|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
15-477 |
1.55e-158 |
|
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: 458.94 E-value: 1.55e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 15 VSLGIELGSTRIKAVLI-TDDFNTIASGSYVWENQFVD-GTWTYALEDVWTGIQQSYTQLAADVRSkyhmSLKHINAIGI 92
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIdAETGRVVASGSAPHENILIDpGWAEQDPEDWWDALQAAFAQLLKDAGA----ELRDVAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 93 SAMMHGYLAFDQQAKLLVPFRTWRNNITGQAADELTELFDF--------NMPQRWSIAHLYQAILNNEAHVKQVDFITTL 164
Cdd:cd07809 77 SGQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGkkcllvglNIPARFTASKLLWLKENEPEHYARIAKILLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 165 AGYVTWKLSGEKVLGIGDASGVFPIDETTDTYNQTMLTKFSQldkvkpySWDIRHILPRVLPAGAIAGKLTAAGASLLDq 244
Cdd:cd07809 157 HDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDP-------SRDLRDLLPEVLPAGEVAGRLTPEGAEELG- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 245 sgtLDAGSVIAPPEGDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPLSKVYrdiDIVMTPDGSPVAMVHVNNCSSDI 324
Cdd:cd07809 229 ---LPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPH---GRVATFCDSTGGMLPLINTTNCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 325 NAWATIFREFAarlgmelkpDRLYETLFLESTRADADAGGLANYSYQSGENITKIQAGRPLFVRTPNSKFSLPNFMLTQL 404
Cdd:cd07809 303 TAWTELFRELL---------GVSYEELDELAAQAPPGAGGLLLLPFLNGERTPNLPHGRASLVGLTLSNFTRANLARAAL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764618287 405 YAAFAPLQLGMDILVNEEhVQTDVMIAQGGLFRTPViGQQVLANALNIPITVMSTaGEGGPWGMAVLANFACR 477
Cdd:cd07809 374 EGATFGLRYGLDILRELG-VEIDEIRLIGGGSKSPV-WRQILADVFGVPVVVPET-GEGGALGAALQAAWGAG 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
14-526 |
9.77e-103 |
|
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: 317.54 E-value: 9.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 14 KVSLGIELGSTRIKAVLITDDFNTIASGSYVWENQFV-DGTWTYALEDVWTGIQQSYTQLAADVRSkyhmSLKHINAIGI 92
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPhPGWAEQDPEDWWEAVVEAIRELLAKAGV----DPEEIAAIGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 93 SAMMHGYLAFDQQAKLLVPFRTWRNNITGQAADELTELFD----FN------MPQrWSIAHLYQaILNNE-AHVKQVDFI 161
Cdd:COG1070 77 SGQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGeealYEitgnplHPG-FTAPKLLW-LKENEpEIFARIAKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 162 TTLAGYVTWKLSGEKVLGIGDASGVFPIDETTDTYNQTMLTKFsqldkvkpyswDI-RHILPRVLPAGAIAGKLTAAGAS 240
Cdd:COG1070 155 LLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEAL-----------GIdRELLPELVPPGEVAGTLTAEAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 241 LLDqsgtLDAGSVIAPPEGDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPLSKVYRDIDIVMTP-DGSPVAMVHVNN 319
Cdd:COG1070 224 ETG----LPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAvPGRWLPMGATNN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 320 CSSDINAWATIFREfaarlgmelKPDRLYETLFLESTRADADAGGLANYSYQSGENITKIQA-GRPLFVRTpNSKFSLPN 398
Cdd:COG1070 300 GGSALRWFRDLFAD---------GELDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPnARGAFFGL-TLSHTRAH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 399 FMLTQLYA-AFApLQLGMDILvNEEHVQTDVMIAQGGLFRTPViGQQVLANALNIPITVMStAGEGGPWGMAVLANFACR 477
Cdd:COG1070 370 LARAVLEGvAFA-LRDGLEAL-EEAGVKIDRIRATGGGARSPL-WRQILADVLGRPVEVPE-AEEGGALGAALLAAVGLG 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 764618287 478 QTAmNLEDFLDQEVfkePESMTLSPEPERVAGYREFIQRYQAGLPVEAA 526
Cdd:COG1070 446 LYD-DLEEAAAAMV---RVGETIEPDPENVAAYDELYERYRELYPALKP 490
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
276-476 |
1.02e-31 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 120.89 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 276 GNISVGTSAFSMNVLDKPLskvyRDIDIVMTPDGS-----PVAMVHVNNCSSDINAWATIFREFAARLGMELKPDRLYEt 350
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPV----LSVHGVWGPYTNemlpgYWGLEGGQSAAGSLLAWLLQFHGLREELRDAGNVESLAE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 351 lfLESTRADADAGGLANYSYQSGENITKIQAGRPLFVRTPNSKFSLPNFMLTQLYAAFAPLQLGMDILVNEEHVQTDVMI 430
Cdd:pfam02782 76 --LAALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764618287 431 AQGGLFRTPVIgQQVLANALNIPITVMSTAgEGGPWGMAVLANFAC 476
Cdd:pfam02782 154 VSGGGSRNPLL-LQLLADALGLPVVVPGPD-EATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
17-472 |
8.54e-25 |
|
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: 106.11 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWENQFVDGTWT-YALEDVWTGIQQSYTQLAADVRSkyhmSLKHINAIGISAM 95
Cdd:cd00366 3 LGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAeQDPEDWWQAVVEAIREVLAKAGI----DPSDIAAIGISGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 96 MHGYLAFDQQAKLLVPFRTWrnnitgqaadeltelfdfnMPQRWSIAHLyqailnneahvkqvdfittlAGYVTWKLSGE 175
Cdd:cd00366 79 MPGVVLVDADGNPLRPAIIW-------------------LDRRAKFLQP--------------------NDYIVFRLTGE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 176 KVLGIGDASGVFPIDETTDTYNQTMLTKFsqldkvkpyswDI-RHILPRVLPAGAIAGKLTAAGASLLdqsGtLDAGSVI 254
Cdd:cd00366 120 FAIDYSNASGTGLYDIKTGDWSEELLDAL-----------GIpREKLPPIVESGEVVGRVTPEAAEET---G-LPAGTPV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 255 APPEGDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPLSKVYRdidiVMTPDGSPVAMVHVNNCssdINAWATIFREF 334
Cdd:cd00366 185 VAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPR----LLNRCHVVPGLWLLEGA---INTGGASLRWF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 335 AARLGMELKPDRLYETLFLESTRADADAGGLANYSYQSGEnitkiqagrplfvRTPNskfslPN-------FMLT----- 402
Cdd:cd00366 258 RDEFGEEEDSDAEYEGLDELAAEVPPGSDGLIFLPYLSGE-------------RSPI-----WDpaargvfFGLTlshtr 319
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764618287 403 -QLY------AAFApLQLGMDILvNEEHVQTDVMIAQGGLFRTPVIgQQVLANALNIPITVMSTAgEGGPWGMAVLA 472
Cdd:cd00366 320 aHLIravlegVAYA-LRDNLEIL-EELGVKIKEIRVTGGGAKSRLW-NQIKADVLGVPVVVPEVA-EGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
17-519 |
9.77e-23 |
|
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: 101.08 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYvwenqfvdgtwTYAL------------EDVWTGIQQSytqlAADVRSKYHMSL 84
Cdd:cd07808 3 LGIDLGTSSVKAVLVDEDGRVLASASA-----------EYPTsspkpgwaeqdpEDWWQATKEA----LRELLAKAGISP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 85 KHINAIGISAMMHGYLAFDQQAKLLVPFRTW---RnniTGQAADELTELFDFNMPQR--------WSIAHLYQaILNNEA 153
Cdd:cd07808 68 SDIAAIGLTGQMHGLVLLDKNGRPLRPAILWndqR---SAAECEELEARLGDEILIItgnpplpgFTLPKLLW-LKENEP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 154 HV-KQVDFITTLAGYVTWKLSGEKVLGIGDASGVFPIDETTDTYNQTMLTKFsQLDkvkpyswdiRHILPRVLPAGAIAG 232
Cdd:cd07808 144 EIfARIRKILLPKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEAL-GLD---------PSILPPIVESTEIVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 233 KLTAAGASLLDqsgtLDAGSVIAPPEGDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPLSKVYRDI----DIVmtpD 308
Cdd:cd07808 214 TLTPEAAEELG----LPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLhtfpHAV---P 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 309 GSPVAMVHVNNCSSDINAWATIFrefaarlgmeLKPDRLYETLFLESTRADADAGGLANYSYQSGEnitkiqagrplfvR 388
Cdd:cd07808 287 GKWYAMGVTLSAGLSLRWLRDLF----------GPDRESFDELDAEAAKVPPGSEGLLFLPYLSGE-------------R 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 389 TPnskfslpnFMLTQLYAAFaplqLGMDILVNEEHVQT--------------DVMIAQGGLFRTPVIG---------QQV 445
Cdd:cd07808 344 TP--------YWDPNARGSF----FGLSLSHTRAHLARavlegvafslrdslEVLKELGIKVKEIRLIgggaksplwRQI 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764618287 446 LANALNIPITVMSTAgEGGPWGMAVLANFACRQtAMNLEDFLDQEVfkePESMTLSPEPERVAGYREFIQRYQA 519
Cdd:cd07808 412 LADVLGVPVVVPAEE-EGSAYGAALLAAVGAGV-FDDLEEAAAACI---KIEKTIEPDPERHEAYDELYARYRE 480
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
17-517 |
1.02e-22 |
|
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: 101.06 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWENQFVDGTWtyA---LEDVWTGIQQSytqlAADVRSKYHMSLKHINAIGIS 93
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGW--AeqdPEDWWDAVCRA----TRALLEKSGIDPSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 94 AMMHGYLAFDQQAKLLvpfrtwRNNIT---GQAADELTELFD-FNMPQRW------------SIAHLYqAILNNEAHV-K 156
Cdd:cd07805 77 GQMQGVVPVDKDGNPL------RNAIIwsdTRAAEEAEEIAGgLGGIEGYrlgggnppsgkdPLAKIL-WLKENEPEIyA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 157 QVDFITTLAGYVTWKLSGEKVLGIGDASGVFPIDETTDTYNQTMLtKFSQLDKVKpyswdirhiLPRVLPAGAIAGKLTA 236
Cdd:cd07805 150 KTHKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELL-RAAGIDPDK---------LPELVPSTEVVGELTP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 237 AGASLLDqsgtLDAG-SVIAPPeGDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPLSKvyrdidivmtPDGSPVAMV 315
Cdd:cd07805 220 EAAAELG----LPAGtPVVGGG-GDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTD----------PDHGIFTLA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 316 HVNncSSDINAWATIFR-----EFAAR--LGMELKPDRLYETLFLESTRADADAGGLanysyqsgenitkiqagrpLFV- 387
Cdd:cd07805 285 SAD--PGRYLLAAEQETaggalEWARDnlGGDEDLGADDYELLDELAAEAPPGSNGL-------------------LFLp 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 388 -----RTPnskFSLPN-----FMLT------QLYAA------FApLQLGMDIlVNEEHVQTDVMIAQGGLFRTPVIgQQV 445
Cdd:cd07805 344 wlngeRSP---VEDPNargafIGLSlehtraDLARAvlegvaFN-LRWLLEA-LEKLTRKIDELRLVGGGARSDLW-CQI 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764618287 446 LANALNIPITVMSTAGEGGPWGMAVLAnfacrQTAMNLEDFLDQEVFKEPESMTLSPEPERVAGYREFIQRY 517
Cdd:cd07805 418 LADVLGRPVEVPENPQEAGALGAALLA-----AVGLGLLKSFDEAKALVKVEKVFEPDPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
17-519 |
4.36e-22 |
|
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: 99.17 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWENQFVDGTW-TYALEDVWTGIQQSYTQLAADVRSKyhmslkHINAIGISAM 95
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWaEQDPEEILEAVLEALKEVLAKLGGG------EVDAIGFSSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 96 MHGYLAFDQQAKLLVPFRTW---RnnITGQAADELTELFDFNMPQR-----------WSIAHLYQailNNEAHVKQVDFI 161
Cdd:cd07770 77 MHSLLGVDEDGEPLTPVITWadtR--AAEEAERLRKEGDGSELYRRtgcpihpmyplAKLLWLKE---ERPELFAKAAKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 162 TTLAGYVTWKLSGEKVLGIGDAS--GVFPIDetTDTYNQTMLtKFSQLDKVKpyswdirhiLPRVLPAGAIAGKLTAAGA 239
Cdd:cd07770 152 VSIKEYLLYRLTGELVTDYSTASgtGLLNIH--TLDWDEEAL-ELLGIDEEQ---------LPELVDPTEVLPGLKPEFA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 240 SLLDqsgtLDAGSVIAPPEGDAGTGMVGTNSVRKRTGNISVGTSAfSMNVL-DKPLSKV------YRdID----IVmtpd 308
Cdd:cd07770 220 ERLG----LLAGTPVVLGASDGALANLGSGALDPGRAALTVGTSG-AIRVVsDRPVLDPpgrlwcYR-LDenrwLV---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 309 GSPvamvhVNNCSSdinawatIFREFAARLGMElkpDRLYETLFLESTRADADAGGLANYSYQSGEnitkiqagrplfvR 388
Cdd:cd07770 290 GGA-----INNGGN-------VLDWLRDTLLLS---GDDYEELDKLAEAVPPGSHGLIFLPYLAGE-------------R 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 389 TP--NSKFSlpnfmltqlyAAFAPLQLG---------------------MDILvnEEHVQTDVMI-AQGGLFRTPVIgQQ 444
Cdd:cd07770 342 APgwNPDAR----------GAFFGLTLNhtradilravlegvafnlksiYEAL--EELAGPVKEIrASGGFLRSPLW-LQ 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764618287 445 VLANALNIPITVmSTAGEGGPWGMAVLANFAcrqtamnLEDFLDQEVFKEPE-SMTLSPEPERVAGYREFIQRYQA 519
Cdd:cd07770 409 ILADVLGRPVLV-PEEEEASALGAALLALEA-------LGLISSLEADELVKiGKVVEPDPENHAIYAELYERFKK 476
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
17-267 |
3.52e-18 |
|
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: 83.93 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWENQFVDGTWT-YALEDVWtgiqQSYTQLAADVRSKYHMSLKHINAIGISAM 95
Cdd:pfam00370 3 LGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAeQDPDEIW----QAVAQCIAKTLSQLGISLKQIKGIGISNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 96 MHGYLAFDQQAKLLVPFRTWRNNITGQAADELTElfDFNMPQRWSIAHLYQA----------ILNNEAHV-KQVDFITTL 164
Cdd:pfam00370 79 GHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWpgftlsklrwIKENEPEVfEKIHKFLTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 165 AGYVTWKLSGEKVLGIGDASGvfpidettdtynqTMLTKFSQLDkvkpysWDI---------RHILPRVLPAGAIAGKLT 235
Cdd:pfam00370 157 HDYLRWRLTGVFVTDHTNASR-------------SMMFNIHKLD------WDPellaalgipRDHLPPLVESSEIYGELN 217
|
250 260 270
....*....|....*....|....*....|..
gi 764618287 236 AAGASLLDqsgtLDAGSVIAPPEGDAGTGMVG 267
Cdd:pfam00370 218 PELAAMWG----LDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
17-472 |
7.14e-16 |
|
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: 79.94 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGS--YVWENQfVDGTWTYALEDVWTGIQQSYTQLAADVRskyhmsLKHINAIGISA 94
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILASASreTPLIHP-GPGWAELDPEELWEAVKEAIREAAAQAG------PDPIAAISVSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 95 MMHGYLAFDQQAKLLVPFRTWRNNITGQAADELTELFDFNMPQR---------WSIAHLyQAILNNEAHV-KQVDFITTL 164
Cdd:cd07773 76 QGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRitglppspmYSLAKL-LWLREHEPEIfAKAAKWLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 165 AGYVTWKLSGEKVLGIGDAS--GVFpiDETTDTYNqTMLTKFSQLDkvkpyswdiRHILPRVLPAGAIAGKLTAAGASLL 242
Cdd:cd07773 155 ADYIAYRLTGEPVTDYSLASrtMLF--DIRKRTWS-EELLEAAGID---------ASLLPELVPSGTVIGTVTPEAAEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 243 DqsgtLDAG-SVIAppeG--DAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPLS---KVYRDIDIVMTPDGSPVAMvH 316
Cdd:cd07773 223 G----LPAGtPVVV---GghDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLdemLAEGGLSYGHHVPGGYYYL-A 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 317 VNNCSSDINAWatifreFAARLGMELKPDRLYETLFLEstrADADAGGLANYSYQSGenitkiqAGRPLFvrTPNSKFSL 396
Cdd:cd07773 295 GSLPGGALLEW------FRDLFGGDESDLAAADELAEA---APPGPTGLLFLPHLSG-------SGTPDF--DPDARGAF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 397 PNFMLT----QLYAA------FApLQLGMDILvNEEHVQTDVMIAQGGLFRTPVIgQQVLANALNIPITVMSTAgEGGPW 466
Cdd:cd07773 357 LGLTLGttraDLLRAileglaFE-LRLNLEAL-EKAGIPIDEIRAVGGGARSPLW-LQLKADILGRPIEVPEVP-EATAL 432
|
....*.
gi 764618287 467 GMAVLA 472
Cdd:cd07773 433 GAALLA 438
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-472 |
7.97e-15 |
|
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: 76.49 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 15 VSLGIELGSTRIKAVLI-TDDFNTIASGSYVwENQFVDGTWTYA----LEDVWTGIQQSYTQLAADVRSKyhmslkhINA 89
Cdd:cd07777 1 NVLGIDIGTTSIKAALLdLESGRILESVSRP-TPAPISSDDPGRseqdPEKILEAVRNLIDELPREYLSD-------VTG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 90 IGISAMMHGYLAFDQQAKLLVPFRTWRNnitgQAADE---LTELFDFNMPQRWS---------IAHLYqAILNNEAHVKQ 157
Cdd:cd07777 73 IGITGQMHGIVLWDEDGNPVSPLITWQD----QRCSEeflGGLSTYGEELLPKSgmrlkpgygLATLF-WLLRNGPLPSK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 158 VDFITTLAGYVTWKLSGEKVLGIGD----ASGVFpiDETTDTYNQTMLTK--FSQldkvkpyswdirHILPRVLPAGAIA 231
Cdd:cd07777 148 ADRAGTIGDYIVARLTGLPKPVMHPtnaaSWGLF--DLETGTWNKDLLEAlgLPV------------ILLPEIVPSGEIV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 232 GKLTAAGAslldqsgtldAGSVIAPPEGDAGTGMVGTNSVRKRTGNISVGTSA---FSMNVLDKPlskvyRDIDIVMTPD 308
Cdd:cd07777 214 GTLSSALP----------KGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAqlsFLTPKFELS-----GSVEIRPFFD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 309 GSPVAMV-HVN--NcssDINAWATIFREFAARLGMELKPDRLYETLfLESTRADADAGGLANYSYQsGENITKIQAGRPL 385
Cdd:cd07777 279 GRYLLVAaSLPggR---ALAVLVDFLREWLRELGGSLSDDEIWEKL-DELAESEESSDLSVDPTFF-GERHDPEGRGSIT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 386 FVRTPNskFSLPNF-------MLTQLYAAFAPLQLGmdilvnEEHVQTdVMIAQGGLFRTPVIgQQVLANALNIPItVMS 458
Cdd:cd07777 354 NIGESN--FTLGNLfralcrgIAENLHEMLPRLDLD------LSGIER-IVGSGGALRKNPVL-RRIIEKRFGLPV-VLS 422
|
490
....*....|....
gi 764618287 459 TAGEGGPWGMAVLA 472
Cdd:cd07777 423 EGSEEAAVGAALLA 436
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
17-523 |
2.67e-13 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 71.92 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSY---------VWENQfvdgtwtyALEDVWTGIQQSYTQLAAdvrskyHMSLKHI 87
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEkltvsrphpLWSEQ--------DPEQWWQATDRAMKALGD------QHSLQDV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 88 NAIGISAMMHGYLAFDQQAKLLVPFRTWRNnitGQAADElTELFDFNMPQRWSI----------AHLYQAILNNEAHV-K 156
Cdd:PRK15027 69 KALGIAGQMHGATLLDAQQRVLRPAILWND---GRCAQE-CALLEARVPQSRVItgnlmmpgftAPKLLWVQRHEPEIfR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 157 QVDFITTLAGYVTWKLSGEKVLGIGDASGVFPIDETTDTYNQTMLTKfSQLDkvkpyswdiRHILPRVLPAGAIAGKLTA 236
Cdd:PRK15027 145 QIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQA-CHLS---------RDQMPALYEGSEITGALLP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 237 AGAslldQSGTLDAGSVIAPpEGDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPLSKvyrdidivmtpdgsPVAMVH 316
Cdd:PRK15027 215 EVA----KAWGMATVPVVAG-GGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSK--------------PESAVH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 317 vNNCSSDINAW--------ATIFREFAARL-GMELKPdrlyeTLFLESTRADADAGGLANYSYQSGEnitkiqagrplfv 387
Cdd:PRK15027 276 -SFCHALPQRWhlmsvmlsAASCLDWAAKLtGLSNVP-----ALIAAAQQADESAEPVWFLPYLSGE------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 388 RTP--NSKFSLPNFMLTQLYaafAPLQL--------------GMDIlVNEEHVQTDVMIAQGGLFRTPViGQQVLANALN 451
Cdd:PRK15027 337 RTPhnNPQAKGVFFGLTHQH---GPNELaravlegvgyaladGMDV-VHACGIKPQSVTLIGGGARSEY-WRQMLADISG 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764618287 452 IPITvMSTAGEGGP-WGMAVLAnfacrQTAMNLEDFLDQEVFKEPESMTLSPEPERVAGYRE----FIQRYQAGLPV 523
Cdd:PRK15027 412 QQLD-YRTGGDVGPaLGAARLA-----QIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPrretFRRLYQQLLPL 482
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
17-472 |
2.84e-13 |
|
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: 71.78 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWENQFVDGTWT-YALEDVWTGIQQSYTQLAAdvRSKYHMslKHINAIGISAM 95
Cdd:cd07779 3 LGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVeQDPDDWWDALCEALKEAVA--KAGVDP--EDIAAIGLTSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 96 MHGYLAFDQQAKLLVPFRTWrnnitgqaadeltelfdfnMPQRwsiahlyqailnneahvkqVDFITTLAGYVTWKLSGE 175
Cdd:cd07779 79 RSTFVPVDEDGRPLRPAISW-------------------QDKR-------------------TAKFLTVQDYLLYRLTGE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 176 KVLGIGDASGVFPIDETTDTYNQTMLTKFSqLDKVKpyswdirhiLPRVLPAGAIAGKLTAAGASLLDqsgtLDAGSVIA 255
Cdd:cd07779 121 FVTDTTSASRTGLPDIRTRDWSDDLLDAFG-IDRDK---------LPELVPPGTVIGTLTKEAAEETG----LPEGTPVV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 256 PPEGDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKPlskvYRDIDIVMTPDGSPV-----AMVHVNNCSSDINaWati 330
Cdd:cd07779 187 AGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKP----VEDPERRIPCNPSAVpgkwvLEGSINTGGSAVR-W--- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 331 FR-EFAARLGMELKPDR-LYETLFLESTRADADAGGLANYSYQSGenitkiqAGRPLFVrtPNSKFSLPNFMLTQLYA-- 406
Cdd:cd07779 259 FRdEFGQDEVAEKELGVsPYELLNEEAAKSPPGSDGLLFLPYLAG-------AGTPYWN--PEARGAFIGLTLSHTRAhl 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764618287 407 --------AFApLQLGMDiLVNEEHVQTDVMIAQGGLFRTPVIGqQVLANALNIPITVMSTAgEGGPWGMAVLA 472
Cdd:cd07779 330 arailegiAFE-LRDNLE-AMEKAGVPIEEIRVSGGGSKSDLWN-QIIADVFGRPVERPETS-EATALGAAILA 399
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
17-476 |
5.10e-13 |
|
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: 71.02 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYvwenqfvdgtwTYALE-----------DVWTGiqqSYTQLAADVRSKYHMSLK 85
Cdd:cd07804 3 LGIDIGTTGTKGVLVDEDGKVLASASI-----------EHDLLtpkpgwaehdpEVWWG---AVCEIIRELLAKAGISPK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 86 HINAIGISAMMHGYLAFDQQAKLLVPFRTWRNNITGQAADELTELFDFNMPQRWSIAHL-YQAIL-------NNEAHV-K 156
Cdd:cd07804 69 EIAAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLdSQSVGpkllwikRNEPEVfK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 157 QVDFITTLAGYVTWKLSGEKVLGIGDA---SGVFPIDetTDTYNQTMLTKFSQLDKvkpyswdirhILPRVLPAGAIAGK 233
Cdd:cd07804 149 KTRKFLGAYDYIVYKLTGEYVIDYSSAgneGGLFDIR--KRTWDEELLEALGIDPD----------LLPELVPSTEIVGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 234 LTAAGAsllDQSGtLDAGSVIAPPEGDAGTGMVGTNSVrkRTGN--ISVGTSAFSMNVLDKPlskvYRDIDIVMTPdgsp 311
Cdd:cd07804 217 VTKEAA---EETG-LAEGTPVVAGTVDAAASALSAGVV--EPGDllLMLGTAGDIGVVTDKL----PTDPRLWLDY---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 312 vamvHVNNCSSDINAWATI-------FR-EFAARLGMELKPDRL--YETLFLESTRADADAGGLANYSYQSGEnitkiqa 381
Cdd:cd07804 283 ----HDIPGTYVLNGGMATsgsllrwFRdEFAGEEVEAEKSGGDsaYDLLDEEAEKIPPGSDGLIVLPYFMGE------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 382 grplfvRTP----NSKFSLpnFMLT------QLY------AAFApLQLGMDILVNEEHVQTDVMIAQGG----LFRtpvi 441
Cdd:cd07804 352 ------RTPiwdpDARGVI--FGLTlshtraHLYrallegVAYG-LRHHLEVIREAGLPIKRLVAVGGGakspLWR---- 418
|
490 500 510
....*....|....*....|....*....|....*
gi 764618287 442 gqQVLANALNIPITVMSTAgEGGPWGMAVLANFAC 476
Cdd:cd07804 419 --QIVADVTGVPQEYVKDT-VGASLGDAFLAGVGV 450
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
17-283 |
3.25e-11 |
|
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: 65.32 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWENQFVDGTWTYAL-EDVWTGIQQSYTQLAADVRskyhmsLKHINAIGISAM 95
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDpEDWWEALRSLLRELPAELR------PRRVVAIAVDGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 96 MHGYLAFDQQAKLLVPFRTWRNNITGQAADELTELFDFNMPQR-------WSIAHLYqAILNNEAHV-KQVDFITTLAGY 167
Cdd:cd07783 77 SGTLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTglavspsSSLAKLL-WLKRHEPEVlAKTAKFLHQADW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 168 VTWKLSGEKVlgigdasgvfpideTTDTYNQTMLTkfsqLD-KVKPYSWDIR-------HILPRVLPAGAIAGKLTAAGA 239
Cdd:cd07783 156 LAGRLTGDRG--------------VTDYNNALKLG----YDpETGRWPSWLLallgippDLLPRVVAPGTVIGTLTAEAA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 764618287 240 SLLdqsGtLDAG-SVIAppeG--DAGTGMVGTNSVRKRTGNISVGTS 283
Cdd:cd07783 218 EEL---G-LPAGtPVVA---GttDSIAAFLASGAVRPGDAVTSLGTT 257
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
15-519 |
5.30e-11 |
|
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: 64.87 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 15 VSLGIELGSTRIKAVLI-TDDFNTIASGSYVWENQFVDGTWTYAL---EDVWTGIQQSYTQLAADVRSkyhmSLKHINAI 90
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVdLADGEELASAVVPYPTGYIPPRPGWAEqnpADYWEALEEAVRGALAEAGV----DPEDVVGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 91 GI----SAMmhgyLAFDQQAKLLVPFRTWRNNiTGQA-ADELTELFDFNMPQR-----------WSIAHLYQaILNNEAH 154
Cdd:cd07781 77 GVdttsSTV----VPVDEDGNPLAPAILWMDH-RAQEeAAEINETAHPALEYYlayyggvysseWMWPKALW-LKRNAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 155 V-KQVDFITTLAGYVTWKLSGEKVLGIGDAS---------GVFPIDEttdtynqtmltkfsqLDKVKPYSWDIRHILP-R 223
Cdd:cd07781 151 VyDAAYTIVEACDWINARLTGRWVRSRCAAGhkwmynewgGGPPREF---------------LAALDPGLLKLREKLPgE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 224 VLPAGAIAGKLTAAGASLLDqsgtLDAGSVIAPPEGDAGTGMVGTNSVrkRTGNISV--GTSAFSMNVLDKP-----LSK 296
Cdd:cd07781 216 VVPVGEPAGTLTAEAAERLG----LPAGIPVAQGGIDAHMGAIGAGVV--EPGTLALimGTSTCHLMVSPKPvdipgICG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 297 VYRDidiVMTPD------GSPvamvhvnnCSSDINAWatiFREFAARLGMElKPDRLYETLFLESTRADADAGGLANYSY 370
Cdd:cd07781 290 PVPD---AVVPGlygleaGQS--------AVGDIFAW---FVRLFVPPAEE-RGDSIYALLSEEAAKLPPGESGLVALDW 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 371 QSGenitkiqagrplfVRTPnskfsLPNFMLTqlyAAFAPLQLGMD------------------IL--VNEEHVQTDVMI 430
Cdd:cd07781 355 FNG-------------NRTP-----LVDPRLR---GAIVGLTLGTTpahiyralleatafgtraIIerFEEAGVPVNRVV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 431 AQGGL-FRTPVIgQQVLANALNIPITVMSTAgEGGPWGMAVLANFACRQTAmNLEDflDQEVFKEPESmTLSPEPERVAG 509
Cdd:cd07781 414 ACGGIaEKNPLW-MQIYADVLGRPIKVPKSD-QAPALGAAILAAVAAGVYA-DIEE--AADAMVRVDR-VYEPDPENHAV 487
|
570
....*....|
gi 764618287 510 YREFIQRYQA 519
Cdd:cd07781 488 YEELYALYKE 497
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
17-472 |
6.19e-11 |
|
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: 64.49 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYvwENQFV---DGTWTYALEDVWTG----IQQSYTQLAADVrskyhmslKHINA 89
Cdd:cd07802 3 LGIDNGTTNVKAVLFDLDGREIAVASR--PTPVIsprPGWAERDMDELWQAtaeaIRELLEKSGVDP--------SDIAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 90 IGISAMMHGYLAFDQQAKllvPFRtwrNNIT---GQAADELTELFDFNMPQRWSiAHLYQ--------AIL----NNEAH 154
Cdd:cd07802 73 VGVTGHGNGLYLVDKDGK---PVR---NAILsndSRAADIVDRWEEDGTLEKVY-PLTGQplwpgqpvALLrwlkENEPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 155 V-KQVDFITTLAGYVTWKLSGEKVLGIGDASGVFpIDETTDTYNQTMLTKFSqLDkvkpyswDIRHILPRVLPAGAIAGK 233
Cdd:cd07802 146 RyDRIRTVLFCKDWIRYRLTGEISTDYTDAGSSL-LDLDTGEYDDELLDLLG-IE-------ELKDKLPPLVPSTEIAGR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 234 LTAAGASLLD-QSGTLDAGSVIappegDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKP-------LSKVYRDIDIVM 305
Cdd:cd07802 217 VTAEAAALTGlPEGTPVAAGAF-----DVVASALGAGAVDEGQLCVILGTWSINEVVTDEPvvpdsvgSNSLHADPGLYL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 306 TPDGSPvamvhvnncSSDIN-AWATifREFAARLGMELKPDrlYETLFLESTRADADAGGL--ANYSYQSGENitkiqag 382
Cdd:cd07802 292 IVEASP---------TSASNlDWFL--DTLLGEEKEAGGSD--YDELDELIAAVPPGSSGVifLPYLYGSGAN------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 383 rplfvrtPNSKFSLpnFMLTQ-------LYA-----AFApLQLGMDILVNEEHVQTdVMIAqGGLFRTPVIGqQVLANAL 450
Cdd:cd07802 352 -------PNARGGF--FGLTAwhtrahlLRAvyegiAFS-HRDHLERLLVARKPET-IRLT-GGGARSPVWA-QIFADVL 418
|
490 500
....*....|....*....|..
gi 764618287 451 NIPITVMSTAgEGGPWGMAVLA 472
Cdd:cd07802 419 GLPVEVPDGE-ELGALGAAICA 439
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
17-294 |
3.04e-10 |
|
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: 62.24 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWEnQFVDGTWTYALE----DVWTGIqqsyTQLAADVRSKYHMSLKHINAIGI 92
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWE-YYTDDDYPDAKEfdpeELWEKI----CEAIREALKKAGISPEDISAVSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 93 SAMMHGYLAFDQQAKLL--VPfrtwrnNITGQAADELTELFDFNMPQRWSIAHLYQAIL----------NNEAHV-KQVD 159
Cdd:cd07798 78 TSQREGIVFLDKDGRELyaGP------NIDARGVEEAAEIDDEFGEEIYTTTGHWPTELfpaarllwfkENRPEIfERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 160 FITTLAGYVTWKLSGEKVLGIGDASGVFPIDETTDTYNQTMLTKFsQLDkvkpyswdiRHILPRVLPAGAIAGKLTAAGA 239
Cdd:cd07798 152 TVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEAL-GLP---------PEILPEIVPSGTVLGTVSEEAA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 764618287 240 SLLDqsgtLDAGSVIAPPEGDAGTGMVGTNSVrkRTGNISV--GTSAFSMNVLDKPL 294
Cdd:cd07798 222 RELG----LPEGTPVVVGGADTQCALLGSGAI--EPGDIGIvaGTTTPVQMVTDEPI 272
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
17-293 |
3.07e-09 |
|
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: 59.18 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVWENQFVDGTW-TYALEDVWTGIQQSYTQLAADVRSKYHmslkHINAIGISA- 94
Cdd:cd24121 3 IGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWaEQDMNETWQAVVATIREVVAKLDVLPD----RVAAIGVTGq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 95 -----MM--------HGYLAFDQQAKLLVpfRTWRNNITGQAADELT--ELFDFNmpQRWSIAHLYQailNNEAHVKQVD 159
Cdd:cd24121 79 gdgtwLVdedgrpvrDAILWLDGRAADIV--ERWQADGIAEAVFEITgtGLFPGS--QAAQLAWLKE---NEPERLERAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 160 FITTLAGYVTWKLSGEKVLGIGDASGVFpIDETTDTYNQTMLTKFSQLDkvkpyswdIRHILPRVLPAGAIAGKLTAAGA 239
Cdd:cd24121 152 TALHCKDWLFYKLTGEIATDPSDASLTF-LDFRTRQYDDEVLDLLGLEE--------LRHLLPPIRPGTEVIGPLTPEAA 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 764618287 240 SLLDqsgtLDAGS-VIAPPEgDAGTGMVGTNSVRKRTGNISVGTSAFSMNVLDKP 293
Cdd:cd24121 223 AATG----LPAGTpVVLGPF-DVVATALGSGAIEPGDACSILGTTGVHEVVVDEP 272
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
17-272 |
5.64e-07 |
|
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: 51.95 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 17 LGIELGSTRIKAVLITDDFNTIASGSYVW---ENQFVDGTWTYALEDVWTGIQQsytqLAADVRSKYHMSLKHINAIGIS 93
Cdd:cd07775 3 LALDAGTGSGRAVIFDLEGNQIAVAQREWrhkEVPDVPGSMDFDTEKNWKLICE----CIREALKKAGIAPKSIAAISTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 94 AMMHGYLAFDQQAKLLvpfrtWR-NNITGQAADELTEL------FDFNM----PQRWSIAHLyqAIL----NNEAHV-KQ 157
Cdd:cd07775 79 SMREGIVLYDNEGEEI-----WAcANVDARAAEEVSELkelyntLEEEVyrisGQTFALGAI--PRLlwlkNNRPEIyRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 158 VDFITTLAGYVTWKLSGEKVL--GIGDASGVFpidettDTYNQTMLTKFSQLDKVKPYswdirhILPRVLPAGAIAGKLT 235
Cdd:cd07775 152 AAKITMLSDWIAYKLSGELAVepSNGSTTGLF------DLKTRDWDPEILEMAGLKAD------ILPPVVESGTVIGKVT 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 764618287 236 AAGASLLDqsgtLDAGSVIAPPEGDAGTGMVGTNSVR 272
Cdd:cd07775 220 KEAAEETG----LKEGTPVVVGGGDVQLGCLGLGVVR 252
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
102-282 |
4.22e-06 |
|
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: 49.06 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 102 FDQQAKLLVPFRTWRNNITGQAADELT------ELFDF--NMPQRW-SIAHLYQAILNNEAHVKQVDFITTLAGYVTWKL 172
Cdd:cd07771 83 LDKNGELLGNPVHYRDPRTEGMMEELFekiskeELYERtgIQFQPInTLYQLYALKKEGPELLERADKLLMLPDLLNYLL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 173 SGEKVLGIGDASgvfpideTT-------DTYNQTMLTKFSqLDkvkpyswdiRHILPRVLPAGAIAGKLTAAGASLLDQS 245
Cdd:cd07771 163 TGEKVAEYTIAS-------TTqlldprtKDWSEELLEKLG-LP---------RDLFPPIVPPGTVLGTLKPEVAEELGLK 225
|
170 180 190
....*....|....*....|....*....|....*..
gi 764618287 246 GTldagSVIAPPEGDAGTGMVGTNSVRKRTGNISVGT 282
Cdd:cd07771 226 GI----PVIAVASHDTASAVAAVPAEDEDAAFISSGT 258
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
420-519 |
5.53e-05 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 45.99 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764618287 420 NEEHVQTDVMIAQGGLFR-TPVIgQQVLANALNIPITVMsTAGEGGPWGMAVLANFAcrqtAMNLEDFLD-QEVFKEPES 497
Cdd:PRK04123 433 EDQGVPVEEVIAAGGIARkNPVL-MQIYADVLNRPIQVV-ASDQCPALGAAIFAAVA----AGAYPDIPEaQQAMASPVE 506
|
90 100
....*....|....*....|..
gi 764618287 498 MTLSPEPERVAGYREFIQRYQA 519
Cdd:PRK04123 507 KTYQPDPENVARYEQLYQEYKQ 528
|
|
| |
