|
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 |
3.67e-161 |
|
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: 465.49 E-value: 3.67e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 15 VSLAIELGSTRIKAVLITS-DFKTIASGSYQWENQFENE-VWTYNLDQVWEGIRDSYKQLSAEVESKyhtnLTKIDNVGI 92
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAeTGRVVASGSAPHENILIDPgWAEQDPEDWWDALQAAFAQLLKDAGAE----LRDVAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 93 SAMMHGYLAFSKEDELLVPFRTWRNNITGPATDQLTELFNF--------NVPQRWCIAHLYQAILNQEEHVDKISFLTTL 164
Cdd:cd07809 77 SGQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGkkcllvglNIPARFTASKLLWLKENEPEHYARIAKILLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 165 SGYVHWQLTGEKVLGIGDASGAFPIDETKGDYDETFMKKFSQldevqqySWETREIFPKVLKAGEDAGRLSEAGAKLLDp 244
Cdd:cd07809 157 HDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDP-------SRDLRDLLPEVLPAGEVAGRLTPEGAEELG- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 245 lghLQSGSRMAPPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPLQKVHreiDIVTTPAGTNVAMVHADNCSSDI 324
Cdd:cd07809 229 ---LPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPH---GRVATFCDSTGGMLPLINTTNCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 325 DAWAQIFQQFAerlgiQLSPEQLYETlfldASKADPDAGGLFNYSYLSGEVITEVDDGRPMFVRTINSNFNLPNFIQTQL 404
Cdd:cd07809 303 TAWTELFRELL-----GVSYEELDEL----AAQAPPGAGGLLLLPFLNGERTPNLPHGRASLVGLTLSNFTRANLARAAL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2532437739 405 YGAFAPLAIGMDTLTEDEqIKLDVMIAHGGLFKTPViAQQVLANALNTPISVMETaGEGGSWGMAVLAAYMAK 477
Cdd:cd07809 374 EGATFGLRYGLDILRELG-VEIDEIRLIGGGSKSPV-WRQILADVFGVPVVVPET-GEGGALGAALQAAWGAG 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
17-525 |
1.14e-112 |
|
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: 343.35 E-value: 1.14e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWENQFENEVW-TYNLDQVWEGIRDSYKQLSAEVeskyHTNLTKIDNVGISAM 95
Cdd:COG1070 4 LGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWaEQDPEDWWEAVVEAIRELLAKA----GVDPEEIAAIGVSGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 96 MHGYLAFSKEDELLVPFRTWRNNITGPATDQLTELFNF--------NVPQR-WCIAHLYQAILNQEEHVDKISFLTTLSG 166
Cdd:COG1070 80 MHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEealyeitgNPLHPgFTAPKLLWLKENEPEIFARIAKVLLPKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 167 YVHWQLTGEKVLGIGDASGAFPIDETKGDYDETFMKKFSqldevqqyswETREIFPKVLKAGEDAGRLSEAGAKLldpLG 246
Cdd:COG1070 160 YLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALG----------IDRELLPELVPPGEVAGTLTAEAAAE---TG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 247 hLQSGSRMAPPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPLQKVHREIDIVTTPA-GTNVAMVHADNCSSDID 325
Cdd:COG1070 227 -LPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVpGRWLPMGATNNGGSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 326 AWAQIFQQfaerlgiqlSPEQLYETLFLDASKADPDAGGLFNYSYLSGEVITEVD-DGRPMFVRtINSNFNLPNFIQTQL 404
Cdd:COG1070 306 WFRDLFAD---------GELDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDpNARGAFFG-LTLSHTRAHLARAVL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 405 YG-AFApLAIGMDTLtEDEQIKLDVMIAHGGLFKTPViAQQVLANALNTPISVMEtAGEGGSWGMAVLAAYMAKSLEmSL 483
Cdd:COG1070 376 EGvAFA-LRDGLEAL-EEAGVKIDRIRATGGGARSPL-WRQILADVLGRPVEVPE-AEEGGALGAALLAAVGLGLYD-DL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2532437739 484 EDFLDQEVfaaPETMTLNPEPAGVQGYADYLAQYQAALPAER 525
Cdd:COG1070 451 EEAAAAMV---RVGETIEPDPENVAAYDELYERYRELYPALK 489
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
276-476 |
9.39e-39 |
|
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: 140.54 E-value: 9.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 276 GNISVGTSAFAMVVLDKPLqkvhREIDIVTTPAG-----TNVAMVHADNCSSDIDAWaqiFQQFAERLGIQLSPEQLYET 350
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPV----LSVHGVWGPYTnemlpGYWGLEGGQSAAGSLLAW---LLQFHGLREELRDAGNVESL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 351 LFLDASKADPDAGGLFNYSYLSGEVITEVDDGRPMFVRTINSNFNLPNFIQTQLYGAFAPLAIGMDTLTEDEQIKLDVMI 430
Cdd:pfam02782 74 AELAALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2532437739 431 AHGGLFKTPVIaQQVLANALNTPISVMETAgEGGSWGMAVLAAYMA 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 |
3.39e-31 |
|
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: 124.60 E-value: 3.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWENQFENEVWT-YNLDQVWEGIRDSYKQLSAEVESkyhtNLTKIDNVGISAM 95
Cdd:cd00366 3 LGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAeQDPEDWWQAVVEAIREVLAKAGI----DPSDIAAIGISGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 96 MHGYLAFSKEDELLVPFRTWrnnitgpaTDQltelfnfnvpqRWCIAHLyqailnqeehvdkisflttlSGYVHWQLTGE 175
Cdd:cd00366 79 MPGVVLVDADGNPLRPAIIW--------LDR-----------RAKFLQP--------------------NDYIVFRLTGE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 176 KVLGIGDASGAFPIDETKGDYDETFMKKFsqldevqqysWETREIFPKVLKAGEDAGRLSEAGAKLLdplgHLQSGSRMA 255
Cdd:cd00366 120 FAIDYSNASGTGLYDIKTGDWSEELLDAL----------GIPREKLPPIVESGEVVGRVTPEAAEET----GLPAGTPVV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 256 PPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPLQKVHReidiVTTPAGTNVAMVHADNCssdIDAWAQIFQQFA 335
Cdd:cd00366 186 AGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPR----LLNRCHVVPGLWLLEGA---INTGGASLRWFR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 336 ERLGIQLSPEQLYETLFLDASKADPDAGGLFNYSYLSGEVITEVD-DGRPMFVRtINSNFNLPNFIQTQLYG-AFApLAI 413
Cdd:cd00366 259 DEFGEEEDSDAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDpAARGVFFG-LTLSHTRAHLIRAVLEGvAYA-LRD 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2532437739 414 GMDTLtEDEQIKLDVMIAHGGLFKTPVIAqQVLANALNTPISVMETAgEGGSWGMAVLA 472
Cdd:cd00366 337 NLEIL-EELGVKIKEIRVTGGGAKSRLWN-QIKADVLGVPVVVPEVA-EGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
17-520 |
2.77e-25 |
|
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: 108.78 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSY---------QWENQfENEVWtynldqvWEGIRDSYKQLSAEVESKYHtnltKI 87
Cdd:cd07808 3 LGIDLGTSSVKAVLVDEDGRVLASASAeyptsspkpGWAEQ-DPEDW-------WQATKEALRELLAKAGISPS----DI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 88 DNVGISAMMHGYLAFSKEDELLVPFRTW---RnniTGPATDQLTELFNFNVPQR--------WCIAHLYQAILNQEEHVD 156
Cdd:cd07808 71 AAIGLTGQMHGLVLLDKNGRPLRPAILWndqR---SAAECEELEARLGDEILIItgnpplpgFTLPKLLWLKENEPEIFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 157 KISFLTTLSGYVHWQLTGEKVLGIGDASGAFPIDETKGDYDETFMKKFsQLDevqqyswetREIFPKVLKAGEDAGRLSE 236
Cdd:cd07808 148 RIRKILLPKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEAL-GLD---------PSILPPIVESTEIVGTLTP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 237 AGAKLLDplghLQSGSRMAPPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPLQKVHReiDIVTTP---AGTNVA 313
Cdd:cd07808 218 EAAEELG----LPEGTPVVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKG--RLHTFPhavPGKWYA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 314 MVHADNCSSDIDAWAQIFQQFAERlgiqlspeqlYETLFLDASKADPDAGGLFNYSYLSGEViTEVDDG--RPMFVrTIN 391
Cdd:cd07808 292 MGVTLSAGLSLRWLRDLFGPDRES----------FDELDAEAAKVPPGSEGLLFLPYLSGER-TPYWDPnaRGSFF-GLS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 392 SNFNLPNFIQTQLYG-AFApLAIGMDTLtEDEQIKLDVMIAHGGLFKTPVIAqQVLANALNTPISVMETAgEGGSWGMAV 470
Cdd:cd07808 360 LSHTRAHLARAVLEGvAFS-LRDSLEVL-KELGIKVKEIRLIGGGAKSPLWR-QILADVLGVPVVVPAEE-EGSAYGAAL 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2532437739 471 LAAyMAKSLEMSLEDFLDQEVfaaPETMTLNPEPAGVQGYADYLAQYQAA 520
Cdd:cd07808 436 LAA-VGAGVFDDLEEAAAACI---KIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
17-519 |
1.97e-24 |
|
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: 106.49 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWENQFENEVW-TYNLDQVWEGIRDSYKQLSAEVESKyhtnltKIDNVGISAM 95
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWaEQDPEEILEAVLEALKEVLAKLGGG------EVDAIGFSSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 96 MHGYLAFSKEDELLVPFRTW---RnnitgpATDQLTELFNFNVPQRW-----C----------IAHLYQailNQEEHVDK 157
Cdd:cd07770 77 MHSLLGVDEDGEPLTPVITWadtR------AAEEAERLRKEGDGSELyrrtgCpihpmyplakLLWLKE---ERPELFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 158 ISFLTTLSGYVHWQLTGEKVLGIGDASGA--FPIDetKGDYDETFMkKFSQLDEVQqyswetreiFPKVLKAGEDAGRLS 235
Cdd:cd07770 148 AAKFVSIKEYLLYRLTGELVTDYSTASGTglLNIH--TLDWDEEAL-ELLGIDEEQ---------LPELVDPTEVLPGLK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 236 EAGAKLLDplghLQSGSRMAPPEGDAGTGMIATNSIRKRTGNISVGTSAfAM-VVLDKPlqkvhreidIVTTPAGT---- 310
Cdd:cd07770 216 PEFAERLG----LLAGTPVVLGASDGALANLGSGALDPGRAALTVGTSG-AIrVVSDRP---------VLDPPGRLwcyr 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 311 -------------NVAMVHadncssdidAWAQifQQFaerlgiqLSPEQLYETLFLDASKADPDAGGLFNYSYLSGEVIT 377
Cdd:cd07770 282 ldenrwlvggainNGGNVL---------DWLR--DTL-------LLSGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 378 E-VDDGRPMFVrTINSNFNLPNFIQTQLYG-AFApLAIGMDTLTEDEQIKLDVmIAHGGLFKTPVIaQQVLANALNTPIS 455
Cdd:cd07770 344 GwNPDARGAFF-GLTLNHTRADILRAVLEGvAFN-LKSIYEALEELAGPVKEI-RASGGFLRSPLW-LQILADVLGRPVL 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2532437739 456 VMETAgEGGSWGMAVLAAYmakslemSLEDFLDQEVFAAPE-TMTLNPEPAGVQGYADYLAQYQA 519
Cdd:cd07770 420 VPEEE-EASALGAALLALE-------ALGLISSLEADELVKiGKVVEPDPENHAIYAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
17-517 |
5.32e-21 |
|
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: 96.05 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWENQFENEVWTY-NLDQVWEGIRDSykqlSAEVESKYHTNLTKIDNVGISAM 95
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEqDPEDWWDAVCRA----TRALLEKSGIDPSDIAAIAFSGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 96 MHGYLAFSKEDELLvpfrtwRNNIT------GPATDQLTELFNFNVPQRWCIAHLYQA------IL----NQEEHVDKIS 159
Cdd:cd07805 79 MQGVVPVDKDGNPL------RNAIIwsdtraAEEAEEIAGGLGGIEGYRLGGGNPPSGkdplakILwlkeNEPEIYAKTH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 160 FLTTLSGYVHWQLTGEKVLGIGDASGAFPIDETKGDYDETFMKKFsQLDevqqyswetREIFPKVLKAGEDAGRLSEAGA 239
Cdd:cd07805 153 KFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAA-GID---------PDKLPELVPSTEVVGELTPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 240 KLLdplgHLQSGSRMAPPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPlqKVHREIDIVTTPA---GTNVAMVH 316
Cdd:cd07805 223 AEL----GLPAGTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKP--KTDPDHGIFTLASadpGRYLLAAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 317 ADNCSSDIDaWAqifqqfAERLGIQLS-PEQLYETLFLDASKADPDAGGLFNYSYLSGEvITEVDDG--RPMFvrtinsn 393
Cdd:cd07805 297 QETAGGALE-WA------RDNLGGDEDlGADDYELLDELAAEAPPGSNGLLFLPWLNGE-RSPVEDPnaRGAF------- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 394 FNL-PNFIQTQLY-----G-AFApLAIGMDTLtEDEQIKLDVMIAHGGLFKTPVIAqQVLANALNTPISVMETAGEGGSW 466
Cdd:cd07805 362 IGLsLEHTRADLAravleGvAFN-LRWLLEAL-EKLTRKIDELRLVGGGARSDLWC-QILADVLGRPVEVPENPQEAGAL 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2532437739 467 GMAVLAAymaksLEMSLEDFLDQEVFAAPETMTLNPEPAGVQGYADYLAQY 517
Cdd:cd07805 439 GAALLAA-----VGLGLLKSFDEAKALVKVEKVFEPDPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
17-476 |
3.14e-20 |
|
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: 93.35 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWENQFENEVWT-YNLDQVWEGIRDSYKQLSAEVESkyhtNLTKIDNVGISAM 95
Cdd:cd07779 3 LGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVeQDPDDWWDALCEALKEAVAKAGV----DPEDIAAIGLTSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 96 MHGYLAFSKEDELLVPFRTWrnnitgpatdqltelfnfnvpqrwciahlyqailnQEEHVDKIsflTTLSGYVHWQLTGE 175
Cdd:cd07779 79 RSTFVPVDEDGRPLRPAISW-----------------------------------QDKRTAKF---LTVQDYLLYRLTGE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 176 KVLGIGDASGAFPIDETKGDYDETFMKKFSqLDevqqyswetREIFPKVLKAGEDAGRLSEAGAKLLdplgHLQSGSRMA 255
Cdd:cd07779 121 FVTDTTSASRTGLPDIRTRDWSDDLLDAFG-ID---------RDKLPELVPPGTVIGTLTKEAAEET----GLPEGTPVV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 256 PPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPLQKVHReiDIVTTPA---GTNVAMVHADNCSSDIDaWA--QI 330
Cdd:cd07779 187 AGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPER--RIPCNPSavpGKWVLEGSINTGGSAVR-WFrdEF 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 331 FQQFAERLGIQLSPEQLYETLfldASKADPDAGGLFNYSYLSGEVITEVD-DGRPMFVrtinsNFNL----PNFIQTQLY 405
Cdd:cd07779 264 GQDEVAEKELGVSPYELLNEE---AAKSPPGSDGLLFLPYLAGAGTPYWNpEARGAFI-----GLTLshtrAHLARAILE 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532437739 406 G-AFApLAIGMDTLtEDEQIKLDVMIAHGGLFKTPVIAqQVLANALNTPISVMETAgEGGSWGMAVLAAYMA 476
Cdd:cd07779 336 GiAFE-LRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWN-QIIADVFGRPVERPETS-EATALGAAILAAVGA 403
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
17-474 |
7.12e-20 |
|
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: 92.27 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGS--YQWENQfENEVWTYNLDQVWEGIRDSYKQLSAEVESKyhtnltKIDNVGISA 94
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILASASreTPLIHP-GPGWAELDPEELWEAVKEAIREAAAQAGPD------PIAAISVSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 95 MMHGYLAFSKEDELLVPFRTWRNNITGPATDQLTELFNFNVPQRWC------------IAHLYQailNQEEHVDKISFLT 162
Cdd:cd07773 76 QGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITglppspmyslakLLWLRE---HEPEIFAKAAKWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 163 TLSGYVHWQLTGEKVLGIGDAS--GAFpiDETKGDYDETFMkKFSQLDevqqyswetREIFPKVLKAGEDAGRLSEAGAK 240
Cdd:cd07773 153 SVADYIAYRLTGEPVTDYSLASrtMLF--DIRKRTWSEELL-EAAGID---------ASLLPELVPSGTVIGTVTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 241 LLD-----PL---GHlqsgsrmappegDAGTGMIATNSIRKRTGNISVGTS-AFAMVVLDKPLQKVHREIDIVTTPAGTN 311
Cdd:cd07773 221 ELGlpagtPVvvgGH------------DHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 312 VAMVHADNCSSdidawAQIFQQFAERLGIqlsPEQLYETLFLDASKADPDAGGLFNYSYLSGEVITEVD-DGRPMFVrTI 390
Cdd:cd07773 289 GYYYLAGSLPG-----GALLEWFRDLFGG---DESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDpDARGAFL-GL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 391 NSNFNLPNFIQTQLYG-AFApLAIGMDTLtEDEQIKLDVMIAHGGLFKTPVIaQQVLANALNTPISVMETAgEGGSWGMA 469
Cdd:cd07773 360 TLGTTRADLLRAILEGlAFE-LRLNLEAL-EKAGIPIDEIRAVGGGARSPLW-LQLKADILGRPIEVPEVP-EATALGAA 435
|
....*
gi 2532437739 470 VLAAY 474
Cdd:cd07773 436 LLAGV 440
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
17-242 |
4.75e-15 |
|
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: 75.07 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWENQFENEVWT-YNLDQVWEgirdSYKQLSAEVESKYHTNLTKIDNVGISAM 95
Cdd:pfam00370 3 LGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAeQDPDEIWQ----AVAQCIAKTLSQLGISLKQIKGIGISNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 96 MHGYLAFSKEDELLVPFRTWRNNITGPATDQLTELFN---------------FNVPQ-RWciahlyqaILNQEEHV-DKI 158
Cdd:pfam00370 79 GHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNnqklyeitglpiwpgFTLSKlRW--------IKENEPEVfEKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 159 SFLTTLSGYVHWQLTGEKVLGIGDASGAFPIDETKGDYDetfmkkfsqlDEVQQYSWETREIFPKVLKAGEDAGRLSEAG 238
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWD----------PELLAALGIPRDHLPPLVESSEIYGELNPEL 220
|
....
gi 2532437739 239 AKLL 242
Cdd:pfam00370 221 AAMW 224
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
17-473 |
7.08e-15 |
|
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: 76.88 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWE-NQFENE--VWTYNLDQVWEGIrdsyKQLSAEVESKYHTNLTKIDNVGIS 93
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWEyYTDDDYpdAKEFDPEELWEKI----CEAIREALKKAGISPEDISAVSST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 94 AMMHGYLAFSKEDELLvpfrtwrnnITGPATDQLTELFNFNVPQ-----------RW-----CIAHLYQAILNQEEHVDK 157
Cdd:cd07798 79 SQREGIVFLDKDGREL---------YAGPNIDARGVEEAAEIDDefgeeiytttgHWptelfPAARLLWFKENRPEIFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 158 ISFLTTLSGYVHWQLTGEKVLGIGDASGAFPIDETKGDYDETFMKKFsQLDEvqqyswetrEIFPKVLKAGEDAGRLSEA 237
Cdd:cd07798 150 IATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEAL-GLPP---------EILPEIVPSGTVLGTVSEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 238 GAKLLDplghLQSGSRMAPPEGDAGTGMIATNSIrkRTGNISV--GTSAFAMVVLDKPLQKVHREIDIvttpagtnvamv 315
Cdd:cd07798 220 AARELG----LPEGTPVVVGGADTQCALLGSGAI--EPGDIGIvaGTTTPVQMVTDEPIIDPERRLWT------------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 316 hadNCSSDIDAWA---------QIFQQFAERLgiQLSPEQLYETLFLDASKADPDAGGLfnYSYLSGEViteVDDGRPMF 386
Cdd:cd07798 282 ---GCHLVPGKWVlesnagvtgLNYQWLKELL--YGDPEDSYEVLEEEASEIPPGANGV--LAFLGPQI---FDARLSGL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 387 VR--------TINSNFNLPNFIQTQLYG-AFAPLAIgMDTLTEDEQIKLDVMIAHGGLFKTPVIAqQVLANALNTPISVM 457
Cdd:cd07798 352 KNggflfptpLSASELTRGDFARAILENiAFAIRAN-LEQLEEVSGREIPYIILCGGGSRSALLC-QILADVLGKPVLVP 429
|
490
....*....|....*.
gi 2532437739 458 ETAgEGGSWGMAVLAA 473
Cdd:cd07798 430 EGR-EASALGAAICAA 444
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-472 |
1.35e-14 |
|
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: 75.72 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 15 VSLAIELGSTRIKAVLITSD-FKTIASGSYQ---WENQFENEVWTYNLDQVWEGIRDSYKQLSAEVESkyhtnltKIDNV 90
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLEsGRILESVSRPtpaPISSDDPGRSEQDPEKILEAVRNLIDELPREYLS-------DVTGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 91 GISAMMHGYLAFSKEDELLVPFRTWRNNITGPATDQLTELFNFNVPQRWC--------IAHLYqAILNQEEHVDKISFLT 162
Cdd:cd07777 74 GITGQMHGIVLWDEDGNPVSPLITWQDQRCSEEFLGGLSTYGEELLPKSGmrlkpgygLATLF-WLLRNGPLPSKADRAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 163 TLSGYVHWQLTGEKVLGIgDASGAFPI---DETKGDYDETFMKK--FSQLdevqqyswetreIFPKVLKAGEDAGRLSEA 237
Cdd:cd07777 153 TIGDYIVARLTGLPKPVM-HPTNAASWglfDLETGTWNKDLLEAlgLPVI------------LLPEIVPSGEIVGTLSSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 238 GAKlldplghlqsGSRMAPPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPLQkvHREIDIVTTPAGTNVAMVHA 317
Cdd:cd07777 220 LPK----------GIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFEL--SGSVEIRPFFDGRYLLVAAS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 318 DNCSSDIDAWAQIFQQFAERLGIQLSPEQLYEtlFLDASKADPDAGGLFNYSYLSGEVITEvdDGRPMFVRTINSNFNLP 397
Cdd:cd07777 288 LPGGRALAVLVDFLREWLRELGGSLSDDEIWE--KLDELAESEESSDLSVDPTFFGERHDP--EGRGSITNIGESNFTLG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 398 NFIQ-------TQLYGAFAPLAIGmdtltedeQIKLDVMIAHGGLF-KTPVIaQQVLANALNTPIsVMETAGEGGSWGMA 469
Cdd:cd07777 364 NLFRalcrgiaENLHEMLPRLDLD--------LSGIERIVGSGGALrKNPVL-RRIIEKRFGLPV-VLSEGSEEAAVGAA 433
|
...
gi 2532437739 470 VLA 472
Cdd:cd07777 434 LLA 436
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
17-476 |
2.25e-13 |
|
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: 72.20 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYqwenqfENEV-------WTYNLDQVWEG----IRDSYKQLSAEVEskyhtnlt 85
Cdd:cd07802 3 LGIDNGTTNVKAVLFDLDGREIAVASR------PTPVisprpgwAERDMDELWQAtaeaIRELLEKSGVDPS-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 86 KIDNVGISAMMHG-YLAfskeDELLVPFRtwrNNITgpATDQ----LTELFNFNVPQRWCIAHLYQ--------AIL--- 149
Cdd:cd07802 69 DIAGVGVTGHGNGlYLV----DKDGKPVR---NAIL--SNDSraadIVDRWEEDGTLEKVYPLTGQplwpgqpvALLrwl 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 150 --NQEEHVDKISFLTTLSGYVHWQLTGEKVLGIGDASGAFpIDETKGDYDETFMKKFSqLDEVqqyswetREIFPKVLKA 227
Cdd:cd07802 140 keNEPERYDRIRTVLFCKDWIRYRLTGEISTDYTDAGSSL-LDLDTGEYDDELLDLLG-IEEL-------KDKLPPLVPS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 228 GEDAGRLSEAGAKLLDplghLQSGSRMAPPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKP-------LQKVHRE 300
Cdd:cd07802 211 TEIAGRVTAEAAALTG----LPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPvvpdsvgSNSLHAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 301 ID----IVTTPAGTnvamvhadncsSDIDaWAQifQQFAERLGIQLSPeqLYETLFLDASKADPDAGGLFNYSYLSGEvi 376
Cdd:cd07802 287 PGlyliVEASPTSA-----------SNLD-WFL--DTLLGEEKEAGGS--DYDELDELIAAVPPGSSGVIFLPYLYGS-- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 377 TEVDDGRPMFVRtINSNFNLPNFIQTQLYG-AFApLAIGMDTLTEDEQIKlDVMIAhGGLFKTPVIAqQVLANALNTPIS 455
Cdd:cd07802 349 GANPNARGGFFG-LTAWHTRAHLLRAVYEGiAFS-HRDHLERLLVARKPE-TIRLT-GGGARSPVWA-QIFADVLGLPVE 423
|
490 500
....*....|....*....|.
gi 2532437739 456 VMETAgEGGSWGMAVLAAYMA 476
Cdd:cd07802 424 VPDGE-ELGALGAAICAAVAA 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
17-474 |
3.41e-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: 71.79 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGS--YQ-------WENQfENEVWtynldqvWEGirdsYKQLSAEVESKYHTNLTKI 87
Cdd:cd07804 3 LGIDIGTTGTKGVLVDEDGKVLASASieHDlltpkpgWAEH-DPEVW-------WGA----VCEIIRELLAKAGISPKEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 88 DNVGISAMMHGYLAFSKEDELLVPFRTWRNNITGPATDQLTELFNFNVPQRWCIAHL-YQAIL--------NQEEHVDKI 158
Cdd:cd07804 71 AAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLdSQSVGpkllwikrNEPEVFKKT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 159 SFLTTLSGYVHWQLTGEKVLGIGDASGAFPI-DETKGDYDETFMKKFSqLDevqqyswetREIFPKVLKAGEDAGRLSEA 237
Cdd:cd07804 151 RKFLGAYDYIVYKLTGEYVIDYSSAGNEGGLfDIRKRTWDEELLEALG-ID---------PDLLPELVPSTEIVGEVTKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 238 GAKLLDplghLQSGSRMAPPEGDAGTGMIATNSIrkRTGN--ISVGTSAFAMVVLDKPLQ------KVHREIDIVTTPAG 309
Cdd:cd07804 221 AAEETG----LAEGTPVVAGTVDAAASALSAGVV--EPGDllLMLGTAGDIGVVTDKLPTdprlwlDYHDIPGTYVLNGG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 310 TNvamvhadNCSSDI----DAWAQIFQQFAERLGIqlSPeqlYETLFLDASKADPDAGGLFNYSYLSGEViTEVDD--GR 383
Cdd:cd07804 295 MA-------TSGSLLrwfrDEFAGEEVEAEKSGGD--SA---YDLLDEEAEKIPPGSDGLIVLPYFMGER-TPIWDpdAR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 384 PMFvrtinsnFNL-PNFIQTQLYGAF---APLAI--GMDTLTEDEQIKLDVMIAHGGLfKTPVIAqQVLANALNTPISVM 457
Cdd:cd07804 362 GVI-------FGLtLSHTRAHLYRALlegVAYGLrhHLEVIREAGLPIKRLVAVGGGA-KSPLWR-QIVADVTGVPQEYV 432
|
490
....*....|....*..
gi 2532437739 458 ETAgEGGSWGMAVLAAY 474
Cdd:cd07804 433 KDT-VGASLGDAFLAGV 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
17-473 |
1.72e-10 |
|
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: 63.03 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIASGSYQWENQFENEVW-TYNLDQVWEGIRDSYKQLSAEVESKYHtnltKIDNVGISAM 95
Cdd:cd24121 3 IGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWaEQDMNETWQAVVATIREVVAKLDVLPD----RVAAIGVTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 96 MHG-YLAfskeDELLVPFR---TWRNnitGPATDQLTELFN-------FNVPQRWCIAHLYQAIL-----NQEEHVDKIS 159
Cdd:cd24121 79 GDGtWLV----DEDGRPVRdaiLWLD---GRAADIVERWQAdgiaeavFEITGTGLFPGSQAAQLawlkeNEPERLERAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 160 FLTTLSGYVHWQLTGEKVLGIGDASGAFpIDETKGDYDETFMKKFsqldEVQQYswetREIFPKVLKAGEDAGRLSEAGA 239
Cdd:cd24121 152 TALHCKDWLFYKLTGEIATDPSDASLTF-LDFRTRQYDDEVLDLL----GLEEL----RHLLPPIRPGTEVIGPLTPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 240 KLLDplghLQSGSR--MAPPegDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPLQKVHRE-IDIVTTPAGTNVAMVH 316
Cdd:cd24121 223 AATG----LPAGTPvvLGPF--DVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVgYTICLGVPGRWLRAMA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 317 ADNCSSDIDAWAQIFQQfAERLGIQLSPEQLYETLFLDASKADPDAGGLFNYSYLS--GEVITEVD-DGRPMFVrTINSN 393
Cdd:cd24121 297 NMAGTPNLDWFLRELGE-VLKEGAEPAGSDLFQDLEELAASSPPGAEGVLYHPYLSpaGERAPFVNpNARAQFT-GLSLE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 394 FNLPNFIQTQLYG-AFAPL----AIGMDTltedEQIKLDvmiahGGLFKTPVIAqQVLANALNTPISVMEtAGEGGSWGM 468
Cdd:cd24121 375 HTRADLLRAVYEGvALAMRdcyeHMGEDP----GELRLS-----GGGARSDTWC-QILADALGVPVRVPA-GEEFGARGA 443
|
....*
gi 2532437739 469 AVLAA 473
Cdd:cd24121 444 AMNAA 448
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
15-523 |
3.38e-10 |
|
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: 62.55 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 15 VSLAIELGSTRIKAVLI-TSDFKTIASGSYQWENQFENEVWTYNL---DQVWEGIRDSYKQLSAEveskyhTNLTKIDNV 90
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVdLADGEELASAVVPYPTGYIPPRPGWAEqnpADYWEALEEAVRGALAE------AGVDPEDVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 91 GISA------MmhgyLAFSKEDELLVPFRTWR-----------NNITGPATDQLTELFNFNVPQRWCIAHLYQaILNQEE 153
Cdd:cd07781 75 GIGVdttsstV----VPVDEDGNPLAPAILWMdhraqeeaaeiNETAHPALEYYLAYYGGVYSSEWMWPKALW-LKRNAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 154 HV-DKISFLTTLSGYVHWQLTGEKVLGIGDASGAFPIDETKGDYDETFMKKFSQLDEVQQYSWETReifpkVLKAGEDAG 232
Cdd:cd07781 150 EVyDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLREKLPGE-----VVPVGEPAG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 233 RLSEAGAKLLDplghLQSGSRMAPPEGDAGTGMIATNSIrkRTGNISV--GTSAFAMVVLDKPLqkvhrEID----IVTT 306
Cdd:cd07781 225 TLTAEAAERLG----LPAGIPVAQGGIDAHMGAIGAGVV--EPGTLALimGTSTCHLMVSPKPV-----DIPgicgPVPD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 307 PAGTNVAMVHADNCSS-DIDAWaqifqqFAERLGIQLSPEQ--LYETLFLDASKADPDAGGLFNYSYLSGevitevddgr 383
Cdd:cd07781 294 AVVPGLYGLEAGQSAVgDIFAW------FVRLFVPPAEERGdsIYALLSEEAAKLPPGESGLVALDWFNG---------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 384 pmfVRTINSNFNLPNFI--QT------QLYGA------FAPLAIgMDTLtEDEQIKLDVMIAHGGL-FKTPVIaQQVLAN 448
Cdd:cd07781 358 ---NRTPLVDPRLRGAIvgLTlgttpaHIYRAlleataFGTRAI-IERF-EEAGVPVNRVVACGGIaEKNPLW-MQIYAD 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2532437739 449 ALNTPISVMETAgEGGSWGMAVLAAYMAKsLEMSLEDflDQEVFAAPETmTLNPEPAGVQGYADYLAQYQAALPA 523
Cdd:cd07781 432 VLGRPIKVPKSD-QAPALGAAILAAVAAG-VYADIEE--AADAMVRVDR-VYEPDPENHAVYEELYALYKELYDA 501
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
17-294 |
2.36e-07 |
|
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: 53.30 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 17 LAIELGSTRIKAVLITSDFKTIA-SGSYQWENQF--ENEVWTYNLDQVWEGIRDSYKqlsaevesKYHTNLTKIDNVGIS 93
Cdd:cd07771 3 LAVDLGASSGRVILGSLDGGKLElEEIHRFPNRPveINGHLYWDIDRLFDEIKEGLK--------KAAEQGGDIDSIGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 94 AmmHG--YLAFSKEDELLVPFRTWRNNITGPATDQLT------ELFNF--NVPQRWC-IAHLYQAILNQEEHVDKISFLT 162
Cdd:cd07771 75 T--WGvdFGLLDKNGELLGNPVHYRDPRTEGMMEELFekiskeELYERtgIQFQPINtLYQLYALKKEGPELLERADKLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 163 TLSGYVHWQLTGEKVLGIGDASgafpideT-------KGDYDETFMKKFSqLDevqqyswetREIFPKVLKAGEDAGRLS 235
Cdd:cd07771 153 MLPDLLNYLLTGEKVAEYTIAS-------TtqlldprTKDWSEELLEKLG-LP---------RDLFPPIVPPGTVLGTLK 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2532437739 236 EAGAKLLDpLGHLQSgsrMAPPEGDAGTGMIATNSIRKRTGNISVGTSAFAMVVLDKPL 294
Cdd:cd07771 216 PEVAEELG-LKGIPV---IAVASHDTASAVAAVPAEDEDAAFISSGTWSLIGVELDEPV 270
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
388-519 |
1.79e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 50.61 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 388 RTINSNFNLPNFI-----QT---QLYGAF-APLAIG----MDTLtEDEQIKLDVMIAHGGLF-KTPVIaQQVLANALNTP 453
Cdd:PRK04123 389 RTPLADQRLKGVItgltlGTdapDIYRALiEATAFGtraiMECF-EDQGVPVEEVIAAGGIArKNPVL-MQIYADVLNRP 466
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2532437739 454 ISVMeTAGEGGSWGMAVLAAYMAKSLEmsleDFLD-QEVFAAPETMTLNPEPAGVQGYADYLAQYQA 519
Cdd:PRK04123 467 IQVV-ASDQCPALGAAIFAAVAAGAYP----DIPEaQQAMASPVEKTYQPDPENVARYEQLYQEYKQ 528
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
14-242 |
2.21e-05 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 46.95 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 14 SVSLAIELGSTRIKAVLITSDFKTIASGSYQWENQ--FENEVW-TYNLDQVWEGIRDSYKQLSAEveskyhtnLTKIDNV 90
Cdd:PRK10331 2 DVILVLDCGATNVRAIAVDRQGKIVARASTPNASDiaAENSDWhQWSLDAILQRFADCCRQINSE--------LTECHIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 91 GISAMMHGY--LAFSKEDELLVPFRTWRNNITGPATDQL------TEL--------FNFNVpqrwciahLYQAILNQEEH 154
Cdd:PRK10331 74 GITVTTFGVdgALVDKQGNLLYPIISWKCPRTAAVMENIeryisaQQLqqisgvgaFSFNT--------LYKLVWLKENH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532437739 155 ------VDKISFLTTLSGYvhwQLTGEkvlgigdasgaFPIDETkgdydetfMKKFSQLDEVQQYSWE---------TRE 219
Cdd:PRK10331 146 pqlleqAHAWLFISSLINH---RLTGE-----------FTTDIT--------MAGTSQMLDIQQRDFSpeilqatglSRR 203
|
250 260
....*....|....*....|...
gi 2532437739 220 IFPKVLKAGEDAGRLSEAGAKLL 242
Cdd:PRK10331 204 LFPRLVEAGEQIGTLQPSAAALL 226
|
|
| |
