....*....|....*...
gi 21357867 512 WRDVNDLKRFRKVARVFEPRPkEYETIANRMDKWSRTI 549
Cdd:cd07793 464 WKSKEELKKLRKIEKIFEPKM-DNEKREELYKNWKKAV 500
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
32-547 |
1.13e-136 |
|
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: 405.31 E-value: 1.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRSGEYYHNFITWKDLRADELVDQWNASwtkssmnwfsyalfllTRQSRFLAGSVLQLmngqvTP-----RLLF 186
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK----------------GLEERIREKTGLPL-----DPyfsatKIKW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 187 EIMNNKKLKQALMQKKARVELLDSWILHKLrTGSSRdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRV 266
Cdd:cd07769 140 ILDNVPGARERAERGELLFGTIDTWLIWKL-TGGKV-----HVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 267 VDNGYKgFGHVHPTAFGpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAW 346
Cdd:cd07769 214 RPSSEV-FGYTDPEGLG-----AGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAW 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 347 QFKKPTrqqgaVYCIEGASHDFGTVVTWA-QSCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDyRSASG-FIG 424
Cdd:cd07769 288 QIGGKV-----TYALEGSIFIAGAAIQWLrDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWD-PDARGaIVG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 425 LTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFM 504
Cdd:cd07769 362 LTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYL 441
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 21357867 505 AGINLGIWRDVNDLKRFRKVARVFEPRPKEyETIANRMDKWSR 547
Cdd:cd07769 442 AGLAVGFWKDLDELASLWQVDKRFEPSMDE-EERERLYRGWKK 483
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
32-555 |
1.34e-127 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 382.49 E-value: 1.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:COG0554 4 YILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRSGEYYHNFITWKDLRADELVDQWNA-------------------SWTKssMNWfsyalflltrqsrflagsv 172
Cdd:COG0554 84 TTVVWDRKTGKPLYNAIVWQDRRTADICEELKAdgledlirektglvldpyfSATK--IKW------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 173 lqlmngqvtprllfeIMNNkkLKQAlmQKKA-RVELL----DSWILHKLrTGSSRdkdveHITDVTSSTATGLYDPFTLS 247
Cdd:COG0554 143 ---------------ILDN--VPGA--RERAeAGELLfgtiDSWLIWKL-TGGKV-----HVTDVTNASRTMLFNIHTLD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 248 WSPLISWLFGINSKILPRVVDNGYkGFGHVHPTAFGpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNL 327
Cdd:COG0554 198 WDDELLELFGIPRSMLPEVRPSSE-VFGETDPDLFG-----AEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLM 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 328 VTGDRCQAVISGMYPLVAWQFK-KPTrqqgavYCIEGASHDFGTVVTW-AQSCELFDSPANTSDIAQSVPDTNDVFFMPA 405
Cdd:COG0554 272 NTGDEPVRSKNGLLTTIAWGLGgKVT------YALEGSIFVAGAAVQWlRDGLGLIDSAAESEALARSVEDNGGVYFVPA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 406 FSGLGPPVNDyRSASG-FIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLS 484
Cdd:COG0554 346 FTGLGAPYWD-PDARGaIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADIL 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21357867 485 RLRVERADNAESSIMGATFMAGINLGIWRDVNDLKRFRKVARVFEPRPKEyETIANRMDKWSRTIARFSDW 555
Cdd:COG0554 425 GVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMDE-EERERLYAGWKKAVERTLGW 494
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
32-545 |
2.50e-113 |
|
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: 345.63 E-value: 2.50e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRSGEYYHNFITWKDLRADELVDQWNA-------------------SWTKssMNWfsyalflltrqsrflagsv 172
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAegheemirektglvldpyfSATK--IRW------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 173 lqlmngqvtprllfeIMNNKKLKQALMQKKarvELL----DSWILHKLRTGSSrdkdveHITDVTSSTATGLYDPFTLSW 248
Cdd:cd07786 140 ---------------ILDNVPGARERAERG---ELAfgtiDSWLIWKLTGGKV------HATDVTNASRTMLFNIHTLEW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 249 SPLISWLFGINSKILPRVVDNGYKgFGHVHPTAFGpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLV 328
Cdd:cd07786 196 DDELLELFGIPASMLPEVKPSSEV-FGYTDPDLLG-----AEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 329 TGDRCQAVISGMYPLVAWQFKKPTrqqgaVYCIEGASHDFGTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFS 407
Cdd:cd07786 270 TGEKPVRSKNGLLTTIAWQLGGKV-----TYALEGSIFIAGAAVQWLRdGLGLIESAAETEALARSVPDNGGVYFVPAFT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 408 GLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLR 487
Cdd:cd07786 345 GLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVP 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21357867 488 VERADNAESSIMGATFMAGINLGIWRDVNDLKRFRKVARVFEPRPKEyETIANRMDKW 545
Cdd:cd07786 425 VERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVDRRFEPSMSE-EEREALYAGW 481
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
33-555 |
2.81e-104 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 322.69 E-value: 2.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 33 ILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPP--DITCLTISTQR 110
Cdd:PTZ00294 4 IGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPsfKIKAIGITNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 111 CTFLTWDHRSGEYYHNFITWKDLRADELVDQWNASWTKSsmNWFSY--ALFLLTRQSRFlagsvlqlmngqvtpRLLFEI 188
Cdd:PTZ00294 84 ETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGS--NFFQKitGLPISTYFSAF---------------KIRWML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 189 MNNKKLKQALMQKKARVELLDSWILHKLRTGSSrdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVD 268
Cdd:PTZ00294 147 ENVPAVKDAVKEGTLLFGTIDTWLIWNLTGGKS------HVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 269 NGYKgFGHVHPTAFGPdwaNTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAWQF 348
Cdd:PTZ00294 221 SSEN-FGTISGEAVPL---LEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 349 KKPTRqqgAVYCIEGASHDFGTVVTWAQS-CELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTP 427
Cdd:PTZ00294 297 GPNGP---TVYALEGSIAVAGAGVEWLRDnMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 428 STTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGI 507
Cdd:PTZ00294 374 KTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGL 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 21357867 508 NLGIWRDVNDLKRF-RKVARVFEPRPKEYETiANRMDKWSRTIARFSDW 555
Cdd:PTZ00294 454 AVGVWKSLEEVKKLiRRSNSTFSPQMSAEER-KAIYKEWNKAVERSLKW 501
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
32-551 |
1.13e-93 |
|
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: 295.20 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQ---LTPPDITCLTIST 108
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKalgISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 109 QRCTFLTWDHRSGEYYHNFITWKDLRADELVDQWNASWTKSSM-----------NWFSyALFLltrqsrflagsvlqlmn 177
Cdd:cd07792 82 QRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDhfrkktglpisTYFS-AVKL----------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 178 gqvtpRLLFEimNNKKLKQALMQKKARVELLDSWILHKLrTGssRDKDVEHITDVTSSTATGLYDPFTLSWSPLISWLFG 257
Cdd:cd07792 144 -----RWLLD--NVPEVKKAVDDGRLLFGTVDSWLIWNL-TG--GKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 258 INSKILPRVVDNGYKgFGHVHPTAFgpdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCqaVI 337
Cdd:cd07792 214 IPMSILPEIRSSSEV-YGKIASGPL------AGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEP--VF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 338 S--GMYPLVAWQFKkptRQQGAVYCIEGASHDFGTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPvn 414
Cdd:cd07792 285 SkhGLLTTVAYKLG---PDAPPVYALEGSIAIAGAAVQWLRdNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAP-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 415 dY-RS-ASGFI-GLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERA 491
Cdd:cd07792 360 -YwRPdARGTIvGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERP 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21357867 492 DNAESSIMGATFMAGINLGIWRDVNDLKRFRKVAR-VFEPRPKEYETiANRMDKWSRTIAR 551
Cdd:cd07792 439 SMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRtVFEPQISEEER-ERRYKRWKKAVER 498
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
32-555 |
1.71e-92 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 292.11 E-value: 1.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:PRK00047 6 YILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRSGEYYHNFITWKDLRADELVDQwnaswtkssmnwfsyalflLTRQSRflaGSVLQlmngQVTPRLLFEIMNN 191
Cdd:PRK00047 86 TTVVWDKETGRPIYNAIVWQDRRTADICEE-------------------LKRDGY---EDYIR----EKTGLVIDPYFSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 KKLKQAL-----MQKKA-RVELL----DSWILHKLRTGSSrdkdveHITDVTSSTATGLYDPFTLSWSPLISWLFGINSK 261
Cdd:PRK00047 140 TKIKWILdnvegARERAeKGELLfgtiDTWLVWKLTGGKV------HVTDYTNASRTMLFNIHTLDWDDELLELLDIPRS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 262 ILPRVVDNGyKGFGHVHPTAFGpdwaNTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDrcQAVIS--G 339
Cdd:PRK00047 214 MLPEVRPSS-EVYGKTNPYGFF----GGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGE--KAVKSenG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 340 MYPLVAWQFKKPtrqqgAVYCIEGASHDFGTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPVNDyRS 418
Cdd:PRK00047 287 LLTTIAWGIDGK-----VVYALEGSIFVAGSAIQWLRdGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWD-SD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 419 ASGFI-GLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESS 497
Cdd:PRK00047 361 ARGAIfGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21357867 498 IMGATFMAGINLGIWRDVNDLKRFRKVARVFEPRPKEyETIANRMDKWSRTIARFSDW 555
Cdd:PRK00047 441 ALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEPQMDE-EEREKLYAGWKKAVKRTLAW 497
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
32-555 |
6.32e-79 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 257.32 E-value: 6.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLT----PPDITCLTIS 107
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKghnvDSGLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 108 TQRCTFLTWDHRSGEYYHNFITWKDLRADELVDQWNASWTKSSMNWFSYALflLTRQSRFLAGSVLQLMNgqvtprllfe 187
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCG--LPISTYFSATKLLWLLE---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 188 imNNKKLKQALMQKKARVELLDSWILHKLrTGSSrdKDVEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVV 267
Cdd:PLN02295 149 --NVDAVKEAVKSGDALFGTIDSWLIWNL-TGGA--SGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 268 DNGYKgFGHVhptafGPDWANTEIPIAASLSDQTAAIWGSQCfQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAWQ 347
Cdd:PLN02295 224 SNSEV-IGTI-----AKGWPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 348 F--KKPTRqqgavYCIEGASHDFGTVVTWAQ-SCELFDSPANTSDIAQSVPDTNDVFFMPAFSGLGPPvnDYRS-ASG-F 422
Cdd:PLN02295 297 LgpDAPTN-----YALEGSVAIAGAAVQWLRdNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAP--RWRDdARGvC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 423 IGLTPSTTKAHMVRALLESIVFRLVQLIEA-----AEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESS 497
Cdd:PLN02295 370 VGITRFTNKAHIARAVLESMCFQVKDVLDAmrkdaGEEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETT 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 21357867 498 IMGATFMAGINLGIWRDVNDLK-RFRKVARVFEPRPKEyETIANRMDKWSRTIARFSDW 555
Cdd:PLN02295 450 ALGAAYAAGLAVGLWTEEEIFAsEKWKNTTTFRPKLDE-EERAKRYASWCKAVERSFDL 507
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
33-556 |
7.57e-70 |
|
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: 232.80 E-value: 7.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 33 ILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRCT 112
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 113 FLTWDhRSGEYYHNFITWKDLRADELVDQWNASWTKSsmnwfsyALFLLTrqsrflaGSVLqlMNGQVTPRLLFeIMNNK 192
Cdd:COG1070 83 LVLLD-ADGEPLRPAILWNDTRAAAEAAELREELGEE-------ALYEIT-------GNPL--HPGFTAPKLLW-LKENE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 193 KlkqALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISwLFGINSKILPRVVDNGY 271
Cdd:COG1070 145 P---EIFARIAKVLLPKDYLRYRL-TG-------EFVTDYSDASGTGLLDVRTRDWSDeLLE-ALGIDRELLPELVPPGE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 272 KgFGHVHPtafgpDWAN-----TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgDRCQAVISGMYPLVAW 346
Cdd:COG1070 213 V-AGTLTA-----EAAAetglpAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCH 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 347 QFKkptrqqGAvYCIEGASHDFGTVVTWAqsCELFDSPAN------TSDIAQSVPDTNDVFFMPAFSGLGPPVNDyRSAS 420
Cdd:COG1070 286 AVP------GR-WLPMGATNNGGSALRWF--RDLFADGELddyeelNALAAEVPPGADGLLFLPYLSGERTPHWD-PNAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 421 G-FIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEkETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIM 499
Cdd:COG1070 356 GaFFGLTLSHTRAHLARAVLEGVAFALRDGLEALE-EAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGAL 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21357867 500 GATFMAGINLGIWRDVND-LKRFRKVARVFEPRPKEYETIANRMDKWSRTIARFSDWY 556
Cdd:COG1070 435 GAALLAAVGLGLYDDLEEaAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKPLF 492
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
32-533 |
5.79e-68 |
|
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: 225.86 E-value: 5.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDhRSGEYYHNFITWKDLRADelvdqwnaswtkssmnwfsyalflltrqsRFLagsvlqlmngqvtprllfeimnn 191
Cdd:cd07779 81 TFVPVD-EDGRPLRPAISWQDKRTA-----------------------------KFL----------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 kklkqalmqkkarveLLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGY 271
Cdd:cd07779 108 ---------------TVQDYLLYRL-TG-------EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGT 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 272 KGfGHVHPTA---FG-PdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMYPLVAwq 347
Cdd:cd07779 165 VI-GTLTKEAaeeTGlP----EGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPS-- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 348 fkkptrqqgAV---YCIEGASHDFGTVVTWAqsCELFDSPAN-------------TSDIAQSVPDTNDVFFMPAFSG-LG 410
Cdd:cd07779 238 ---------AVpgkWVLEGSINTGGSAVRWF--RDEFGQDEVaekelgvspyellNEEAAKSPPGSDGLLFLPYLAGaGT 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 411 PPVNDYRSASgFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETsQKLHMIRVDGGVSRNDFVCQFLADLSRLRVER 490
Cdd:cd07779 307 PYWNPEARGA-FIGLTLSHTRAHLARAILEGIAFELRDNLEAMEKAG-VPIEEIRVSGGGSKSDLWNQIIADVFGRPVER 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 21357867 491 ADNAESSIMGATFMAGINLGIWRDVND-LKRFRKVARVFEPRPK 533
Cdd:cd07779 385 PETSEATALGAAILAAVGAGIYPDFEEaVKAMVRVTDTFEPDPE 428
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
33-510 |
1.46e-56 |
|
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: 195.88 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 33 ILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVknAQLTPPDITCLTISTQRCT 112
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAA--AQAGPDPIAAISVSSQGES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 113 FLTWDhRSGEYYHNFITWKDLRADELVDQWNASWTKssmnwfsYALFLLTrqsrflaGSVLQLMNGqvtprlLFEIMNNK 192
Cdd:cd07773 80 GVPVD-RDGEPLGPAIVWFDPRGKEEAEELAERIGA-------EELYRIT-------GLPPSPMYS------LAKLLWLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 193 KLKQALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGYK 272
Cdd:cd07773 139 EHEPEIFAKAAKWLSVADYIAYRL-TG-------EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 273 GfGHVHPTAFGPDWANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTG-AFLNLVTGDRCQAVISGMYPLVAWQFKkp 351
Cdd:cd07773 211 I-GTVTPEAAEELGLPAGTPVVVGGHDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVP-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 352 trqqGAVYCIeGASHDFGTVVTWAQS--CELFDSPANTSDIAQSVPDT-NDVFFMPAFSGLGPPVNDYRSASGFIGLTPS 428
Cdd:cd07773 288 ----GGYYYL-AGSLPGGALLEWFRDlfGGDESDLAAADELAEAAPPGpTGLLFLPHLSGSGTPDFDPDARGAFLGLTLG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 429 TTKAHMVRALLESIVFRLVQLIEAAEKETsQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGIN 508
Cdd:cd07773 363 TTRADLLRAILEGLAFELRLNLEALEKAG-IPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVG 441
|
..
gi 21357867 509 LG 510
Cdd:cd07773 442 AG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
32-556 |
4.06e-56 |
|
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: 195.83 E-value: 4.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDhRSGEYYHNFITWKDLRADELVDQWNASWTKssmnwfsyaLFLLTRQSRFLAGSVLqlmngqvtPRLLFeIMNN 191
Cdd:cd07808 81 GLVLLD-KNGRPLRPAILWNDQRSAAECEELEARLGD---------EILIITGNPPLPGFTL--------PKLLW-LKEN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 -----KKLKQALMQKkarvellDsWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRV 266
Cdd:cd07808 142 epeifARIRKILLPK-------D-YLRYRL-TG-------ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 267 VDnGYKGFGHVHPTA---FGpdwANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgDRCQAVisgmYPL 343
Cdd:cd07808 206 VE-STEIVGTLTPEAaeeLG---LPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPD----PKG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 344 VAWQFKKPTRQQgavYCIEGASHDFGTVVTWAqsCELFDSPANT-----SDIAQSVPDTNDVFFMPAFSGLGPPVNDYRS 418
Cdd:cd07808 277 RLHTFPHAVPGK---WYAMGVTLSAGLSLRWL--RDLFGPDRESfdeldAEAAKVPPGSEGLLFLPYLSGERTPYWDPNA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 419 ASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAeKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSI 498
Cdd:cd07808 352 RGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSA 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 21357867 499 MGATFMAGINLGIWRDVND-LKRFRKVARVFEPRPkeyetiaNRMDKWSRTIARFSDWY 556
Cdd:cd07808 431 YGAALLAAVGAGVFDDLEEaAAACIKIEKTIEPDP-------ERHEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
32-547 |
1.94e-54 |
|
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: 191.23 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVknAQLTPPDITCLTISTQRC 111
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDhRSGEYYHNFITWKDLRADELVDQWnaswtKSSMnwFSYALFLLTrqsrflaGSVLQLMNgqvtprLLFEIMNN 191
Cdd:cd07770 79 SLLGVD-EDGEPLTPVITWADTRAAEEAERL-----RKEG--DGSELYRRT-------GCPIHPMY------PLAKLLWL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 KKLKQALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISWLfGINSKILPRVVDng 270
Cdd:cd07770 138 KEERPELFAKAAKFVSIKEYLLYRL-TG-------ELVTDYSTASGTGLLNIHTLDWDEeALELL-GIDEEQLPELVD-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 271 ykgFGHVHPTAfGPDWAN-----TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDR---------CQAV 336
Cdd:cd07770 207 ---PTEVLPGL-KPEFAErlgllAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPvldppgrlwCYRL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 337 ISGMYplvawqfkkptrqqgavyCIEGASHDFGTVVTWAQScELFDSPANTSDI----AQSVPDTNDVFFMPAFSGLGPP 412
Cdd:cd07770 283 DENRW------------------LVGGAINNGGNVLDWLRD-TLLLSGDDYEELdklaEAVPPGSHGLIFLPYLAGERAP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 413 V-NDYRSASgFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEkETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERA 491
Cdd:cd07770 344 GwNPDARGA-FFGLTLNHTRADILRAVLEGVAFNLKSIYEALE-ELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVP 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 21357867 492 DNAESSIMGATFMAGINLGIWRDVnDLKRFRKVARVFEPRPKEYETIANRMDKWSR 547
Cdd:cd07770 422 EEEEASALGAALLALEALGLISSL-EADELVKIGKVVEPDPENHAIYAELYERFKK 476
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
33-505 |
7.21e-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: 184.69 E-value: 7.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 33 ILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRCT 112
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 113 FLTWDhRSGEYYHNFITWKDLRAdelvdqwnaswtkssmnwfsyalflltrqsRFLagsvlqlmngqvtprllfeiMNNk 192
Cdd:cd00366 82 VVLVD-ADGNPLRPAIIWLDRRA------------------------------KFL--------------------QPN- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 193 klkqalmqkkarvelldSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISWlFGINSKILPRVVdNGY 271
Cdd:cd00366 110 -----------------DYIVFRL-TG-------EFAIDYSNASGTGLYDIKTGDWSEeLLDA-LGIPREKLPPIV-ESG 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 272 KGFGHVHPTAfgpdwA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgDRCQA---VISGMYPL 343
Cdd:cd00366 163 EVVGRVTPEA-----AeetglPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT-DEPVPpdpRLLNRCHV 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 344 VawqfkkptrqqGAVYCIEGASHDFGTVVTWA--QSCELFDSPAN----TSDIAQSVPDTNDVFFMPAFSGLGPPVNDYR 417
Cdd:cd00366 237 V-----------PGLWLLEGAINTGGASLRWFrdEFGEEEDSDAEyeglDELAAEVPPGSDGLIFLPYLSGERSPIWDPA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 418 SASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSqKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESS 497
Cdd:cd00366 306 ARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGV-KIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
....*...
gi 21357867 498 IMGATFMA 505
Cdd:cd00366 385 ALGAAILA 392
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
32-536 |
4.47e-52 |
|
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: 185.03 E-value: 4.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDhRSGEYYHNFITWKDLRADELVDQWNASWTKssmnWFSYALFLLTRQSrflAGSVLqlmngqvtPRLLFeimnn 191
Cdd:cd07805 81 GVVPVD-KDGNPLRNAIIWSDTRAAEEAEEIAGGLGG----IEGYRLGGGNPPS---GKDPL--------AKILW----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 kkLKQALMQ--KKARVeLLDS--WILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISwLFGINSKILPRV 266
Cdd:cd07805 140 --LKENEPEiyAKTHK-FLDAkdYLNFRL-TG-------RAATDPSTASTTGLMDLRKRRWSEeLLR-AAGIDPDKLPEL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 267 VDNGYKgFGHVHPTAfgpdwAN-----TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRC-------- 333
Cdd:cd07805 208 VPSTEV-VGELTPEA-----AAelglpAGTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKtdpdhgif 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 334 --QAVISGMYPLVAwqfkkptRQQGAvycieGASHDfgtvvtWAQSCELFDSPANTSD-------IAQSVPDTNDVFFMP 404
Cdd:cd07805 282 tlASADPGRYLLAA-------EQETA-----GGALE------WARDNLGGDEDLGADDyelldelAAEAPPGSNGLLFLP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 405 AFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETsQKLHMIRVDGGVSRNDFVCQFLADLS 484
Cdd:cd07805 344 WLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLT-RKIDELRLVGGGARSDLWCQILADVL 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 21357867 485 RLRVERADNA-ESSIMGATFMAGINLGIWRDVNDLKRFRKVARVFEPRPKEYE 536
Cdd:cd07805 423 GRPVEVPENPqEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENRA 475
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
32-510 |
1.01e-40 |
|
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: 153.09 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDhRSGEYYHNFITWKDLRADELVDQWNASWTkssmnwfSYALFLLTRQsrflagsvlQLMNGQVTPrLLFEIMNN 191
Cdd:cd07802 81 GLYLVD-KDGKPVRNAILSNDSRAADIVDRWEEDGT-------LEKVYPLTGQ---------PLWPGQPVA-LLRWLKEN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 -----KKLKQALMQKkarvellDsWILHKLrTGssrdkdvEHITDVTSSTaTGLYDPFTLSWSPLISWLFGIN--SKILP 264
Cdd:cd07802 143 eperyDRIRTVLFCK-------D-WIRYRL-TG-------EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 265 RVVDNGYKGfGHVHPTAfgpdwA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTgAFLNLVTGDRcqavisg 339
Cdd:cd07802 206 PLVPSTEIA-GRVTAEA-----AaltglPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGT-WSINEVVTDE------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 340 myPLVAwqfkkPTRQQGAVYCIEG------ASHDFGTVVTWAQScELFDSP--ANTSD-------IAQSVPDTNDVFFMP 404
Cdd:cd07802 272 --PVVP-----DSVGSNSLHADPGlyliveASPTSASNLDWFLD-TLLGEEkeAGGSDydeldelIAAVPPGSSGVIFLP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 405 AFSGlgPPVNDYRSAsGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETsqKLHMIRVDGGVSRNDFVCQFLADLS 484
Cdd:cd07802 344 YLYG--SGANPNARG-GFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVL 418
|
490 500
....*....|....*....|....*.
gi 21357867 485 RLRVERADNAESSIMGATFMAGINLG 510
Cdd:cd07802 419 GLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
32-510 |
1.48e-34 |
|
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: 135.73 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRsGEYYHNFITWKDLRADELVDqwnasWTKSsmNWFSYALFLLTrqsrflaGSVLqlmNGQ-VTPRLLFeIMN 190
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIE-----WLNE--NIGEDRIFEIT-------GNPL---DSQsVGPKLLW-IKR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 191 N-----KKLKQALMQKkarvelldSWILHKLrTGssrdkdvEHITDVTS-STATGLYDPFTLSWSPLISWLFGINSKILP 264
Cdd:cd07804 142 NepevfKKTRKFLGAY--------DYIVYKL-TG-------EYVIDYSSaGNEGGLFDIRKRTWDEELLEALGIDPDLLP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 265 RVVDNGyKGFGHVHPtafgpDWA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVIsg 339
Cdd:cd07804 206 ELVPST-EIVGEVTK-----EAAeetglAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPR-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 340 mYPLVAWQFKKPtrqqgavYCIEGASHDFGTVVTW-------AQSCELFDSPANTSDI----AQSVPDTND-VFFMPAFS 407
Cdd:cd07804 278 -LWLDYHDIPGT-------YVLNGGMATSGSLLRWfrdefagEEVEAEKSGGDSAYDLldeeAEKIPPGSDgLIVLPYFM 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 408 GLGPPVNDyRSASG-FIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEkETSQKLHMIRVDGGVSRNDFVCQFLADLSRL 486
Cdd:cd07804 350 GERTPIWD-PDARGvIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIR-EAGLPIKRLVAVGGGAKSPLWRQIVADVTGV 427
|
490 500
....*....|....*....|....
gi 21357867 487 RVERADNAESSIMGATFMAGINLG 510
Cdd:cd07804 428 PQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
32-507 |
2.30e-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: 134.66 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVknAQLTPPDITCLTISTQRC 111
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELP--AELRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRsGEYYHNFITWKDLRADELVDQWNASWtkssmnwfsyALFLLTRQSRFLAGSVLqlmngqvtPRLLFEIMNN 191
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAA----------GAVAPRTGLAVSPSSSL--------AKLLWLKRHE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 KKLkqalmQKKARVELLDS-WILHKLrTGSsrdkdvEHITDVTSSTATGlYDPFTLSWSPLISWLFGINSKILPRVVDNG 270
Cdd:cd07783 140 PEV-----LAKTAKFLHQAdWLAGRL-TGD------RGVTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 271 YKgFGHVHPTA---FG-PdwanTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVISGMY--PLV 344
Cdd:cd07783 207 TV-IGTLTAEAaeeLGlP----AGTPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYshRHG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 345 AwqfkkptrqqgAVYCIEGASHDFGTVVTWAQSCELFDspANTSDIAQSVPDtnDVFFMPaFSGLGP--PVNDyRSASGF 422
Cdd:cd07783 282 D-----------GYWLVGGASNTGGAVLRWFFSDDELA--ELSAQADPPGPS--GLIYYP-LPLRGErfPFWD-PDARGF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 423 IgLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAESSiMGAT 502
Cdd:cd07783 345 L-LPRPHDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAA-LGAA 422
|
....*
gi 21357867 503 FMAGI 507
Cdd:cd07783 423 LLAAA 427
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
32-510 |
7.77e-33 |
|
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: 130.81 E-value: 7.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNP--QPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQ 109
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 110 R--CTFLtwDHRSGEYYH--NFitwkDLRADELVDQWN-----ASWTKSSMnWFSyALFLLTRqsrfLAGsvlqlmngqv 180
Cdd:cd07798 81 RegIVFL--DKDGRELYAgpNI----DARGVEEAAEIDdefgeEIYTTTGH-WPT-ELFPAAR----LLW---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 181 tprllFeimnnKKLKQALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINS 260
Cdd:cd07798 139 -----F-----KENRPEIFERIATVLSISDWIGYRL-TG-------ELVSEPSQASETQLFDIKKREWSQELLEALGLPP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 261 KILPRVVDNGYKgFGHVHPtafgpDWA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTG----D 331
Cdd:cd07798 201 EILPEIVPSGTV-LGTVSE-----EAArelglPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDepiiD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 332 RCQAVISGMYPLvawqfkkPTRqqgavYCIEGASHDFGTVVTWAQScELFDSPANTSD-----IAQSVPDTNDVFfmpaf 406
Cdd:cd07798 275 PERRLWTGCHLV-------PGK-----WVLESNAGVTGLNYQWLKE-LLYGDPEDSYEvleeeASEIPPGANGVL----- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 407 SGLGPPVNDYRSAS----GFIGLTP----STTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQ 478
Cdd:cd07798 337 AFLGPQIFDARLSGlkngGFLFPTPlsasELTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQ 416
|
490 500 510
....*....|....*....|....*....|..
gi 21357867 479 FLADLSRLRVERADNAESSIMGATFMAGINLG 510
Cdd:cd07798 417 ILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
315-509 |
3.92e-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: 113.96 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 315 VKVTMGTGAFLnLVTGDRCQAVISGMYPLVAWQFKKPtrqqgaVYCIEGASHDFGTVVTWA----QSCELFDSPANTSDI 390
Cdd:pfam02782 1 LAISAGTSSFV-LVETPEPVLSVHGVWGPYTNEMLPG------YWGLEGGQSAAGSLLAWLlqfhGLREELRDAGNVESL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 391 AQ-----SVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIR 465
Cdd:pfam02782 74 AElaalaAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21357867 466 VDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINL 509
Cdd:pfam02782 154 VSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
32-306 |
5.48e-28 |
|
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: 112.43 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TFLTWDHRSGEYYhNFITWKDLRADELVDqwnaSWTKSSMNWFSYALFLLTRQSRFLAgsvlqlmngqvtPRLLFeIMNN 191
Cdd:pfam00370 81 GTVLLDKNDKPLY-NAILWKDRRTAEIVE----NLKEEGNNQKLYEITGLPIWPGFTL------------SKLRW-IKEN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 192 KKLKQALMQKkarVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVDNGY 271
Cdd:pfam00370 143 EPEVFEKIHK---FLTIHDYLRWRL-TG-------VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSE 211
|
250 260 270
....*....|....*....|....*....|....*
gi 21357867 272 KgFGHVHPTAFGPDWANTEIPIAASLSDQTAAIWG 306
Cdd:pfam00370 212 I-YGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
32-510 |
9.53e-27 |
|
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: 113.03 E-value: 9.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLD-EQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQR 110
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 111 CTFLTWDhRSGEYYHNFITWKDLR----ADELVDQWNaswtkssmnwFSYALFLLTRQS-RFLAGSVLQLMNgqvtprll 185
Cdd:cd07809 81 HGLVALD-ADGKVLRPAKLWCDTRtapeAEELTEALG----------GKKCLLVGLNIPaRFTASKLLWLKE-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 186 feimNNKKLKQALmqkkARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLF---GINSKI 262
Cdd:cd07809 142 ----NEPEHYARI----AKILLPHDYLNWKL-TG-------EKVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 263 LPRVVDNGYKGfGHVHPTA---FGpdwANTEIPIAASLSDQ-TAAIwGSQCFQKNDVKVTMGTGAFLNLVTGDRCQAVIS 338
Cdd:cd07809 206 LPEVLPAGEVA-GRLTPEGaeeLG---LPAGIPVAPGEGDNmTGAL-GTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 339 GMYP----LVAWqfkkptrqqgaVYCIEGAShDFGTVVTWAqsCELFDSPANTSD--IAQSVPDTNDVFFMPAFSGlgPP 412
Cdd:cd07809 281 RVATfcdsTGGM-----------LPLINTTN-CLTAWTELF--RELLGVSYEELDelAAQAPPGAGGLLLLPFLNG--ER 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 413 VNDYRSASG-FIGLTPS-TTKAHMVRALLESIVFRL---VQLIEAAEKETSQklhmIRVDGGVSRNDFVCQFLADLSRLR 487
Cdd:cd07809 345 TPNLPHGRAsLVGLTLSnFTRANLARAALEGATFGLrygLDILRELGVEIDE----IRLIGGGSKSPVWRQILADVFGVP 420
|
490 500
....*....|....*....|...
gi 21357867 488 VERADNAESSIMGATFMAGINLG 510
Cdd:cd07809 421 VVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
32-510 |
1.69e-26 |
|
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: 112.33 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQRC 111
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 112 TflTW--DhRSGEYYHNFITWKDLRADELVDQWNASWTkssmnwfSYALFLLTrqsrflaGSVLqlmNGQVTPRLLFEIM 189
Cdd:cd24121 81 G--TWlvD-EDGRPVRDAILWLDGRAADIVERWQADGI-------AEAVFEIT-------GTGL---FPGSQAAQLAWLK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 190 NNKKlkqALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATgLYDPFTLSWSPLISWLFGINS--KILPRVV 267
Cdd:cd24121 141 ENEP---ERLERARTALHCKDWLFYKL-TG-------EIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEElrHLLPPIR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 268 DngykGFGHVHPTAfgPDWAN-----TEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTgAFLNLVTGDRC--QAVISGM 340
Cdd:cd24121 209 P----GTEVIGPLT--PEAAAatglpAGTPVVLGPFDVVATALGSGAIEPGDACSILGT-TGVHEVVVDEPdlEPEGVGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 341 YPLVAWQfKKPTRQQGAVYciegashdfGT-VVTWA--QSCELFDSPANTSD----------IAQSVPDTNDVFFMPAFS 407
Cdd:cd24121 282 TICLGVP-GRWLRAMANMA---------GTpNLDWFlrELGEVLKEGAEPAGsdlfqdleelAASSPPGAEGVLYHPYLS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 408 GLG---PPVNDYRSASgFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAeketSQKLHMIRVDGGVSRNDFVCQFLADLS 484
Cdd:cd24121 352 PAGeraPFVNPNARAQ-FTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADAL 426
|
490 500
....*....|....*....|....*.
gi 21357867 485 RLRVERADNAESSIMGATFMAGINLG 510
Cdd:cd24121 427 GVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
32-505 |
5.02e-23 |
|
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: 101.91 E-value: 5.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQcevRGSAVDAVELLNPQ------PGYFEIEPESLWRKIVGVITQAVKNAQltpPDITCLT 105
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLE---SGRILESVSRPTPApissddPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 106 ISTQRCTFLTWDHRsGEYYHNFITWKDLRADELVDqwnaswtkSSMNWFSYALFLLTrqsrflaGSVLQLMNGQVTprlL 185
Cdd:cd07777 75 ITGQMHGIVLWDED-GNPVSPLITWQDQRCSEEFL--------GGLSTYGEELLPKS-------GMRLKPGYGLAT---L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 186 FEIMNNKKLKQalmqKKARVELLDSWILHKLrTGSSrdkdvEHITDVTSSTATGLYDPFTLSWSP-LISWLfGINSKILP 264
Cdd:cd07777 136 FWLLRNGPLPS----KADRAGTIGDYIVARL-TGLP-----KPVMHPTNAASWGLFDLETGTWNKdLLEAL-GLPVILLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 265 RVVDNGyKGFGHVHPTAfgpdwaNTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTGAFLNLVTgdrCQAVISGMY--- 341
Cdd:cd07777 205 EIVPSG-EIVGTLSSAL------PKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLT---PKFELSGSVeir 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 342 PlvawqFKKPTrqqgavYCIEGAS--------HDFGTVVTWAQscELFDSPANT---SDIAQSVP--DTNDVFFMPAFSG 408
Cdd:cd07777 275 P-----FFDGR------YLLVAASlpggralaVLVDFLREWLR--ELGGSLSDDeiwEKLDELAEseESSDLSVDPTFFG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 409 lgpPVNDYRSASGFIGLTPSTTK-AHMVRALLESIVfrlVQLIEAAEKETSQKLHM--IRVDGGVSR-NDFVCQFLADLS 484
Cdd:cd07777 342 ---ERHDPEGRGSITNIGESNFTlGNLFRALCRGIA---ENLHEMLPRLDLDLSGIerIVGSGGALRkNPVLRRIIEKRF 415
|
490 500
....*....|....*....|.
gi 21357867 485 RLRVERADNAESSIMGATFMA 505
Cdd:cd07777 416 GLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
32-545 |
9.72e-23 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 101.64 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSA-VDAVELLNPQ-PGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQ 109
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAqREWRHKEVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 110 RCTFLTWDHRSGEYY--HNFitwkDLRADELVdqwnaSWTKSSMNWFSYALFLLTRQSRFLAGsvlqlmngqvTPRLLFe 187
Cdd:cd07775 81 REGIVLYDNEGEEIWacANV----DARAAEEV-----SELKELYNTLEEEVYRISGQTFALGA----------IPRLLW- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 188 IMNNKKlkqALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVV 267
Cdd:cd07775 141 LKNNRP---EIYRKAAKITMLSDWIAYKL-SG-------ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 268 DNGYKgFGHVHPTAFGPDWANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTgaFLNL-------VTGDRCQ-----A 335
Cdd:cd07775 210 ESGTV-IGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGS--FWQQevntaapVTDPAMNirvncH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 336 VISGMyplvaWQFkkptrqqgavyciEGASHDFGTVVTW---AQSCEL--------FDSPANTSDIAQSVPdTNDVFFMP 404
Cdd:cd07775 287 VIPDM-----WQA-------------EGISFFPGLVMRWfrdAFCAEEkeiaerlgIDAYDLLEEMAKDVP-PGSYGIMP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 405 AFSGLGPPVNDYRSASGFIGLT---PSTTKAHMVRALLES--IVFRL-VQLIEAAekeTSQKLHMIRVDGGVSRNDFVCQ 478
Cdd:cd07775 348 IFSDVMNYKNWRHAAPSFLNLDidpEKCNKATFFRAIMENaaIVSAGnLERIAEF---SGIFPDSLVFAGGASKGKLWCQ 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357867 479 FLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVND-LKRFRKVARVFEPRPKEYETIANRMDKW 545
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; ... |
34-538 |
7.26e-22 |
|
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: 98.76 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 34 LALDVGTTCVRSFVLDEQC-EVRGSAVDAVELL--NPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITCLTISTQR 110
Cdd:cd07781 3 IGIDFGTQSVRAGLVDLADgEELASAVVPYPTGyiPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDTTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 111 CTFLTWDhRSGEYYHNFITWKDLRA-------DELVDQWNASWT-----KSSMNWFsyalflltrqsrflagsvlqlmng 178
Cdd:cd07781 83 STVVPVD-EDGNPLAPAILWMDHRAqeeaaeiNETAHPALEYYLayyggVYSSEWM------------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 179 qvTPRLLfEIMNNKKlkqALMQKKAR-VELLDsWILHKLrTGssrdkdvehiTDVTSSTATG---LYDPFTLSWS----- 249
Cdd:cd07781 138 --WPKAL-WLKRNAP---EVYDAAYTiVEACD-WINARL-TG----------RWVRSRCAAGhkwMYNEWGGGPPrefla 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 250 ---PLiswLFGINSKILPRVVDNGyKGFGHVHPtafgpDWA-----NTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGT 321
Cdd:cd07781 200 aldPG---LLKLREKLPGEVVPVG-EPAGTLTA-----EAAerlglPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 322 gAFLNLVTGDRCQAV--ISGMYPlvawqfkkptrqqGAV----YCIEGASHDFGTVVTWAqsCELFDSPANT-------- 387
Cdd:cd07781 271 -STCHLMVSPKPVDIpgICGPVP-------------DAVvpglYGLEAGQSAVGDIFAWF--VRLFVPPAEErgdsiyal 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 388 -SDIAQSV-PDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSqKLHMIR 465
Cdd:cd07781 335 lSEEAAKLpPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGV-PVNRVV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357867 466 VDGGVS-RNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDL-KRFRKVARVFEPRP---KEYETI 538
Cdd:cd07781 414 ACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAaDAMVRVDRVYEPDPenhAVYEEL 491
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
230-526 |
3.58e-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: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 230 TDVTSSTATGLYDPFTLSWS-PLISWLfGINSKILPRVVDNGyKGFGHVHPTaFGPDWANTEIPIAASLSDQTA-AIWGS 307
Cdd:cd07771 168 AEYTIASTTQLLDPRTKDWSeELLEKL-GLPRDLFPPIVPPG-TVLGTLKPE-VAEELGLKGIPVIAVASHDTAsAVAAV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 308 QCFQKNDVKVTMGT----GAFLN--LVTGDRCQA----------------VISGMYPL----VAWQfkkptrqqgavycI 361
Cdd:cd07771 245 PAEDEDAAFISSGTwsliGVELDepVITEEAFEAgftneggadgtirllkNITGLWLLqecrREWE-------------E 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 362 EGASHDFGTVVTWAQSCELFDSPANTSDiaqsvpdtnDVFF----MPAFsglgppVNDYrsaSGFIGLTPSTTKAHMVRA 437
Cdd:cd07771 312 EGKDYSYDELVALAEEAPPFGAFIDPDD---------PRFLnpgdMPEA------IRAY---CRETGQPVPESPGEIARC 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 438 LLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVeRADNAESSIMGATFMAGINLGiwrDVND 517
Cdd:cd07771 374 IYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPV-IAGPVEATAIGNLLVQLIALG---EIKS 449
|
....*....
gi 21357867 518 LKRFRKVAR 526
Cdd:cd07771 450 LEEGRELVR 458
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
34-518 |
7.09e-16 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 80.40 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 34 LALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRkivgVITQAVK--NAQLTPPDITCLTISTQR- 110
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQ----ATDRAMKalGDQHSLQDVKALGIAGQMh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 111 -CTFLTWDHRsgeYYHNFITWKDLRADElvdqwNASWTKSSMNwfsyalflltrQSRFLAGSVlqLMNGQVTPRLLFEim 189
Cdd:PRK15027 79 gATLLDAQQR---VLRPAILWNDGRCAQ-----ECALLEARVP-----------QSRVITGNL--MMPGFTAPKLLWV-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 190 nnKKLKQALMQKKARVELLDSWIlhKLR-TGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRVVD 268
Cdd:PRK15027 136 --QRHEPEIFRQIDKVLLPKDYL--RLRmTG-------EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 269 nGYKGFGHVHPtAFGPDWANTEIPIAASLSDQTAAIWGSQCFQKNDVKVTMGTgaflnlvtgdrcqaviSGMYPLVAWQF 348
Cdd:PRK15027 205 -GSEITGALLP-EVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT----------------SGVYFAVSEGF 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 349 -KKPtrqqgavyciEGASHDFG----------TVVTWAQSC--------ELFDSPANTSDIAQSVPDTNDVFFMPAFSGL 409
Cdd:PRK15027 267 lSKP----------ESAVHSFChalpqrwhlmSVMLSAASCldwaakltGLSNVPALIAAAQQADESAEPVWFLPYLSGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 410 GPPVNDYRSASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEkETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVE 489
Cdd:PRK15027 337 RTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADISGQQLD 415
|
490 500 510
....*....|....*....|....*....|
gi 21357867 490 -RADNAESSIMGATFMAGINLGIWRDVNDL 518
Cdd:PRK15027 416 yRTGGDVGPALGAARLAQIAANPEKSLIEL 445
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
32-551 |
4.54e-14 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 74.66 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDE--------QCEVRGSAVDAVellnpqPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDITC 103
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLngnqiavgQAEWRHLAVPDV------PGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 104 LTISTQRCTFLTWDHRSGEyyhnfiTWK----DLRADELVdqwnaSWTKSSMNWFSYALFLLTRQSrfLAGSVLqlmngq 179
Cdd:PRK10939 78 VSATSMREGIVLYDRNGTE------IWAcanvDARASREV-----SELKELHNNFEEEVYRCSGQT--LALGAL------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 180 vtPRLLFEimnnKKLKQALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGIN 259
Cdd:PRK10939 139 --PRLLWL----AHHRPDIYRQAHTITMISDWIAYML-SG-------ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 260 SKILPRVVDNGYKgFGHVHPTAFGPDWANTEIPIAASLSD--------------QTAAIWGSqcFQKNDVKVTMG-TGAF 324
Cdd:PRK10939 205 ADILPPVKETGTV-LGHVTAKAAAETGLRAGTPVVMGGGDvqlgclglgvvrpgQTAVLGGT--FWQQVVNLPAPvTDPN 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 325 LNLvtgdRCQA-VISGMyplvaWQFkkptrqqgavyciEGASHDFGTVVTWAQS--CEL---------FDSPANTSDIAQ 392
Cdd:PRK10939 282 MNI----RINPhVIPGM-----VQA-------------ESISFFTGLTMRWFRDafCAEekllaerlgIDAYSLLEEMAS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 393 SVP-DTNDVffMPAFSGLGPPVNDYRSASGFIGLT--PS-TTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDG 468
Cdd:PRK10939 340 RVPvGSHGI--IPIFSDVMRFKSWYHAAPSFINLSidPEkCNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAG 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 469 GVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDL-KRFRKVARVFEPRPKEYETIANRMDKWSR 547
Cdd:PRK10939 418 GGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETgERLVRWERTFEPNPENHELYQEAKEKWQA 497
|
....
gi 21357867 548 TIAR 551
Cdd:PRK10939 498 VYAD 501
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
31-530 |
6.86e-14 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 73.91 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 31 AFILALDVGTTCVRSFVLDEQCEVRGSA--VDAVELLNPQPGYFEIEPESLWRKIVGVITQAvkNAQLTPPDITCLTIST 108
Cdd:PRK10331 2 DVILVLDCGATNVRAIAVDRQGKIVARAstPNASDIAAENSDWHQWSLDAILQRFADCCRQI--NSELTECHIRGITVTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 109 QRCTFLTWDhRSGEYYHNFITWKDLRADELVDQWnaswtkssmnwfsyalflltrqSRFLAGSVLQLMNG--QVTPRLLF 186
Cdd:PRK10331 80 FGVDGALVD-KQGNLLYPIISWKCPRTAAVMENI----------------------ERYISAQQLQQISGvgAFSFNTLY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 187 EIMNNKKLKQALMQKKARVELLDSWILHKLrTGssrdkdvEHITDVTSSTATGLYDPFTLSWSPLISWLFGINSKILPRV 266
Cdd:PRK10331 137 KLVWLKENHPQLLEQAHAWLFISSLINHRL-TG-------EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 267 VDNGYKgFGHVHPTAFGPDWANTEIPIAASLSDQTAAIWGSQCfQKNDVKVTMGTGAFLNLvtgdRCQAVISgmyplvAW 346
Cdd:PRK10331 209 VEAGEQ-IGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSGA-GQNQPVLSSGTWEILMV----RSAQVDT------SL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 347 QFkkptRQQGAVYCIEGASHDFGTVVTWAQSC------ELFDSPANTSDI----AQSVPD-TNDVFFMPAFSGLGppvnd 415
Cdd:PRK10331 277 LS----QYAGSTCELDSQSGLYNPGMQWLASGvlewvrKLFWTAETPYQTmieeARAIPPgADGVKMQCDLLACQ----- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 416 yrsASGFIGLTPSTTKAHMVRALLESIVFRLVQLIEAAEKETSQKLHMIRVDGGVSRNDFVCQFLADLSRLRVERADNAE 495
Cdd:PRK10331 348 ---NAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAE 424
|
490 500 510
....*....|....*....|....*....|....*.
gi 21357867 496 SSIMGATFMAGINLGIWRDVNDLK-RFRKVARVFEP 530
Cdd:PRK10331 425 TTVAGAAMFGWYGVGEFSSPEQARaQMKYQYRYFYP 460
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
32-145 |
1.47e-07 |
|
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: 54.08 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 32 FILALDVGTTCVRSFVLDEQCEVRGSAVDAVELLNPQPGYFEIEPESLWRKIVGVITQAVKNAQLTPPDI-------TC- 103
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVkgigfdaTCs 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 21357867 104 ---LTISTQRCTfltwDHRSGEYYHNFITWKDLRADELVDQWNAS 145
Cdd:cd07782 81 lvvLDAEGKPVS----VSPSGDDERNVILWMDHRAVEEAERINAT 121
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
388-544 |
7.46e-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: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 388 SDIAQSVPDTNDVFFMPAFSGLGPPVNDYRSASGFIGLTPSTTK---AHMVRALLESIVFRLVQLIEAAEKETSQkLHMI 464
Cdd:cd07768 351 RQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMlnlTYKYIAILEALAFGTRLIIDTFQNEGIH-IKEL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357867 465 RVDGGVSRNDFVCQFLADLSRLRVERADNAESSIMGATFMAGINLGIWRDVNDL----KRFRKVARVFEPRPKEYETIAN 540
Cdd:cd07768 430 RASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQLADSIteadISNDRKSETFEPLAYRLGADYI 509
|
....
gi 21357867 541 RMDK 544
Cdd:cd07768 510 LLYK 513
|
|
| |
