|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
12-473 |
6.68e-170 |
|
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: 487.83 E-value: 6.68e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 12 TALGVEFGSTRIKSVLIDANNFEVLASGSFEWENQLVN-GIWTYSLDDVWKGLQASYTDLKAEVKDKydfkLSKIGQIGI 90
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAETGRVVASGSAPHENILIDpGWAEQDPEDWWDALQAAFAQLLKDAGAE----LRDVAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 91 SAMMHGYLVFDQADKQLAEFRTWRNAITEQAAGELSKLFNF--------NIPQRWCIAHLYQAILNQEKSVSQIDFMTTL 162
Cdd:cd07809 77 SGQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGkkcllvglNIPARFTASKLLWLKENEPEHYARIAKILLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 163 AGYVHWRLTGKKVTGIGDASGIFPIDSNSKDYDQKKLDQFSDldgvekqPWDIKRILPKVLLAGQNAGQLTKEGSLlidp 242
Cdd:cd07809 157 HDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDP-------SRDLRDLLPEVLPAGEVAGRLTPEGAE---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 243 SGDLQDGSVFCPPEGDAGTGMVATNSVNQRSGNVSAGTSIFSMVVLEHPLKKVYPEVDvvsTPTGDDVAMIHANNATSDI 322
Cdd:cd07809 226 ELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVA---TFCDSTGGMLPLINTTNCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 323 NAWMHLFEEFLvlagkkldkeTVFRSLFFSALTDADADAGNLLTYGYYSGENITGLKEGRPLLVRSPESKFTIANLMRAQ 402
Cdd:cd07809 303 TAWTELFRELL----------GVSYEELDELAAQAPPGAGGLLLLPFLNGERTPNLPHGRASLVGLTLSNFTRANLARAA 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696225539 403 ILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTPrVAQQILADVLETPISVTENaAEGGAWGIAILAAYV 473
Cdd:cd07809 373 LEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSP-VWRQILADVFGVPVVVPET-GEGGALGAALQAAWG 441
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
14-517 |
2.88e-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: 319.09 E-value: 2.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANnFEVLASGSFEWENQLV-NGIWTYSLDDVWKGLQASYtdlkAEVKDKYDFKLSKIGQIGISA 92
Cdd:COG1070 4 LGIDIGTTSVKAVLFDAD-GEVVASASAEYPLSSPhPGWAEQDPEDWWEAVVEAI----RELLAKAGVDPEEIAAIGVSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHGYLVFDQADKQLAEFRTWRNAITEQAAGELSKLFN----FNI---PQR--WCIAHLYQaILNQEKSV-SQIDFMTTL 162
Cdd:COG1070 79 QMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGeealYEItgnPLHpgFTAPKLLW-LKENEPEIfARIAKVLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 163 AGYVHWRLTGKKVTGIGDASGIFPIDSNSKDYDQKKLDQFsdldGVEkqpwdiKRILPKVLLAGQNAGQLTKEGSLLidp 242
Cdd:COG1070 158 KDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEAL----GID------RELLPELVPPGEVAGTLTAEAAAE--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 243 SGdLQDGSVFCPPEGDAGTGMVATNSVNQRSGNVSAGTSIFSMVVLEHPLKKVYPEVDVVSTPTGDD-VAMIHANNATSD 321
Cdd:COG1070 225 TG-LPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRwLPMGATNNGGSA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 322 INAWMHLFEEFLVLAGKKLDKEtvfrslffsaLTDADADAGNLLTYGYYSGENITGL-KEGRPLLVRSPeSKFTIANLMR 400
Cdd:COG1070 304 LRWFRDLFADGELDDYEELNAL----------AAEVPPGADGLLFLPYLSGERTPHWdPNARGAFFGLT-LSHTRAHLAR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 401 AQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTPrVAQQILADVLETPISVTEnAAEGGAWGIAILAAYVDKASElS 480
Cdd:COG1070 373 AVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSP-LWRQILADVLGRPVEVPE-AEEGGALGAALLAAVGLGLYD-D 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 696225539 481 LAEYLKSKVFSASstiTIEPNYDDLPGTHKFMDRYQK 517
Cdd:COG1070 450 LEEAAAAMVRVGE---TIEPDPENVAAYDELYERYRE 483
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
274-472 |
4.47e-44 |
|
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: 154.40 E-value: 4.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 274 GNVSAGTSIFSMVVLEHPLkkvyPEVDVVSTPTGDD-----VAMIHANNATSDINAWMHLFEEFLvlagKKLDKETVFRS 348
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPV----LSVHGVWGPYTNEmlpgyWGLEGGQSAAGSLLAWLLQFHGLR----EELRDAGNVES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 349 LFFSALTDADADAGNLLTYGYYSGENITGLKEGRPLLVRSPESKFTIANLMRAQILSVFGALKIGMDILKKEE-VKIDRL 427
Cdd:pfam02782 73 LAELAALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEgHPIDTI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 696225539 428 TGHGGLFKtPRVAQQILADVLETPISVTENaAEGGAWGIAILAAY 472
Cdd:pfam02782 153 HVSGGGSR-NPLLLQLLADALGLPVVVPGP-DEATALGAALLAAV 195
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
14-470 |
9.51e-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: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANnFEVLASGSFEWENQLVNGIWT-YSLDDVWKGLQASytdLKaEVKDKYDFKLSKIGQIGISA 92
Cdd:cd00366 3 LGIDIGTTSVKAALFDED-GNLVASASREYPLIYPQPGWAeQDPEDWWQAVVEA---IR-EVLAKAGIDPSDIAAIGISG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHGYLVFDqadkqlAEFRTWRNAITeqaagelsklfnfNIPQRWCIAHLyqailnqeksvsqidfmttlAGYVHWRLTG 172
Cdd:cd00366 78 QMPGVVLVD------ADGNPLRPAII-------------WLDRRAKFLQP--------------------NDYIVFRLTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 173 KKVTGIGDASGIFPIDSNSKDYDQKKLDQFsDLDgvekqpwdiKRILPKVLLAGQNAGQLTKEGSLLidpSGDlqdgsvf 252
Cdd:cd00366 119 EFAIDYSNASGTGLYDIKTGDWSEELLDAL-GIP---------REKLPPIVESGEVVGRVTPEAAEE---TGL------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 253 cpPEG--------DAGTGMVATNSVNQRSGNVSAGTSIFSMVVLEHPlkkVYPEVDVVSTPTGDDVAMIHAN--NATSDI 322
Cdd:cd00366 179 --PAGtpvvagggDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEP---VPPDPRLLNRCHVVPGLWLLEGaiNTGGAS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 323 NAWMhlFEEFLvlagkKLDKETVFRSLFFSALTDADADAGNLLTYGYYSGEnitglkegrpllvRSPE------------ 390
Cdd:cd00366 254 LRWF--RDEFG-----EEEDSDAEYEGLDELAAEVPPGSDGLIFLPYLSGE-------------RSPIwdpaargvffgl 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 391 -SKFTIANLMRAQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTpRVAQQILADVLETPISVTENaAEGGAWGIAIL 469
Cdd:cd00366 314 tLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKS-RLWNQIKADVLGVPVVVPEV-AEGAALGAAIL 391
|
.
gi 696225539 470 A 470
Cdd:cd00366 392 A 392
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
14-471 |
1.98e-21 |
|
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: 96.85 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANNFEVL-ASGSFEWENqLVNGIWTYSLDDVWkglQASYTDLKaEVKDKYDFKLSKIGQIGISA 92
Cdd:cd07802 3 LGIDNGTTNVKAVLFDLDGREIAvASRPTPVIS-PRPGWAERDMDELW---QATAEAIR-ELLEKSGVDPSDIAGVGVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHG-YLVfDQADKQLaefrtwRNAITEQ---AAGELSKLFNfNIPQRWCIAHLYQ--------AIL-----NQEKSVSQ 155
Cdd:cd07802 78 HGNGlYLV-DKDGKPV------RNAILSNdsrAADIVDRWEE-DGTLEKVYPLTGQplwpgqpvALLrwlkeNEPERYDR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 156 IDFMTTLAGYVHWRLTGKKVTGIGDAsGIFPIDSNSKDYDQKKLDQFsdldGVEkqpwDIKRILPKVLLAGQNAGQLTKE 235
Cdd:cd07802 150 IRTVLFCKDWIRYRLTGEISTDYTDA-GSSLLDLDTGEYDDELLDLL----GIE----ELKDKLPPLVPSTEIAGRVTAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 236 GSLLIDpsgdLqdgsvfcpPEG--------DAGTGMVATNSVNQRSGNVSAGTSIFSMVVLEHPLkkVYPEVDVVSTPTG 307
Cdd:cd07802 221 AAALTG----L--------PEGtpvaagafDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPV--VPDSVGSNSLHAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 308 DDVAMIHANNATSDINawmhlFEEFL-VLAGKKLDKETVFRSLFFSALTDADADAGNLLTYGYYSGENI--------TGL 378
Cdd:cd07802 287 PGLYLIVEASPTSASN-----LDWFLdTLLGEEKEAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGAnpnarggfFGL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 379 KegrpllvrspeSKFTIANLMRAqilsVF-G---ALKIGMD-ILKKEEVKIDRLTGhgGLFKTPRVAQqILADVLETPIS 453
Cdd:cd07802 362 T-----------AWHTRAHLLRA----VYeGiafSHRDHLErLLVARKPETIRLTG--GGARSPVWAQ-IFADVLGLPVE 423
|
490
....*....|....*...
gi 696225539 454 VTEnAAEGGAWGIAILAA 471
Cdd:cd07802 424 VPD-GEELGALGAAICAA 440
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
13-470 |
8.62e-19 |
|
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: 88.82 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 13 ALGVEFGSTRIKSVLIDANNFEVLASGSFEWENQLVNGIWTYSLDDVWKGLQASyTDLKAEVKDKYdfkLSKIGQIGISA 92
Cdd:cd07777 2 VLGIDIGTTSIKAALLDLESGRILESVSRPTPAPISSDDPGRSEQDPEKILEAV-RNLIDELPREY---LSDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHGYLVFDQADKQLAEFRTWRNA-ITEQAAGELSklFNFNIPQRWC---------IAHLYqAILNQEKSVSQIDFMTTL 162
Cdd:cd07777 78 QMHGIVLWDEDGNPVSPLITWQDQrCSEEFLGGLS--TYGEELLPKSgmrlkpgygLATLF-WLLRNGPLPSKADRAGTI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 163 AGYVHWRLTGKK--VTGIGDA--SGIFpiDSNSKDYDQKKLdQFSDLDGVekqpwdikrILPKVLLAGQNAGQLTKEGSL 238
Cdd:cd07777 155 GDYIVARLTGLPkpVMHPTNAasWGLF--DLETGTWNKDLL-EALGLPVI---------LLPEIVPSGEIVGTLSSALPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 239 LID---PSGDLQdGSVFcppegdaGTGMVATNSVnqrsgNVSAGTS-IFSMVVlehPLKKVYPEVDVVstPTGDD----- 309
Cdd:cd07777 223 GIPvyvALGDNQ-ASVL-------GSGLNEENDA-----VLNIGTGaQLSFLT---PKFELSGSVEIR--PFFDGryllv 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 310 VAMIHANNAtsdINAWMHLFEEFLVLAGKKLDKETVFRSLFFSALTDADADagnLLTYGYYSGENITGLKEGRPLLVRsp 389
Cdd:cd07777 285 AASLPGGRA---LAVLVDFLREWLRELGGSLSDDEIWEKLDELAESEESSD---LSVDPTFFGERHDPEGRGSITNIG-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 390 ESKFTIANLMRAQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTPRVAQQILADVLETPISVTENAAEgGAWGIAIL 469
Cdd:cd07777 357 ESNFTLGNLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGALRKNPVLRRIIEKRFGLPVVLSEGSEE-AAVGAALL 435
|
.
gi 696225539 470 A 470
Cdd:cd07777 436 A 436
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
14-472 |
2.93e-17 |
|
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: 84.11 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANNfEVLASGSFEWENQLVNGIWT-YSLDDVWKGLQASYTDLKAEVKDKydfkLSKIGQIGISA 92
Cdd:cd07779 3 LGIDVGTTSTRAIIFDLDG-NIVASGYREYPPYYPEPGWVeQDPDDWWDALCEALKEAVAKAGVD----PEDIAAIGLTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHGYLVFDQADKQLaefrtwRNAITeqaagelsklfnfnipqrWciahlyqailnQEKSVSQIdfmTTLAGYVHWRLTG 172
Cdd:cd07779 78 QRSTFVPVDEDGRPL------RPAIS------------------W-----------QDKRTAKF---LTVQDYLLYRLTG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 173 KKVTGIGDASGIFPIDSNSKDYDQKKLDQFsdldGVEKQpwdikrILPKVLLAGQNAGQLTKEGSLLIdpsgDLQDGSVF 252
Cdd:cd07779 120 EFVTDTTSASRTGLPDIRTRDWSDDLLDAF----GIDRD------KLPELVPPGTVIGTLTKEAAEET----GLPEGTPV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 253 CPPEGDAGTGMVATNSVNQRSGNVSAGTSIFSMVVLEHPLKKvyPEVDVVSTPTGDD---VAMIHANNATSDINaWMHlf 329
Cdd:cd07779 186 VAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVED--PERRIPCNPSAVPgkwVLEGSINTGGSAVR-WFR-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 330 EEFLVLAGKKLDKETVFRSLFFSALTDADADAGNLLTYGYYSGenitglkEGRPllVRSPESKFTIANL---------MR 400
Cdd:cd07779 261 DEFGQDEVAEKELGVSPYELLNEEAAKSPPGSDGLLFLPYLAG-------AGTP--YWNPEARGAFIGLtlshtrahlAR 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696225539 401 AQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTPrVAQQILADVLETPISVTENaAEGGAWGIAILAAY 472
Cdd:cd07779 332 AILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSD-LWNQIIADVFGRPVERPET-SEATALGAAILAAV 401
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
14-517 |
3.46e-17 |
|
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: 84.14 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANnFEVLASGSFEWE-NQLVNGIWTYSLDDVWKGLQASYTDLKAEVKDkydfklSKIGQIGISA 92
Cdd:cd07770 3 LGIDIGTTSTKAVLFDED-GRVVASSSAEYPlIRPEPGWAEQDPEEILEAVLEALKEVLAKLGG------GEVDAIGFSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHGYLVFDQADKQLAEFRTW---RNAitEQAAGELSKLFNFNIPQR-----------WCIAHLYQailNQEKSVSQIDF 158
Cdd:cd07770 76 AMHSLLGVDEDGEPLTPVITWadtRAA--EEAERLRKEGDGSELYRRtgcpihpmyplAKLLWLKE---ERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 159 MTTLAGYVHWRLTGKKVTGIGDAS--GIFpiDSNSKDYDQKKLDqFSDLDgvEKQpwdikriLPKVLLAGQNAGQLTKEG 236
Cdd:cd07770 151 FVSIKEYLLYRLTGELVTDYSTASgtGLL--NIHTLDWDEEALE-LLGID--EEQ-------LPELVDPTEVLPGLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 237 SLLIdpsgDLQDGSVFCPPEGDAGTGMVATNSVNQRSGNVSAGTSifSM--VVLEHPLKKVYPE-----VD----VVSTP 305
Cdd:cd07770 219 AERL----GLLAGTPVVLGASDGALANLGSGALDPGRAALTVGTS--GAirVVSDRPVLDPPGRlwcyrLDenrwLVGGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 306 TgddvamihaNNATSDInAWMHlfeeflvlagKKLDKETVFRSLFFSALTDADADAGNLLTYGYYSGEnitglkegrpll 385
Cdd:cd07770 293 I---------NNGGNVL-DWLR----------DTLLLSGDDYEELDKLAEAVPPGSHGLIFLPYLAGE------------ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 386 vRSP----ESKFTIANL---------MRAQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTPrVAQQILADVLETPI 452
Cdd:cd07770 341 -RAPgwnpDARGAFFGLtlnhtradiLRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSP-LWLQILADVLGRPV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696225539 453 SVTENaAEGGAWGIAILAAYVdkaseLSLAEYLKSKvFSASSTITIEPNyddlPGTHKfmdRYQK 517
Cdd:cd07770 419 LVPEE-EEASALGAALLALEA-----LGLISSLEAD-ELVKIGKVVEPD----PENHA---IYAE 469
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
14-521 |
3.01e-16 |
|
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: 81.43 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANNfEVLASGSFEWEnqlvngiwTYSL---------DDVWKGLQasytDLKAEVKDKYDFKLSK 84
Cdd:cd07808 3 LGIDLGTSSVKAVLVDEDG-RVLASASAEYP--------TSSPkpgwaeqdpEDWWQATK----EALRELLAKAGISPSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 85 IGQIGISAMMHGYLVFDQADKQLaefrtwRNAI------TEQAAGELSKLFNFNIPQR--------WCIAHLYQaILNQE 150
Cdd:cd07808 70 IAAIGLTGQMHGLVLLDKNGRPL------RPAIlwndqrSAAECEELEARLGDEILIItgnpplpgFTLPKLLW-LKENE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 151 KSV-SQID-FMttLA-GYVHWRLTGKKVTGIGDASGIFPIDSNSKDYDQKKLDQFsDLDgvekqpwdiKRILPKVLLAGQ 227
Cdd:cd07808 143 PEIfARIRkIL--LPkDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEAL-GLD---------PSILPPIVESTE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 228 NAGQLTKEGSLLIDpsgdLQDG-SVFCPpEGDAGTGMVATNSVNQRSGNVSAGTSIFSMVVLEHPLKKVYPEVDVVSTPT 306
Cdd:cd07808 211 IVGTLTPEAAEELG----LPEGtPVVAG-AGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 307 GDD-VAMIHANNATSDINAWMHLFeeflvlAGKKLDKETVFRSLFfsaltDADADAGNLLTYGYYSGEnitglkegrpll 385
Cdd:cd07808 286 PGKwYAMGVTLSAGLSLRWLRDLF------GPDRESFDELDAEAA-----KVPPGSEGLLFLPYLSGE------------ 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 386 vRSP-------------ESKFTIANLMRAQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTPrVAQQILADVLETPI 452
Cdd:cd07808 343 -RTPywdpnargsffglSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSP-LWRQILADVLGVPV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 696225539 453 SVTENaAEGGAWGIAILAAYVDKASElSLAEYLKSKVFSASstiTIEPNyddlPGTHKfmdRYQKGLDI 521
Cdd:cd07808 421 VVPAE-EEGSAYGAALLAAVGAGVFD-DLEEAAAACIKIEK---TIEPD----PERHE---AYDELYAR 477
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
14-472 |
3.09e-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: 81.09 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANnFEVLASGSFEweNQLV---NGIWTYSLDDVWKGLQASYTDLKAEVKDkydfklSKIGQIGI 90
Cdd:cd07773 3 LGIDIGTTNVKAVLFDED-GRILASASRE--TPLIhpgPGWAELDPEELWEAVKEAIREAAAQAGP------DPIAAISV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 91 SAM-MHGYLVfDQADKQLAEFRTWRNAITEQAAGELSKLFN----FNI----PQRWC----IAHLYQailNQEKSVSQID 157
Cdd:cd07773 74 SSQgESGVPV-DRDGEPLGPAIVWFDPRGKEEAEELAERIGaeelYRItglpPSPMYslakLLWLRE---HEPEIFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 158 FMTTLAGYVHWRLTGKKVTGIGDAS--GIFpiDSNSKDYDqKKLDQFSDLDgvekqpwdiKRILPKVLLAGQNAGQLTKE 235
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDYSLASrtMLF--DIRKRTWS-EELLEAAGID---------ASLLPELVPSGTVIGTVTPE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 236 GSllidpsgdlqdgSVFCPPEG--------DAGTGMVATNSVNQRSGNVSAGTSIFSMVVLEHPL---KKVYPEVDVVST 304
Cdd:cd07773 218 AA------------EELGLPAGtpvvvgghDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPldeMLAEGGLSYGHH 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 305 PTGDDVAMIHANNATSDINAWMHLFeeflvlagkklDKETVFRSLFFSALTDADADAGNLLTYGYYSGENITGLKEGRPL 384
Cdd:cd07773 286 VPGGYYYLAGSLPGGALLEWFRDLF-----------GGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 385 LVRSPESKFTIANLMRAQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTPrVAQQILADVLETPISVTENaAEGGAW 464
Cdd:cd07773 355 AFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSP-LWLQLKADILGRPIEVPEV-PEATAL 432
|
....*...
gi 696225539 465 GIAILAAY 472
Cdd:cd07773 433 GAALLAGV 440
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
14-471 |
3.31e-13 |
|
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: 71.78 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANnFEVLASGSFEWENQLVNGIWTY-SLDDVWKGLQASyTdlkAEVKDKYDFKLSKIGQIGISA 92
Cdd:cd07805 3 LAIDLGTSGVKAALVDLD-GELVASAFAPYPTYYPKPGWAEqDPEDWWDAVCRA-T---RALLEKSGIDPSDIAAIAFSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHGYLVFDQADKQLaefrtwRNAIT-------EQAAgELSKLFNFnipqrwciAHLYQAILNQEKSVS----------- 154
Cdd:cd07805 78 QMQGVVPVDKDGNPL------RNAIIwsdtraaEEAE-EIAGGLGG--------IEGYRLGGGNPPSGKdplakilwlke 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 155 ---QIDFMTTL----AGYVHWRLTGKKVTGIGDASGIFPIDSNSKDYDQKKLDQFsDLDgvekqpwdiKRILPKVLLAGQ 227
Cdd:cd07805 143 nepEIYAKTHKfldaKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAA-GID---------PDKLPELVPSTE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 228 NAGQLTKEGSLLIDpsgdLQDG-SVFCPPeGDAGTGMVATNSVNQRSGNVSAGTSifSMVVLEHPLKKVYPEVDVVSTPT 306
Cdd:cd07805 213 VVGELTPEAAAELG----LPAGtPVVGGG-GDAAAAALGAGAVEEGDAHIYLGTS--GWVAAHVPKPKTDPDHGIFTLAS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 307 GD-DVAMIHANNATSDINAwmhlfeEFLV--LAGKKLDKETVFRsLFFSALTDADADAGNLLTYGYYSGEnitglkegrp 383
Cdd:cd07805 286 ADpGRYLLAAEQETAGGAL------EWARdnLGGDEDLGADDYE-LLDELAAEAPPGSNGLLFLPWLNGE---------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 384 llvRSPES----KFTIANLM----RAQIL-SVF-G---ALKIGMDILKKEEVKIDRLTGHGGLFKTPrVAQQILADVLET 450
Cdd:cd07805 349 ---RSPVEdpnaRGAFIGLSlehtRADLArAVLeGvafNLRWLLEALEKLTRKIDELRLVGGGARSD-LWCQILADVLGR 424
|
490 500
....*....|....*....|.
gi 696225539 451 PISVTENAAEGGAWGIAILAA 471
Cdd:cd07805 425 PVEVPENPQEAGALGAALLAA 445
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
14-472 |
4.29e-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: 71.40 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANNfEVLASGSFEwenqlvngiwtYSLD-----------DVWKGlqaSYTDLKAEVKDKYDFKL 82
Cdd:cd07804 3 LGIDIGTTGTKGVLVDEDG-KVLASASIE-----------HDLLtpkpgwaehdpEVWWG---AVCEIIRELLAKAGISP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 83 SKIGQIGISAM--------------MHGYLVFD-QADKQLAEFRTW----------RNAITEQAAGelSKLfnfnipqRW 137
Cdd:cd07804 68 KEIAAIGVSGLvpalvpvdengkplRPAILYGDrRATEEIEWLNENigedrifeitGNPLDSQSVG--PKL-------LW 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 138 ciahlyqaILNQEKSV-SQIDFMTTLAGYVHWRLTGKKVTGIGDASGIFPI-DSNSKDYDQKKLDQFS-DLDgvekqpwd 214
Cdd:cd07804 139 --------IKRNEPEVfKKTRKFLGAYDYIVYKLTGEYVIDYSSAGNEGGLfDIRKRTWDEELLEALGiDPD-------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 215 ikrILPKVLLAGQNAGQLTKEGSLLidpSGdLQDGSVFCPPEGDAGTGMVATNSVnqRSGNVSA--GTSIFSMVVLEHP- 291
Cdd:cd07804 203 ---LLPELVPSTEIVGEVTKEAAEE---TG-LAEGTPVVAGTVDAAASALSAGVV--EPGDLLLmlGTAGDIGVVTDKLp 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 292 -LKKVYPEVDVVstpTGDDVAMIHANNATSDINAWMHLFEEFLVLAGKKlDKETVFRSLFFSAlTDADADAGNLLTYGYY 370
Cdd:cd07804 274 tDPRLWLDYHDI---PGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEKS-GGDSAYDLLDEEA-EKIPPGSDGLIVLPYF 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 371 SGEnitglkegrpllvRSP----ESKFTI---------ANLMRAQILSVFGALKIGMDILKKEEVKIDRLTGHGGLFKTP 437
Cdd:cd07804 349 MGE-------------RTPiwdpDARGVIfgltlshtrAHLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSP 415
|
490 500 510
....*....|....*....|....*....|....*
gi 696225539 438 rVAQQILADVLETPISVTENAAeGGAWGIAILAAY 472
Cdd:cd07804 416 -LWRQIVADVTGVPQEYVKDTV-GASLGDAFLAGV 448
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
13-237 |
6.07e-12 |
|
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: 65.82 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 13 ALGVEFGSTRIKSVLIDANNfEVLASGSFEWENQLVNGIWT-YSLDDVWKGLQASYtdlkAEVKDKYDFKLSKIGQIGIS 91
Cdd:pfam00370 2 YLGIDCGTTSTKAILFNEQG-KIIAVAQLENPQITPHPGWAeQDPDEIWQAVAQCI----AKTLSQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 92 AMMHGYLVFDQADKQLAEFRTWRNAITEQAAGELSKLFNFN-------IPQ---------RWciahlyqaILNQEKSV-S 154
Cdd:pfam00370 77 NQGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQklyeitgLPIwpgftlsklRW--------IKENEPEVfE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 155 QIDFMTTLAGYVHWRLTGKKVTGIGDASGIFPIDSNSKDYDQKKLDQFsdldGVEkqpwdiKRILPKVLLAGQNAGQLTK 234
Cdd:pfam00370 149 KIHKFLTIHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAAL----GIP------RDHLPPLVESSEIYGELNP 218
|
...
gi 696225539 235 EGS 237
Cdd:pfam00370 219 ELA 221
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
14-471 |
2.04e-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: 63.01 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANNfEVLASGSFEWE---NQLVNGIWTYSLDDVWKGLqasyTDLKAEVKDKYDFKLSKIGQIGI 90
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEG-KIVAIAYREWEyytDDDYPDAKEFDPEELWEKI----CEAIREALKKAGISPEDISAVSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 91 SAMMHGYLVFDQADKQL--------------AEFRTWR-NAITEQAAGELSKLFnfnipqrwCIAHLYQAILNQEKSVSQ 155
Cdd:cd07798 78 TSQREGIVFLDKDGRELyagpnidargveeaAEIDDEFgEEIYTTTGHWPTELF--------PAARLLWFKENRPEIFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 156 IDFMTTLAGYVHWRLTGKKVTGIGDASGIFPIDSNSKDYDQKKLDQFsDLDgvekqpwdiKRILPKVLLAGQNAGQLTKE 235
Cdd:cd07798 150 IATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEAL-GLP---------PEILPEIVPSGTVLGTVSEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 236 GS--LLIDPS-------GDLQDGSVfcppegdaGTGMVATNSVNqrsgnVSAGTSIFSMVVLEHPLkkvypevdvvstpt 306
Cdd:cd07798 220 AAreLGLPEGtpvvvggADTQCALL--------GSGAIEPGDIG-----IVAGTTTPVQMVTDEPI-------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 307 gDDVAMihannatsdiNAW--MHLFEEFLVL------AGKKLDKetvFRSLFFSALTD---------ADADAGNLLTYGY 369
Cdd:cd07798 273 -IDPER----------RLWtgCHLVPGKWVLesnagvTGLNYQW---LKELLYGDPEDsyevleeeaSEIPPGANGVLAF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 370 YSGEN----ITGLKEGrPLLVRSP--ESKFTIANLMRAQILSVFGALKIGMDILKK-EEVKIDRLTGHGGLFKTPRVAQq 442
Cdd:cd07798 339 LGPQIfdarLSGLKNG-GFLFPTPlsASELTRGDFARAILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALLCQ- 416
|
490 500
....*....|....*....|....*....
gi 696225539 443 ILADVLETPISVTENaAEGGAWGIAILAA 471
Cdd:cd07798 417 ILADVLGKPVLVPEG-REASALGAAICAA 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
14-472 |
1.50e-09 |
|
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: 59.93 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANNfEVLASGSFEWENQLVNGIWTY-SLDDVWKGLQASYTDLKAEVkdkydfKLSKIGQIGISA 92
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDG-TVLASASEPYPTSRPGPGWVEqDPEDWWEALRSLLRELPAEL------RPRRVVAIAVDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 93 MMHGYLVFDQADKQLAEFRTWRNAITEQAAGELSKLFNFNIPQ--------------RWCIAHLYQAILNQEKSVSQIDf 158
Cdd:cd07783 76 TSGTLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRtglavspssslaklLWLKRHEPEVLAKTAKFLHQAD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 159 mttlagYVHWRLTGKKvtGIGDASgifpidSNSK-DYDQKKLDQFSDLdgvEKQPWDIKRILPKVLLAGQNAGQLTKEGS 237
Cdd:cd07783 155 ------WLAGRLTGDR--GVTDYN------NALKlGYDPETGRWPSWL---LALLGIPPDLLPRVVAPGTVIGTLTAEAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 238 lliDPSGDLQDGSVFCppeG--DAGTGMVATNSVNQRSGNVSAGTS-IFSMVV---LEHPLKKVY--PEVDVVSTPTGdd 309
Cdd:cd07783 218 ---EELGLPAGTPVVA---GttDSIAAFLASGAVRPGDAVTSLGTTlVLKLLSdkrVPDPGGGVYshRHGDGYWLVGG-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 310 vamihANNATSDINAWmHLFEEFLVLAGKKLDKETvfrslffsaltdadadAGNLLTYGYYS-GE-------NITGLKEG 381
Cdd:cd07783 290 -----ASNTGGAVLRW-FFSDDELAELSAQADPPG----------------PSGLIYYPLPLrGErfpfwdpDARGFLLP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 382 RPLlvrspeskfTIANLMRAQILSVFGALKIGMDILKK-EEVKIDRLTGHGGLFKTPRVaQQILADVLETPISVTENaaE 460
Cdd:cd07783 348 RPH---------DRAEFLRALLEGIAFIERLGYERLEElGAPPVEEVRTAGGGARNDLW-NQIRADVLGVPVVIAEE--E 415
|
490
....*....|..
gi 696225539 461 GGAWGIAILAAY 472
Cdd:cd07783 416 EAALGAALLAAA 427
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
13-517 |
5.56e-09 |
|
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: 58.32 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 13 ALGVEFGSTRIKSVLIDANNFEVLASGSFE---WENQLVNGIWTYSLDDVWKGL-QASYTDLKAEVKDKYDfklskIGQI 88
Cdd:cd07781 2 VIGIDFGTQSVRAGLVDLADGEELASAVVPyptGYIPPRPGWAEQNPADYWEALeEAVRGALAEAGVDPED-----VVGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 89 GI----SAMmhgyLVFDQADKQLAEFRTWR--------NAITEQAAGEL---SKLFNFNIPQRWCIAHLYQaILNQEKSV 153
Cdd:cd07781 77 GVdttsSTV----VPVDEDGNPLAPAILWMdhraqeeaAEINETAHPALeyyLAYYGGVYSSEWMWPKALW-LKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 154 -SQIDFMTTLAGYVHWRLTGKKVTGIGDAS--------GIFPidsnSKDYdqkkldqFSDLDGVEKQPWDikRILPKVLL 224
Cdd:cd07781 152 yDAAYTIVEACDWINARLTGRWVRSRCAAGhkwmynewGGGP----PREF-------LAALDPGLLKLRE--KLPGEVVP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 225 AGQNAGQLTKEGSLLIDpsgdLQDGSVFCPPEGDAGTGMVATNSVnqRSGNVSA--GTSIFSMVVLEHPLK-----KVYP 297
Cdd:cd07781 219 VGEPAGTLTAEAAERLG----LPAGIPVAQGGIDAHMGAIGAGVV--EPGTLALimGTSTCHLMVSPKPVDipgicGPVP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 298 EVdVVstptgDDVAMIHA-NNATSDINAWmhlFEEFLVLAGKKLDKETvfrslfFSALTDA----DADAGNLLTYGYYSG 372
Cdd:cd07781 293 DA-VV-----PGLYGLEAgQSAVGDIFAW---FVRLFVPPAEERGDSI------YALLSEEaaklPPGESGLVALDWFNG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 373 -------ENITGLKEGRPLLVRSPEskftianLMRAQILSV-FGALKIgMDILKKEEVKIDRLTGHGGLFKTPRVAQQIL 444
Cdd:cd07781 358 nrtplvdPRLRGAIVGLTLGTTPAH-------IYRALLEATaFGTRAI-IERFEEAGVPVNRVVACGGIAEKNPLWMQIY 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 696225539 445 ADVLETPISVTENaAEGGAWGIAILAAYVDKASElSLAEylKSKVFsASSTITIEPN------YDDLpgthkfMDRYQK 517
Cdd:cd07781 430 ADVLGRPIKVPKS-DQAPALGAAILAAVAAGVYA-DIEE--AADAM-VRVDRVYEPDpenhavYEEL------YALYKE 497
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
14-471 |
3.12e-07 |
|
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: 53.01 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 14 LGVEFGSTRIKSVLIDANNfEVLASGSFEweNQLVN---GIWTYSLDDVWKGLQASYTDLKAEVKDKYDfklsKIGQIGI 90
Cdd:cd24121 3 IGIDAGTSVVKAVAFDLDG-RELAVAARR--NAVLYpqpGWAEQDMNETWQAVVATIREVVAKLDVLPD----RVAAIGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 91 SAMMHG-YLVfdqaDKQLAEFR---TW---RNA--ITE-QAAGELSKLFNFN---------IPQrwcIAHLYQailNQEK 151
Cdd:cd24121 76 TGQGDGtWLV----DEDGRPVRdaiLWldgRAAdiVERwQADGIAEAVFEITgtglfpgsqAAQ---LAWLKE---NEPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 152 SVSQIDFMTTLAGYVHWRLTGKKVTGIGDASGIFpIDSNSKDYDQKKLDQFsdldGVEKQpwdiKRILPKVLLAGQNAGQ 231
Cdd:cd24121 146 RLERARTALHCKDWLFYKLTGEIATDPSDASLTF-LDFRTRQYDDEVLDLL----GLEEL----RHLLPPIRPGTEVIGP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 232 LTKEGSLLIdpsgDLQDGSvfcpPEGDAGTGMVAT----NSVNQRSGNVSAGTSIFSMVVLEHPLKKVYPEVDVVSTPTG 307
Cdd:cd24121 217 LTPEAAAAT----GLPAGT----PVVLGPFDVVATalgsGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTICLGVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 308 DDVA-MIHANNATSDINAWMHLFEEFLVLAGKKLDKEtVFRsLFFSALTDADADAGNLLTYGYYS--GE----------- 373
Cdd:cd24121 289 GRWLrAMANMAGTPNLDWFLRELGEVLKEGAEPAGSD-LFQ-DLEELAASSPPGAEGVLYHPYLSpaGErapfvnpnara 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 374 NITGLKegrpllvrspeSKFTIANLMRAQILSVFGALK-----IGMDIlkkEEVkidRLTghGGLFKTPRVAqQILADVL 448
Cdd:cd24121 367 QFTGLS-----------LEHTRADLLRAVYEGVALAMRdcyehMGEDP---GEL---RLS--GGGARSDTWC-QILADAL 426
|
490 500
....*....|....*....|...
gi 696225539 449 ETPISVTENaAEGGAWGIAILAA 471
Cdd:cd24121 427 GVPVRVPAG-EEFGARGAAMNAA 448
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
97-292 |
2.69e-05 |
|
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: 46.75 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 97 YLVFDQADKQLAEFRTWRNAITEQAAGELSK------LFNF--NIPQRWC-IAHLYQAILNQEKSVSQIDFMTTLAGYVH 167
Cdd:cd07771 80 FGLLDKNGELLGNPVHYRDPRTEGMMEELFEkiskeeLYERtgIQFQPINtLYQLYALKKEGPELLERADKLLMLPDLLN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696225539 168 WRLTGKKVTGIGDAS--GIFpiDSNSKDYDQKKLDQFsDLDgvekqpwdiKRILPKVLLAGQNAGQLTKEgsllIDPSGD 245
Cdd:cd07771 160 YLLTGEKVAEYTIASttQLL--DPRTKDWSEELLEKL-GLP---------RDLFPPIVPPGTVLGTLKPE----VAEELG 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 696225539 246 LQDGSVFCPPEGDAGTGMVATNSVNQRSGNVSAGT-SIFsMVVLEHPL 292
Cdd:cd07771 224 LKGIPVIAVASHDTASAVAAVPAEDEDAAFISSGTwSLI-GVELDEPV 270
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
407-471 |
2.76e-05 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 46.76 E-value: 2.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696225539 407 FGALKIgMDILKKEEVKIDRLTGHGGLFKTPRVAQQILADVLETPISVTEnAAEGGAWGIAILAA 471
Cdd:PRK04123 423 FGTRAI-MECFEDQGVPVEEVIAAGGIARKNPVLMQIYADVLNRPIQVVA-SDQCPALGAAIFAA 485
|
|
| |
