|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-478 |
0e+00 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 893.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 1 MPIAFIFDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEATDYHIWDIEEIWSKLMTCAKQTLAQLTPeqrQDIVGISV 80
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARASTPNASDIAAENSDWHQWSLDAILQRFADCCRQINSELTE---CHIRGITV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 81 TTFGVDGAIFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLF 160
Cdd:PRK10331 78 TTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 161 ISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSC 240
Cdd:PRK10331 158 ISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 241 GHDTQFAIFGSGAGYNQPVLSSGTWEILMARTQQAKPEWQYVKDGLTIEFDSQAGYFNPGVQWVSSGIMEWLGKRFFSdv 320
Cdd:PRK10331 238 GHDTQFALFGSGAGQNQPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQSGLYNPGMQWLASGVLEWVRKLFWT-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 321 agTADYYPTMINEGSQVPAGSNGLKLVGNFDGTsqQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAE 400
Cdd:PRK10331 316 --AETPYQTMIEEARAIPPGADGVKMQCDLLAC--QNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKAS 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1130437276 401 SIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEPSGDVRVYQS 478
Cdd:PRK10331 392 ELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYPQTEPEFIEE 469
|
|
| fuculo_kin_coli |
TIGR02628 |
L-fuculokinase; Members of this family are L-fuculokinase, from the clade that includes the ... |
3-470 |
0e+00 |
|
L-fuculokinase; Members of this family are L-fuculokinase, from the clade that includes the L-fuculokinase of Escherichia coli. This enzyme catalyzes the second step in fucose catabolism. This family belongs to FGGY family of carbohydrate kinases (pfam02782, pfam00370). It is encoded by the kinase (K) gene of the fucose (fuc) operon. [Energy metabolism, Sugars]
Pssm-ID: 131676 [Multi-domain] Cd Length: 465 Bit Score: 650.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 3 IAFIFDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEATDYHIWDIEEIWSKLMTCAKQTLAQLTpeqRQDIVGISVTT 82
Cdd:TIGR02628 2 VILVLDCGATNLRAIAINRQGKIVASASTPNATKQAIENNDYHIWDLEAIWQKLADCCQQINSELT---EKHIRGIAVTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 83 FGVDGAIFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLFIS 162
Cdd:TIGR02628 79 FGVDGAPFDKQGNQLYPIISWKCPRTAPVMDNIERLLDAQRLYAINGIGAYSFNTLYKLVWLKEHHPQLFERMHKFVFIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 163 SILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGH 242
Cdd:TIGR02628 159 SMITHRLTGEFTTDITMAGTSMMTDLTQRNWSPQILQALGLSRRLFPPLVEAGEQIGTLQNSAAAMLGLPVGVPVISAGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 243 DTQFAIFGSGAGYNQPVLSSGTWEILMARTQQAKPEWQYVKDGLTIEFDSQAGYFNPGVQWVSSGIMEWLGKRFFSDVAG 322
Cdd:TIGR02628 239 DTQFALFGSGAEQNQPVLSSGTWEILMARSQQVDTSLLSQYAGSTCELDSQAGLYNPAMQWLASGVLEWVRKLFFTAETP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 323 TADYYPTMINEGSQV-PAGSNGLKLVGNFDGTSQqtGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAES 401
Cdd:TIGR02628 319 SDHYYQMMIEEARLIaNGADGVVNFQCDLLSCGQ--GGIQGLTLNTTRGHIYRAALEGLTAQLKRNLQMLEQIGQFKASE 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130437276 402 IICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEPS 470
Cdd:TIGR02628 397 LLLVGGGSKNTLWNQIRANMLDIPVKVVDDAETTVAGAAMFGFYGVGEYNSPEEAQAQMHPQYRYFYPQ 465
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
7-448 |
3.13e-128 |
|
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: 379.24 E-value: 3.13e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 7 FDCGATNLRIVAMDHHGKLLAVHHIANNTQqgEEATDYHIWDIEEIWSKLMTCAKQTLAQLTPEQrqdIVGISVTTFGVD 86
Cdd:cd07773 5 IDIGTTNVKAVLFDEDGRILASASRETPLI--HPGPGWAELDPEELWEAVKEAIREAAAQAGPDP---IAAISVSSQGES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 87 GAIFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLFISSILT 166
Cdd:cd07773 80 GVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 167 YRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGHDTQF 246
Cdd:cd07773 160 YRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHLC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 247 AIFGSGA-GYNQPVLSSGTWEILMARTQQAKPEWQYVKDGLTIEFDSQAGYFNPGVQWVSSGIMEWLGKRFFSDVAGTAD 325
Cdd:cd07773 240 AALGAGViEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSYGHHVPGGYYYLAGSLPGGALLEWFRDLFGGDESDLAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 326 yyptMINEGSQVPAGSNGLKLVGNFDGT------SQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGqFNA 399
Cdd:cd07773 320 ----ADELAEAAPPGPTGLLFLPHLSGSgtpdfdPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAG-IPI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1130437276 400 ESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAG 448
Cdd:cd07773 395 DEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
7-477 |
2.04e-102 |
|
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: 314.85 E-value: 2.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 7 FDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEAtdyhiW---DIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTTF 83
Cdd:COG1070 6 IDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPG-----WaeqDPEDWWEAVVEAIRELLAKA-GVDPEEIAAIGVSGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 84 GvDGAI-FDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVG-HYSFnTLFKLLWLKQHKPELYAQAESFLFI 161
Cdd:COG1070 80 M-HGLVlLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPlHPGF-TAPKLLWLKENEPEIFARIAKVLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 162 SSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCG 241
Cdd:COG1070 158 KDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 242 HDTQFAIFGSGA-GYNQPVLSSGTWEILMARTQQAKPEWQYVKDGLTiefDSQAGYFNPGVQWVSSGIM-EWLGKRFFsd 319
Cdd:COG1070 238 GDNAAAALGAGAvEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFC---HAVPGRWLPMGATNNGGSAlRWFRDLFA-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 320 vAGTADYYPTMINEGSQVPAGSNGLKLVGNFDG------TSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQ 393
Cdd:COG1070 313 -DGELDDYEELNALAAEVPPGADGLLFLPYLSGertphwDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 394 VGQfNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEP-SGD 472
Cdd:COG1070 392 AGV-KIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPdPEN 470
|
....*
gi 1130437276 473 VRVYQ 477
Cdd:COG1070 471 VAAYD 475
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-250 |
7.01e-93 |
|
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: 281.92 E-value: 7.01e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 3 IAFIFDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEatDYHIWDIEEIWSKLMTCAKQTLAQLTPEQrQDIVGISVTT 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHP--GWAEQDPDEIWQAVAQCIAKTLSQLGISL-KQIKGIGISN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 83 FGVDGAIFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLFIS 162
Cdd:pfam00370 78 QGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 163 SILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGH 242
Cdd:pfam00370 158 DYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGG 237
|
....*...
gi 1130437276 243 DTQFAIFG 250
Cdd:pfam00370 238 DQQAAAFG 245
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
7-442 |
2.07e-80 |
|
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: 254.80 E-value: 2.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 7 FDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEatDYHIWDIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTTFGVD 86
Cdd:cd00366 5 IDIGTTSVKAALFDEDGNLVASASREYPLIYPQP--GWAEQDPEDWWQAVVEAIREVLAKA-GIDPSDIAAIGISGQMPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 87 GAIFDKHGKQLYPIISWKCPRtqpimqalgdyldveklyqrngvghysfntlfkllwlkqHKpelyaqaesFLFISSILT 166
Cdd:cd00366 82 VVLVDADGNPLRPAIIWLDRR---------------------------------------AK---------FLQPNDYIV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 167 YRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGHDTQF 246
Cdd:cd00366 114 FRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTAA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 247 AIFGSGA-GYNQPVLSSGTWEILMARTQQAKPEwqyvKDGLTIEFDSQAG-YFNPGVQWVSSGIMEWLGKRFFSDvAGTA 324
Cdd:cd00366 194 AALGAGVvEPGDAVDSTGTSSVLSVCTDEPVPP----DPRLLNRCHVVPGlWLLEGAINTGGASLRWFRDEFGEE-EDSD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 325 DYYPTMINEGSQVPAGSNGLKLVGNFDG------TSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGqFN 398
Cdd:cd00366 269 AEYEGLDELAAEVPPGSDGLIFLPYLSGerspiwDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELG-VK 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1130437276 399 AESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMF 442
Cdd:cd00366 348 IKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAIL 391
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-469 |
1.28e-73 |
|
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: 240.13 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEAtdyhiW---DIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTtfG 84
Cdd:cd07808 6 DLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPG-----WaeqDPEDWWQATKEALRELLAKA-GISPSDIAAIGLT--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 85 -VDGAIF-DKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFnTLFKLLWLKQHKPELYAQAESFLFIS 162
Cdd:cd07808 78 qMHGLVLlDKNGRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPGF-TLPKLLWLKENEPEIFARIRKILLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 163 SILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGH 242
Cdd:cd07808 157 DYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 243 DTQFAIFGSGA-GYNQPVLSSGTWEILMARTQQAKPEWQyvkDGLTIefdsqagyFNPGV--QWVSSGIM-------EWL 312
Cdd:cd07808 237 DNAAAALGAGVvEPGDALISLGTSGVVFAPTDKPVPDPK---GRLHT--------FPHAVpgKWYAMGVTlsaglslRWL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 313 GKRFFSDVAGtadyYPTMINEGSQVPAGSNGL----KLVG----NFDgtSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRL 384
Cdd:cd07808 306 RDLFGPDRES----FDELDAEAAKVPPGSEGLlflpYLSGertpYWD--PNARGSFFGLSLSHTRAHLARAVLEGVAFSL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 385 KAGLEVLQQVGqFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAF 464
Cdd:cd07808 380 RDSLEVLKELG-IKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIE 458
|
....*
gi 1130437276 465 KRMEP 469
Cdd:cd07808 459 KTIEP 463
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
7-477 |
8.91e-73 |
|
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: 237.80 E-value: 8.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 7 FDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEAtdyhiW---DIEEIWSKLMTCAKQTLAQlTPEQRQDIVGISVTT- 82
Cdd:cd07805 5 IDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPG-----WaeqDPEDWWDAVCRATRALLEK-SGIDPSDIAAIAFSGq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 83 -FGVdgaIF-DKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYS-FNTLFKLLWLKQHKPELYAQAESFL 159
Cdd:cd07805 79 mQGV---VPvDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSgKDPLAKILWLKENEPEIYAKTHKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 160 FISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLS 239
Cdd:cd07805 156 DAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 240 CGHDTQFAIFGSGAG-YNQPVLSSGT--WeilMARTQQAKPE--------WQYVKDGLTIEFDSQ--AGyfnpgvqwvss 306
Cdd:cd07805 236 GGGDAAAAALGAGAVeEGDAHIYLGTsgW---VAAHVPKPKTdpdhgiftLASADPGRYLLAAEQetAG----------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 307 GIMEWLGKRFFSDVAGTADYYPTMINEGSQVPAGSNGL----KLVGN----FDGTSQqtGSIEGLSMHTQRGEIYRAGLE 378
Cdd:cd07805 302 GALEWARDNLGGDEDLGADDYELLDELAAEAPPGSNGLlflpWLNGErspvEDPNAR--GAFIGLSLEHTRADLARAVLE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 379 YMAHRLKAGLEVLQQVGQfNAESIICVGGGSKNGLWNQIRADVLNRPIDVV-DMSETTVLGAAMFTLTGAGVFENIEQAQ 457
Cdd:cd07805 380 GVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPeNPQEAGALGAALLAAVGLGLLKSFDEAK 458
|
490 500
....*....|....*....|.
gi 1130437276 458 QAMKPAfKRMEPS-GDVRVYQ 477
Cdd:cd07805 459 ALVKVE-KVFEPDpENRARYD 478
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
8-477 |
1.36e-72 |
|
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: 237.07 E-value: 1.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEATDYHiwDIEEIWSKLMTCAKQTLAQLTPEQrqdIVGISVTTF---- 83
Cdd:cd07770 6 DIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQ--DPEEILEAVLEALKEVLAKLGGGE---VDAIGFSSAmhsl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 84 -GVDgaifdKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVG-HYSFnTLFKLLWLKQHKPELYAQAESFLFI 161
Cdd:cd07770 81 lGVD-----EDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPiHPMY-PLAKLLWLKEERPELFAKAAKFVSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 162 SSILTYRLTGVQSTDRTMA-GTSMMtNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSC 240
Cdd:cd07770 155 KEYLLYRLTGELVTDYSTAsGTGLL-NIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 241 GHDTQFAIFGSGAGY-NQPVLS---SGtweilMARtqqakpewqYVKDGLTIefDSQAGYFN---PGVQWVSSG------ 307
Cdd:cd07770 234 ASDGALANLGSGALDpGRAALTvgtSG-----AIR---------VVSDRPVL--DPPGRLWCyrlDENRWLVGGainngg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 308 -IMEWLGKRFFSDVAGtadyYPTMINEGSQVPAGSNGLK----LVG----NFDgtSQQTGSIEGLSMHTQRGEIYRAGLE 378
Cdd:cd07770 298 nVLDWLRDTLLLSGDD----YEELDKLAEAVPPGSHGLIflpyLAGerapGWN--PDARGAFFGLTLNHTRADILRAVLE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 379 YMAHRLKAGLEVLQQVGQfNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAqq 458
Cdd:cd07770 372 GVAFNLKSIYEALEELAG-PVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEAD-- 448
|
490 500
....*....|....*....|
gi 1130437276 459 AMKPAFKRMEP-SGDVRVYQ 477
Cdd:cd07770 449 ELVKIGKVVEPdPENHAIYA 468
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
8-476 |
3.30e-69 |
|
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: 227.02 E-value: 3.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEatDYHIWDIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTTFGvdG 87
Cdd:cd07779 6 DVGTTSTRAIIFDLDGNIVASGYREYPPYYPEP--GWVEQDPDDWWDALCEALKEAVAKA-GVDPEDIAAIGLTSQR--S 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 88 AIF--DKHGKQLYPIISWKCPRTqpimqalgdyldveklyqrngvghysfntlfkllwlkqHKpelyaqaesFLFISSIL 165
Cdd:cd07779 81 TFVpvDEDGRPLRPAISWQDKRT--------------------------------------AK---------FLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 166 TYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGHDTQ 245
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 246 FAIFGSGA-GYNQPVLSSGTWEILMARTQQakpewqYVKD---GLTIEFDSQAGYFNP-GVQWVSSGIMEWLGKRFFSDV 320
Cdd:cd07779 194 CAALGAGVlEPGTASLSLGTAAVVIAVSDK------PVEDperRIPCNPSAVPGKWVLeGSINTGGSAVRWFRDEFGQDE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 321 ----AGTADYYPTMINEGSQVPAGSNGLKLV------GNFDGTSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEV 390
Cdd:cd07779 268 vaekELGVSPYELLNEEAAKSPPGSDGLLFLpylagaGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 391 LQQVGQfNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEPS 470
Cdd:cd07779 348 MEKAGV-PIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPD 426
|
....*..
gi 1130437276 471 GD-VRVY 476
Cdd:cd07779 427 PEnVAIY 433
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
6-448 |
3.42e-68 |
|
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: 224.79 E-value: 3.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 6 IFDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEATDYHIWDIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTTFGv 85
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDAKEFDPEELWEKICEAIREALKKA-GISPEDISAVSSTSQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 86 DGAIF-DKHGKQLYpiiswKCP----RTQPIMQALGDYLDVEKlYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLF 160
Cdd:cd07798 82 EGIVFlDKDGRELY-----AGPnidaRGVEEAAEIDDEFGEEI-YTTTGHWPTELFPAARLLWFKENRPEIFERIATVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 161 ISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSC 240
Cdd:cd07798 156 ISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 241 GHDTQFAIFGSGAG-YNQPVLSSGTWEILMARTqqAKPE-------WQ--YVKDGL-TIEfdsqagyFNPGVqwvsSGIM 309
Cdd:cd07798 236 GADTQCALLGSGAIePGDIGIVAGTTTPVQMVT--DEPIidperrlWTgcHLVPGKwVLE-------SNAGV----TGLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 310 -EWLGKRFFSDVAGTadyYPTMINEGSQVPAGSNG-LKLVGN--FDGTSQQTG------SIEGLSMHTQRGEIYRAGLEY 379
Cdd:cd07798 303 yQWLKELLYGDPEDS---YEVLEEEASEIPPGANGvLAFLGPqiFDARLSGLKnggflfPTPLSASELTRGDFARAILEN 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130437276 380 MAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAG 448
Cdd:cd07798 380 IAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
7-461 |
8.39e-67 |
|
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: 221.63 E-value: 8.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 7 FDCGATNLRIVAMDHHGKLLA---VHHIANNTQQgeeaTDYHI-WDIEEIWSKLmtcaKQTLAQLTpEQRQDIVGISVTT 82
Cdd:cd07771 5 VDLGASSGRVILGSLDGGKLEleeIHRFPNRPVE----INGHLyWDIDRLFDEI----KEGLKKAA-EQGGDIDSIGIDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 83 FGVDGAIFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLFIS 162
Cdd:cd07771 76 WGVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 163 SILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLsADISV-LSCG 241
Cdd:cd07771 156 DLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGL-KGIPViAVAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 242 HDTQFAI-----FGSGAGYnqpvLSSGTWEILMARTqqAKPewqyvkdgLTIEFDSQAGYFNPGVqwvssgimeWLGK-R 315
Cdd:cd07771 235 HDTASAVaavpaEDEDAAF----ISSGTWSLIGVEL--DEP--------VITEEAFEAGFTNEGG---------ADGTiR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 316 FFSDVAG--------------TADY-YPTMINEGSQVPAgsngLKLV-----------GNFDGTSQQTGSIEGLSMHTQR 369
Cdd:cd07771 292 LLKNITGlwllqecrreweeeGKDYsYDELVALAEEAPP----FGAFidpddprflnpGDMPEAIRAYCRETGQPVPESP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 370 GEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIdVVDMSETTVLGAAMFTLTGAGV 449
Cdd:cd07771 368 GEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPV-IAGPVEATAIGNLLVQLIALGE 446
|
490
....*....|..
gi 1130437276 450 FENIEQAQQAMK 461
Cdd:cd07771 447 IKSLEEGRELVR 458
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
8-448 |
4.31e-63 |
|
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: 211.26 E-value: 4.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQqgEEATDYHIWDIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTTFGvDG 87
Cdd:cd07802 6 DNGTTNVKAVLFDLDGREIAVASRPTPVI--SPRPGWAERDMDELWQATAEAIRELLEKS-GVDPSDIAGVGVTGHG-NG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 88 AIF-DKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLFISSILT 166
Cdd:cd07802 82 LYLvDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 167 YRLTGVQSTDRTMAGTSMMtNIASDSWDSEVLDVLGLTA--NHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGHDT 244
Cdd:cd07802 162 YRLTGEISTDYTDAGSSLL-DLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 245 QFAIFGSGAgYNQPVLSS--GTW---EILMARTQQAKPEWQY----VKDGLTIEFDSQAgyfnpgvqwvSSGIMEWLGKR 315
Cdd:cd07802 241 VASALGAGA-VDEGQLCVilGTWsinEVVTDEPVVPDSVGSNslhaDPGLYLIVEASPT----------SASNLDWFLDT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 316 FFSDV-AGTADYYPTMINEGSQVPAGSNGLK----LVGNFDGtSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEV 390
Cdd:cd07802 310 LLGEEkEAGGSDYDELDELIAAVPPGSSGVIflpyLYGSGAN-PNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLER 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1130437276 391 LQQvgQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAG 448
Cdd:cd07802 389 LLV--ARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
8-469 |
4.13e-61 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 207.17 E-value: 4.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEAT---DYHIWdieeiWSKLMTCAKQTLAQlTPEQRQDIVGISVTtfG 84
Cdd:TIGR01312 4 DLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWseqDPEDW-----WDATEEAIKELLEQ-ASEMGQDIKGIGIS--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 85 -VDGAI-FDKHGKQLYPIISWKCPRTQP----IMQALGDyldvEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESF 158
Cdd:TIGR01312 76 qMHGLVlLDANGEVLRPAILWNDTRTAQeceeLEAELGD----ERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 159 LFISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVL 238
Cdd:TIGR01312 152 MLPKDYLRYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 239 SCGHDTQFAIFGSGA-GYNQPVLSSGTWEILMARTQQAKPEwqyvkdgltieFDSQAGYFNPGV--QWVSSGIM------ 309
Cdd:TIGR01312 232 AGGGDNAAGAIGTGTvDPGDAMMSLGTSGVVYAVTDKPLPD-----------PAGAVHGFCHALpgGWLPMGVTlsatss 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 310 -EWlgkrfFSDVAGTADYyPTMINEGSQVPAGSNGLKLVGNFDG------TSQQTGSIEGLSMHTQRGEIYRAGLEYMAH 382
Cdd:TIGR01312 301 lEW-----FRELFGKEDV-EALNELAEQSPPGAEGVTFLPYLNGertphlDPQARGSFIGLTHNTTRADLTRAVLEGVTF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 383 RLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKP 462
Cdd:TIGR01312 375 ALRDSLDILREAGGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVVK 454
|
....*..
gi 1130437276 463 AFKRMEP 469
Cdd:TIGR01312 455 QTESVLP 461
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-477 |
1.85e-55 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 192.16 E-value: 1.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 6 IFDCGATNLRIVAMDHHGKLLAV-----HHIANNTQQGeeATDYhiwDIEEIWSKLMTCAKQTLAQlTPEQRQDIVGISV 80
Cdd:cd07775 4 ALDAGTGSGRAVIFDLEGNQIAVaqrewRHKEVPDVPG--SMDF---DTEKNWKLICECIREALKK-AGIAPKSIAAIST 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 81 TTFGVDGAIFDKHGKQLypiisWKC----PRTQPIMQAL---GDYLDvEKLYQRNGvGHYSFNTLFKLLWLKQHKPELYA 153
Cdd:cd07775 78 TSMREGIVLYDNEGEEI-----WACanvdARAAEEVSELkelYNTLE-EEVYRISG-QTFALGAIPRLLWLKNNRPEIYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 154 QAESFLFISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSA 233
Cdd:cd07775 151 KAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 234 DISVLSCGHDTQFAIFGSGA-GYNQPVLSSGT-W--EILMA----------RTQQA--KPEWQYvkDGLTiefdsqagyF 297
Cdd:cd07775 231 GTPVVVGGGDVQLGCLGLGVvRPGQTAVLGGSfWqqEVNTAapvtdpamniRVNCHviPDMWQA--EGIS---------F 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 298 NPGVqwvssgIMEWLGKRFFSDVAGTA-----DYYPTMINEGSQVPAGSNGLKL----VGNFDGTSQQTGSIEGLSMH-- 366
Cdd:cd07775 300 FPGL------VMRWFRDAFCAEEKEIAerlgiDAYDLLEEMAKDVPPGSYGIMPifsdVMNYKNWRHAAPSFLNLDIDpe 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 367 -TQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLT 445
Cdd:cd07775 374 kCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGV 453
|
490 500 510
....*....|....*....|....*....|...
gi 1130437276 446 GAGVFENIEQAQQAMKPAFKRMEPSGDVR-VYQ 477
Cdd:cd07775 454 GAGIYSSLEEAVESLVKWEREYLPNPENHeVYQ 486
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-477 |
1.96e-55 |
|
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: 192.37 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMD-HHGKLLAVHhianntqqgeeATDYHIWDI-----------EEIWSKLMTCAKQTLAQLtPEQRQDI 75
Cdd:cd07781 6 DFGTQSVRAGLVDlADGEELASA-----------VVPYPTGYIpprpgwaeqnpADYWEALEEAVRGALAEA-GVDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 76 VGISVTTFGVDGAIFDKHGKQLYPIISWKCPRTQP---IMQALGDylDVEKLYQRNGVGHYSFNTLF-KLLWLKQHKPEL 151
Cdd:cd07781 74 VGIGVDTTSSTVVPVDEDGNPLAPAILWMDHRAQEeaaEINETAH--PALEYYLAYYGGVYSSEWMWpKALWLKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 152 YAQAESFLFISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGL----TANHFP-PMKSAGEKIGTLLPTLA 226
Cdd:cd07781 152 YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPgllkLREKLPgEVVPVGEPAGTLTAEAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 227 EELGLSADISVLSCGHDTQFAIFGSGAGynQP-----VLSSGTWEILMARTQQAKPE-WQYVKDGL-----TIEfdsqAG 295
Cdd:cd07781 232 ERLGLPAGIPVAQGGIDAHMGAIGAGVV--EPgtlalIMGTSTCHLMVSPKPVDIPGiCGPVPDAVvpglyGLE----AG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 296 yfnpgvQwVSSG-IMEWLGKRFFSDVAGTAD-YYPTMINEGSQVPAGSNGLKLVGNFDG-----TSQQ-TGSIEGLSMHT 367
Cdd:cd07781 306 ------Q-SAVGdIFAWFVRLFVPPAEERGDsIYALLSEEAAKLPPGESGLVALDWFNGnrtplVDPRlRGAIVGLTLGT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 368 QRGEIYRAGLEYMAHRLKAGLEVLQQVGqFNAESIICVGGGS-KNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTG 446
Cdd:cd07781 379 TPAHIYRALLEATAFGTRAIIERFEEAG-VPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVA 457
|
490 500 510
....*....|....*....|....*....|..
gi 1130437276 447 AGVFENIEQAQQAMKPAFKRMEPSGD-VRVYQ 477
Cdd:cd07781 458 AGVYADIEEAADAMVRVDRVYEPDPEnHAVYE 489
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
7-449 |
1.39e-53 |
|
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: 185.89 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 7 FDCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEATDYHiwDIEEIWSKLMTCAKQTLAQLTPEQrqdIVGISVTtfGVD 86
Cdd:cd07783 5 IDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQ--DPEDWWEALRSLLRELPAELRPRR---VVAIAVD--GTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 87 GAIF--DKHGKQLYPIISW--KCPRTQP--IMQALGDYLdveklyQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLF 160
Cdd:cd07783 78 GTLVlvDREGEPLRPAIMYndARAVAEAeeLAEAAGAVA------PRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 161 ISSILTYRLTGVQ-STDRTMAGTSMMtNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLS 239
Cdd:cd07783 152 QADWLAGRLTGDRgVTDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 240 CGHDTQFAIFGSGAGynQP---VLSSGTWEILMARTQQAKPewqyvkdgltiefDSQAGYFN---PGVQWV------SSG 307
Cdd:cd07783 231 GTTDSIAAFLASGAV--RPgdaVTSLGTTLVLKLLSDKRVP-------------DPGGGVYShrhGDGYWLvggasnTGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 308 imEWLGKRFFSD------------VAGTADYYPTMINeGSQVPAGSNGLKlvGNFdgtsqqtgsiegLSMHTQRGEIYRA 375
Cdd:cd07783 296 --AVLRWFFSDDelaelsaqadppGPSGLIYYPLPLR-GERFPFWDPDAR--GFL------------LPRPHDRAEFLRA 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1130437276 376 GLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDmSETTVLGAAMftLTGAGV 449
Cdd:cd07783 359 LLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAAL--LAAAGL 429
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
8-448 |
7.54e-53 |
|
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: 184.27 E-value: 7.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVH---HIANNTQQG--EEatdyhiwDIEEIWSKLMTCAKQTLAQlTPEQRQDIVGISVTT 82
Cdd:cd07804 6 DIGTTGTKGVLVDEDGKVLASAsieHDLLTPKPGwaEH-------DPEVWWGAVCEIIRELLAK-AGISPKEIAAIGVSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 83 FGVDGAIFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQR--NGVGHYSfnTLFKLLWLKQHKPELYAQAESFLF 160
Cdd:cd07804 78 LVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEItgNPLDSQS--VGPKLLWIKRNEPEVFKKTRKFLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 161 ISSILTYRLTGVQSTDRTMAG-TSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLS 239
Cdd:cd07804 156 AYDYIVYKLTGEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 240 CGHDTQFAIFGSGA---GYNQPVL-SSGTWEILMARTQQAKPEWqyvkdgltIEFDSQAGYFNPGVQWVSSG-IMEWLGK 314
Cdd:cd07804 236 GTVDAAASALSAGVvepGDLLLMLgTAGDIGVVTDKLPTDPRLW--------LDYHDIPGTYVLNGGMATSGsLLRWFRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 315 RFFSDV-----AGTADYYPTMINEGSQVPAGSNGLKLVGNFDG------TSQQTGSIEGLSMHTQRGEIYRAGLEYMAHR 383
Cdd:cd07804 308 EFAGEEveaekSGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGertpiwDPDARGVIFGLTLSHTRAHLYRALLEGVAYG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1130437276 384 LKAGLEVLQQVGQFNAEsIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAG 448
Cdd:cd07804 388 LRHHLEVIREAGLPIKR-LVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
7-441 |
4.15e-45 |
|
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: 163.49 E-value: 4.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 7 FDCGATNLRIVAMD-HHGKLLAV----HHianNTQQGEEATDYhiwDIEEIWSKLMTCAKQtLAQLTPEQRQDIVGIsvt 81
Cdd:cd07809 5 IDLGTQSIKAVLIDaETGRVVASgsapHE---NILIDPGWAEQ---DPEDWWDALQAAFAQ-LLKDAGAELRDVAAI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 82 tfGVDG-----AIFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFnTLFKLLWLKQHKPELYAQAE 156
Cdd:cd07809 75 --GISGqmhglVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARF-TASKLLWLKENEPEHYARIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 157 SFLFISSILTYRLTGVQSTDRTMA-GTSMMtNIASDSWDSEVLDVLGLTANH---FPPMKSAGEKIGTLLPTLAEELGLS 232
Cdd:cd07809 152 KILLPHDYLNWKLTGEKVTGLGDAsGTFPI-DPRTRDYDAELLAAIDPSRDLrdlLPEVLPAGEVAGRLTPEGAEELGLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 233 ADISVLSCGHDTQFAIFGSGAGYN-QPVLSSGTWEILMARTQQAkpewqyVKDGLtiefDSQAGYFNPGVQWV-----SS 306
Cdd:cd07809 231 AGIPVAPGEGDNMTGALGTGVVNPgTVAVSLGTSGTAYGVSDKP------VSDPH----GRVATFCDSTGGMLplintTN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 307 GIMEWLgKRFFSDVAGTadyYPTMINEGSQVPAGSNGLKLVGNFDG-----TSQQTGSIEGLSM--HTqRGEIYRAGLEY 379
Cdd:cd07809 301 CLTAWT-ELFRELLGVS---YEELDELAAQAPPGAGGLLLLPFLNGertpnLPHGRASLVGLTLsnFT-RANLARAALEG 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1130437276 380 MAHRLKAGLEVLQQVGqFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAM 441
Cdd:cd07809 376 ATFGLRYGLDILRELG-VEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAAL 436
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
8-472 |
4.68e-43 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 158.98 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANntqqgEEATDYHIW---DIEEIWSKLMTCAKQTLAQLTPE-QRQDIVGISVTTF 83
Cdd:PTZ00294 8 DQGTTSTRFIIFDEKGNVVSSHQIPH-----EQITPHPGWlehDPEEILRNVYKCMNEAIKKLREKgPSFKIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 84 GVDGAIFDKH-GKQLYPIISWKCPRTQPIMQAL-GDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQA--ESFL 159
Cdd:PTZ00294 83 RETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELtKKYGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVkeGTLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 160 F--ISSILTYRLTGVQS--TDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELglsADI 235
Cdd:PTZ00294 163 FgtIDTWLIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAVPLL---EGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 236 SVLSCGHDTQFAIFG-----SGAGYNqpvlSSGTWEILMARTQQAKpewQYVKDGL--TIEF----DSQAGYFNPGVQWV 304
Cdd:PTZ00294 240 PITGCIGDQQAALIGhgcfeKGDAKN----TYGTGCFLLMNTGTEI---VFSKHGLltTVCYqlgpNGPTVYALEGSIAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 305 SSGIMEWLGKR--FFSDVAGTADYYPTMINEGSQ--VPAGSnGLkLVGNFDGTSqqTGSIEGLSMHTQRGEIYRAGLEYM 380
Cdd:PTZ00294 313 AGAGVEWLRDNmgLISHPSEIEKLARSVKDTGGVvfVPAFS-GL-FAPYWRPDA--RGTIVGMTLKTTRAHIVRAALEAI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 381 AHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAM 460
Cdd:PTZ00294 389 ALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLI 468
|
490
....*....|..
gi 1130437276 461 KPAFKRMEPSGD 472
Cdd:PTZ00294 469 RRSNSTFSPQMS 480
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
8-470 |
1.39e-42 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 157.24 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNT---QQGeeatdyhiW---DIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVT 81
Cdd:cd07769 6 DQGTTSTRAILFDEDGNIVASAQKEHEQiypQPG--------WvehDPEEIWENTLEVIREALAKA-GISASDIAAIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 82 ----TFgvdgAIFDKH-GKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVghySFNTLF---KLLWLKQHKPELYA 153
Cdd:cd07769 77 nqreTT----VVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGL---PLDPYFsatKIKWILDNVPGARE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 154 QAES--FLF--ISSILTYRLTG--VQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTllptlAE 227
Cdd:cd07769 150 RAERgeLLFgtIDTWLIWKLTGgkVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGY-----TD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 228 ELGLSADISVLSCGHDTQFAIFG-----SGAGYNqpvlSSGTWEILMARTqqaKPEWQYVKDGL--TI--EFDSQAGYFN 298
Cdd:cd07769 225 PEGLGAGIPIAGILGDQQAALFGqgcfePGMAKN----TYGTGCFLLMNT---GEKPVPSKNGLltTIawQIGGKVTYAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 299 PGVQWVSSGIMEWL--GKRFFSDVAGTADYyptmineGSQVPaGSNGLKLVGNFDGT------SQQTGSIEGLSMHTQRG 370
Cdd:cd07769 298 EGSIFIAGAAIQWLrdNLGLIEDAAETEEL-------ARSVE-DNGGVYFVPAFSGLgapywdPDARGAIVGLTRGTTKA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 371 EIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVF 450
Cdd:cd07769 370 HIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFW 449
|
490 500
....*....|....*....|
gi 1130437276 451 ENIEQAQQAMKpAFKRMEPS 470
Cdd:cd07769 450 KDLDELASLWQ-VDKRFEPS 468
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
48-477 |
4.42e-42 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 156.70 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 48 DIEEIWSKLMTCAKQTL--AQLTPeqrQDIVGISVTTFGVDGAIFDKHGKQLypiisWKCPR-----TQPIMQALGDYLD 120
Cdd:PRK10939 49 DLEKNWQLACQCIRQALqkAGIPA---SDIAAVSATSMREGIVLYDRNGTEI-----WACANvdaraSREVSELKELHNN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 121 VEK-LYQRNGvGHYSFNTLFKLLWLKQHKPELYAQAESFLFISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLD 199
Cdd:PRK10939 121 FEEeVYRCSG-QTLALGALPRLLWLAHHRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 200 VLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGHDTQFAIFGSGA-GYNQPVLSSGTWeilmartqqakpe 278
Cdd:PRK10939 200 MAGLRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVVMGGGDVQLGCLGLGVvRPGQTAVLGGTF------------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 279 WQYVKD-GLTIEFDSQAGYFNPGV---QWVSSGI-------MEWLGKRFFSDVAGTA-----DYYPTMINEGSQVPAGSN 342
Cdd:PRK10939 267 WQQVVNlPAPVTDPNMNIRINPHVipgMVQAESIsfftgltMRWFRDAFCAEEKLLAerlgiDAYSLLEEMASRVPVGSH 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 343 GL----KLVGNFDGTSQQTGSIEGLSMHTQ---RGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWN 415
Cdd:PRK10939 347 GIipifSDVMRFKSWYHAAPSFINLSIDPEkcnKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWS 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1130437276 416 QIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEPSGDVR-VYQ 477
Cdd:PRK10939 427 QILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHeLYQ 489
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
8-448 |
5.48e-35 |
|
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: 135.83 E-value: 5.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQQGEeatdyHIW---DIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTTFG 84
Cdd:cd24121 6 DAGTSVVKAVAFDLDGRELAVAARRNAVLYPQ-----PGWaeqDMNETWQAVVATIREVVAKL-DVLPDRVAAIGVTGQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 85 vDGA-IFDKHGKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLFISS 163
Cdd:cd24121 80 -DGTwLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 164 ILTYRLTGVQSTDRTMAGTSMMtNIASDSWDSEVLDVLGLTA--NHFPPMKSAGEKIGTLLPTLAEELGLSADISV---- 237
Cdd:cd24121 159 WLFYKLTGEIATDPSDASLTFL-DFRTRQYDDEVLDLLGLEElrHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVvlgp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 238 -------LSCG---HDTQFAIFGSgAGYNQPVLSSgtweilmARTQQAKPewqyvkdGLTIEFDSQAGYfnpgVQWVSSg 307
Cdd:cd24121 238 fdvvataLGSGaiePGDACSILGT-TGVHEVVVDE-------PDLEPEGV-------GYTICLGVPGRW----LRAMAN- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 308 iM------EWLGKRFFSDVAGTA-----DYYPTMINEGSQVPAGSNGLkLV----------GNF-DGTSQqtGSIEGLSM 365
Cdd:cd24121 298 -MagtpnlDWFLRELGEVLKEGAepagsDLFQDLEELAASSPPGAEGV-LYhpylspagerAPFvNPNAR--AQFTGLSL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 366 HTQRGEIYRAGLEYMAHrlkAGLEVLQQVGQFNAESIICvGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLT 445
Cdd:cd24121 374 EHTRADLLRAVYEGVAL---AMRDCYEHMGEDPGELRLS-GGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAV 449
|
...
gi 1130437276 446 GAG 448
Cdd:cd24121 450 ALG 452
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
8-470 |
1.04e-33 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 132.61 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHianntqqgEEATDYHI---W---DIEEIWSKLMTCAKQTLAQ--LTPEqrqDIVGIS 79
Cdd:cd07786 6 DQGTTSSRAILFDHDGNIVAVAQ--------REFTQIYPkpgWvehDPEEIWESQLAVAREALAKagIRAS---DIAAIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 80 V-----TTfgvdgAIFDKH-GKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNG--VGHYsfntlF---KLLWLKQHK 148
Cdd:cd07786 75 ItnqreTT-----VVWDREtGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGlvLDPY-----FsatKIRWILDNV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 149 PELYAQAES--FLF--ISSILTYRLTG--VQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTll 222
Cdd:cd07786 145 PGARERAERgeLAFgtIDSWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGY-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 223 pTLAEELGlsADISVLSCGHDTQFAIFGSG--------AGYnqpvlssGTWEILMARTqQAKPewQYVKDGL--TI--EF 290
Cdd:cd07786 223 -TDPDLLG--AEIPIAGIAGDQQAALFGQAcfepgmakNTY-------GTGCFMLMNT-GEKP--VRSKNGLltTIawQL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 291 DSQAGY------FNPG--VQWVSSGImewlgkRFFSDVAGTADYyptmineGSQVPaGSNGLKLVGNFDG------TSQQ 356
Cdd:cd07786 290 GGKVTYalegsiFIAGaaVQWLRDGL------GLIESAAETEAL-------ARSVP-DNGGVYFVPAFTGlgapywDPDA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 357 TGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTV 436
Cdd:cd07786 356 RGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTA 435
|
490 500 510
....*....|....*....|....*....|....
gi 1130437276 437 LGAAMFTLTGAGVFENIEQAQQAMKpAFKRMEPS 470
Cdd:cd07786 436 LGAAYLAGLAVGLWKSLDELAKLWQ-VDRRFEPS 468
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
21-269 |
2.15e-33 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 131.77 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 21 HHGKLLAVHHIANNTQQGEeatDYHIWDIEEIWSKLmtcaKQTLAQLTPEQRQdIVGISVTTFGVDGAIFDKHGKQLYPI 100
Cdd:PRK10640 10 RSLTLREIHRFNNGLHSQD---GFDTWDVDSLESAI----RLGLNKVCEEGIR-IDSIGIDTWGVDYVLLDKQGQRVGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 101 ISWKCPRTQPIMQALGDYLDVEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQAESFLFISSILTYRLTGVQSTDRTMA 180
Cdd:PRK10640 82 VSYRDSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 181 GTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLsadISVLScgHDTQFAIFGSG-AGYNQPV 259
Cdd:PRK10640 162 TTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQGNEIPV---VAVAS--HDTASAVIASPlNDSDAAY 236
|
250
....*....|
gi 1130437276 260 LSSGTWEiLM 269
Cdd:PRK10640 237 LSSGTWS-LM 245
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
6-441 |
2.79e-31 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. 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: 466792 [Multi-domain] Cd Length: 424 Bit Score: 124.68 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 6 IFDCGATNLRIVAMDHHGKLLavHHIANNTQQGEEATDYHIwDIEEIWSKLMTcakqTLAQLTpeQRQDIVGISVTTFGV 85
Cdd:cd07772 4 VFDIGKTNKKLLLFDENGEVL--AERSTPNPEIEEDGYPCE-DVEAIWEWLLD----SLAELA--KRHRIDAINFTTHGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 86 DGAIFDKHGKQLYPIISwkcprtqpIMQALGDYLDvEKLYQRNG--VGHYS-----FNTLFK-LLWLKQHKPELYAQAES 157
Cdd:cd07772 75 TFALLDENGELALPVYD--------YEKPIPDEIN-EAYYAERGpfEETGSpplpgGLNLGKqLYWLKREKPELFARAKT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 158 FLFISSILTYRLTGVQSTDRTMAG--TSMMtNIASDSWDSEVLDvLGLtANHFPPMKSAGEKIGTLLPTLAEELGLSADI 235
Cdd:cd07772 146 ILPLPQYWAWRLTGKAASEITSLGchTDLW-DFEKNEYSSLVKK-EGW-DKLFPPLRKAWEVLGPLRPDLARRTGLPKDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 236 SVLSCGHDTQFAIFGSGAGYNQP--VLSSGTWEILMARTQQAKPEWQYVKDGLTI------------------EFDSQAG 295
Cdd:cd07772 223 PVGCGIHDSNAALLPYLAAGKEPftLLSTGTWCIAMNPGNDLPLTELDLARDCLYnldvfgrpvktarfmggrEYERLVE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 296 YFNpgvqwvSSGIMEWLGKRFFSDVAGTADYYPTMINEGSQVPAGsnGLKLVGNFDGTSQqtgsieglsmhtqrgEIYRA 375
Cdd:cd07772 303 RIA------KSFPQLPSLADLAKLLARGTFALPSFAPGGGPFPGS--GGRGVLSAFPSAE---------------EAYAL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1130437276 376 GLEYMAhrLKAgLEVLQQVGqFNAESIICVGGGSKNGLWNQIRADVL-NRPIDVVDMSETTVLGAAM 441
Cdd:cd07772 360 AILYLA--LMT-DYALDLLG-SGVGRIIVEGGFAKNPVFLRLLAALRpDQPVYLSDDSEGTALGAAL 422
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
51-477 |
1.97e-30 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 123.69 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 51 EIWSKLMTCAKQTLAQLtPEQRQDIVGISVTTFGVDGAIFDKHGKQL--YP---------IISWKCPRTQP-------IM 112
Cdd:COG1069 56 DYLEALEAAVREALAQA-GVDPADVVGIGVDATGCTPVPVDADGTPLalLPefaenphamVILWKDHTAQEeaerineLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 113 QALG-DYLdveklyQRNGvGHYSFNTLF-KLLWLKQHKPELYAQAESFLFISSILTYRLTGVQSTDRTMAGTSMMTNIAS 190
Cdd:COG1069 135 KARGeDYL------RYVG-GIISSEWFWpKILHLLREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAHE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 191 DSWDS-EVLDVLGLTANHFP-----PMKSAGEKIGTLLPTLAEELGLSADISVlscghdtQFAIF-----GSGAGYNQP- 258
Cdd:COG1069 208 GGYPSeEFFAALDPLLDGLAdrlgtEIYPLGEPAGTLTAEWAARLGLPPGTAV-------AVGAIdahagAVGAGGVEPg 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 259 --VLSSGT--WEILMARTQQAKPE-WQYVKDGLTiefdsqAGYF-NPGVQ--------WVSSGIMEWLGKRFFSDVAGtA 324
Cdd:COG1069 281 tlVKVMGTstCHMLVSPEERFVPGiCGQVDGSIV------PGMWgYEAGQsavgdifaWFVRLLVPPLEYEKEAEERG-I 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 325 DYYPTMINEGSQVPAGSNGLkLV-----GN--FDGTSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEvlqqvgQF 397
Cdd:COG1069 354 SLHPLLTEEAAKLPPGESGL-HAldwfnGNrsPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIE------RF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 398 NA-----ESIICVGGGS-KNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRM-EPS 470
Cdd:COG1069 427 EEegvpiDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGFDKVyTPD 506
|
....*...
gi 1130437276 471 GD-VRVYQ 477
Cdd:COG1069 507 PEnVAVYD 514
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
8-472 |
1.35e-29 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 120.94 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHhianntqQGEEATDY-------HiwDIEEIWSKLMTCAKQTLAQ--LTPEqrqDIVGI 78
Cdd:COG0554 9 DQGTTSTRAILFDRDGNIVAVA-------QREFTQIYpqpgwveH--DPEEIWESVLAVIREALAKagISAE---DIAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 79 SVT----TFgvdgAIFDKH-GKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVghySFNTLF---KLLWLKQHKPE 150
Cdd:COG0554 77 GITnqreTT----VVWDRKtGKPLYNAIVWQDRRTADICEELKADGLEDLIREKTGL---VLDPYFsatKIKWILDNVPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 151 LYAQAES--FLF--ISSILTYRLTG--VQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPT 224
Cdd:COG0554 150 ARERAEAgeLLFgtIDSWLIWKLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 225 LaeelgLSADISVLSCGHDTQFAIFGSG---AG-----Y-----------NQPVLSsgtweilmartqqakpewqyvKDG 285
Cdd:COG0554 230 L-----FGAEIPIAGIAGDQQAALFGQAcfePGmakntYgtgcfllmntgDEPVRS---------------------KNG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 286 L--TI--EFDSQAGY------FNPG--VQWVSSGImewlgkRFFSDVAGTADYyptmineGSQVPaGSNGLKLVGNFDG- 352
Cdd:COG0554 284 LltTIawGLGGKVTYalegsiFVAGaaVQWLRDGL------GLIDSAAESEAL-------ARSVE-DNGGVYFVPAFTGl 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 353 -----TSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPID 427
Cdd:COG0554 350 gapywDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVE 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1130437276 428 VVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAfKRMEPSGD 472
Cdd:COG0554 430 RPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVD-RRFEPQMD 473
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
8-473 |
1.35e-28 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 118.26 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHiANNTQQGEEAtDYHIWDIEEIWSKLMTCAKQTLAQLT---------------PEQR 72
Cdd:PLN02295 6 DQGTTSTRFIIYDRDARPVASHQ-VEFTQIYPQA-GWVEHDPMEILESVLTCIAKALEKAAakghnvdsglkaigiTNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 73 QDIVGISVTTfgvdgaifdkhGKQLYPIISWKCPRTQPIMQALGDYLdveklyqRNGVGHY------SFNTLF---KLLW 143
Cdd:PLN02295 84 ETTVAWSKST-----------GRPLYNAIVWMDSRTSSICRRLEKEL-------SGGRKHFvetcglPISTYFsatKLLW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 144 LKQHKPELYAQAES----FLFISSILTYRLTGVQS-----TDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSA 214
Cdd:PLN02295 146 LLENVDAVKEAVKSgdalFGTIDSWLIWNLTGGASggvhvTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 215 GEKIGTLLPTlaeelGLSADISVLSCGHDTQFAIFGSGAGYNQPVLSSGTWEILMART-QQAKPEwqyvKDGL--TIEF- 290
Cdd:PLN02295 226 SEVIGTIAKG-----WPLAGVPIAGCLGDQHAAMLGQRCRPGEAKSTYGTGCFILLNTgEEVVPS----KHGLltTVAYk 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 291 ---DSQAGYFNPGVQWVSSGIMEWLgkRFFSDVAGTADYYPTMineGSQVPAgSNGLKLVGNFDG------TSQQTGSIE 361
Cdd:PLN02295 297 lgpDAPTNYALEGSVAIAGAAVQWL--RDNLGIIKSASEIEAL---AATVDD-TGGVYFVPAFSGlfaprwRDDARGVCV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 362 GLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQ----VGQFNAESIICV-GGGSKNGLWNQIRADVLN----RPIDVvdms 432
Cdd:PLN02295 371 GITRFTNKAHIARAVLESMCFQVKDVLDAMRKdageEKSHKGLFLLRVdGGATANNLLMQIQADLLGspvvRPADI---- 446
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1130437276 433 ETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEPSGDV 473
Cdd:PLN02295 447 ETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPKLDE 487
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
8-472 |
1.25e-27 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 115.31 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHI--ANNTQQG---EEatdyhiwDIEEIWSKLMTCAKQTLAQLTPEQRQ--DIVGISV 80
Cdd:cd07792 7 DQGTTSTRFIVFDSTGELVASHQVehKQIYPKPgwvEH-------DPMEILESVYECIEEAVEKLKALGISpsDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 81 -----TTFgvdgaIFDKH-GKQLYPIISWKCPRTQPImqalgdyldVEKLYQRNGVG--HYS------FNTLF---KLLW 143
Cdd:cd07792 80 tnqreTTV-----VWDKStGKPLYNAIVWLDTRTSDT---------VEELSAKTPGGkdHFRkktglpISTYFsavKLRW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 144 LKQHKPELYAQAES--FLF--ISSILTYRLTG-----VQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSA 214
Cdd:cd07792 146 LLDNVPEVKKAVDDgrLLFgtVDSWLIWNLTGgknggVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 215 GEKIGTLlptlaeELGLSADISVLSCGHDTQFAIFGS------------GAG----YN---QPVLSsgtweilmartqqa 275
Cdd:cd07792 226 SEVYGKI------ASGPLAGVPISGCLGDQQAALVGQgcfkpgeakntyGTGcfllYNtgeEPVFS-------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 276 kpewqyvKDGL--TIEFdsQAGYFNP--------------GVQWvssgIMEWLGkrFFSDVAGTADYyptmineGSQVPa 339
Cdd:cd07792 286 -------KHGLltTVAY--KLGPDAPpvyalegsiaiagaAVQW----LRDNLG--IISSASEVETL-------AASVP- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 340 GSNGLKLVGNFDG------TSQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQ-VGQfnAESIICVGGG-SKN 411
Cdd:cd07792 343 DTGGVYFVPAFSGlfapywRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKdSGI--PLTSLRVDGGmTKN 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1130437276 412 GLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEPSGD 472
Cdd:cd07792 421 NLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQIS 481
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
259-441 |
1.14e-26 |
|
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: 106.64 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 259 VLSSGTWEILMARTQQAKPEwqyvKDGLTIEFDSQAG---YFNPGVQWVSSGIMEWLGKRFFS--DVAGTADYYPTMINE 333
Cdd:pfam02782 2 AISAGTSSFVLVETPEPVLS----VHGVWGPYTNEMLpgyWGLEGGQSAAGSLLAWLLQFHGLreELRDAGNVESLAELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 334 GSQVPAGSNGLKLVGNFDGT------SQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGG 407
Cdd:pfam02782 78 ALAAVAPAGGLLFYPDFSGNrapgadPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190
....*....|....*....|....*....|....
gi 1130437276 408 GSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAM 441
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAAL 191
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
8-442 |
2.08e-26 |
|
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: 111.16 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMD-HHGKLLAVHHIANNTQQGEEATDYHIWDIEEIWSKLMTCakqtLAQLTPEQRQDIVGISVTT--FG 84
Cdd:cd07777 6 DIGTTSIKAALLDlESGRILESVSRPTPAPISSDDPGRSEQDPEKILEAVRNL----IDELPREYLSDVTGIGITGqmHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 85 VdgAIFDKHGKQLYPIISWK---CPRTQPimqaLGDYLDVEKLYQRNGV----GhYSFNTLFkllWLKQHKPeLYAQAES 157
Cdd:cd07777 82 I--VLWDEDGNPVSPLITWQdqrCSEEFL----GGLSTYGEELLPKSGMrlkpG-YGLATLF---WLLRNGP-LPSKADR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 158 FLFISSILTYRLTG--VQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTlaeelgLSADI 235
Cdd:cd07777 151 AGTIGDYIVARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSA------LPKGI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 236 SVL-SCGhDTQFAIFGSGAGY-NQPVLSSGTWEILMARTQ--QAKPEWQ---YVKDG--LTIE-------FDSQAGYFNp 299
Cdd:cd07777 225 PVYvALG-DNQASVLGSGLNEeNDAVLNIGTGAQLSFLTPkfELSGSVEirpFFDGRylLVAAslpggraLAVLVDFLR- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 300 gvqwvssGIMEWLGKRFFSDVAgtadyYPTMINEGSQvpAGSNGLKLVGNFDGT---SQQTGSIEGLSMHTQR-GEIYRA 375
Cdd:cd07777 303 -------EWLRELGGSLSDDEI-----WEKLDELAES--EESSDLSVDPTFFGErhdPEGRGSITNIGESNFTlGNLFRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1130437276 376 GLEYMAHRLKAGLEVLQQvGQFNAESIICVGGGS-KNGLWNQIRADVLNRPIDVVDMSETTVLGAAMF 442
Cdd:cd07777 369 LCRGIAENLHEMLPRLDL-DLSGIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALL 435
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-427 |
3.61e-26 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 110.83 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHhiannTQQGEEATDYHIW---DIEEIWSKLMTCAKqTLAQLTPEQRQDIVGISVTTFG 84
Cdd:PRK15027 6 DLGTSGVKVILLNEQGEVVASQ-----TEKLTVSRPHPLWseqDPEQWWQATDRAMK-ALGDQHSLQDVKALGIAGQMHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 85 vdGAIFDKHGKQLYPIISW---KCPRTQPIMQalgdyldvEKLYQ-RNGVGHYSFN--TLFKLLWLKQHKPELYAQAESF 158
Cdd:PRK15027 80 --ATLLDAQQRVLRPAILWndgRCAQECALLE--------ARVPQsRVITGNLMMPgfTAPKLLWVQRHEPEIFRQIDKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 159 LFISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLPTLAEELGLSAdISVL 238
Cdd:PRK15027 150 LLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 239 SCGHDTQFAIFGSG-AGYNQPVLSSGTWEILMArtqqakpewqyVKDGLTIEFDSQAGYFN---PG------VQWVSSGI 308
Cdd:PRK15027 229 AGGGDNAAGAVGVGmVDANQAMLSLGTSGVYFA-----------VSEGFLSKPESAVHSFChalPQrwhlmsVMLSAASC 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 309 MEWLGKrffsdVAGTADYyPTMINEGSQVPAGSNGLKLVGNFDG------TSQQTGSIEGLSMHTQRGEIYRAGLEYMAH 382
Cdd:PRK15027 298 LDWAAK-----LTGLSNV-PALIAAAQQADESAEPVWFLPYLSGertphnNPQAKGVFFGLTHQHGPNELARAVLEGVGY 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1130437276 383 RLKAGLEVLQQVGqFNAESIICVGGGSKNGLWNQIRADVLNRPID 427
Cdd:PRK15027 372 ALADGMDVVHACG-IKPQSVTLIGGGARSEYWRQMLADISGQQLD 415
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
71-477 |
3.24e-25 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 108.78 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 71 QRQDIVGISVTTFGVDGAIFDKHGKQL------------YPIIsWKCPRTQPimQAlgDYLDV------EKLYQRNGVGH 132
Cdd:PRK04123 76 DPAAVVGIGVDFTGSTPAPVDADGTPLallpefaenphaMVKL-WKDHTAQE--EA--EEINRlahergEADLSRYIGGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 133 YSFNTLF-KLLWLKQHKPELYAQAESFLFISSILTYRLTGVQSTD-----RTMAGTSMMTNiasDSWDS----EVLDVL- 201
Cdd:PRK04123 151 YSSEWFWaKILHVLREDPAVYEAAASWVEACDWVVALLTGTTDPQdivrsRCAAGHKALWH---ESWGGlpsaDFFDALd 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 202 -----GLTANHFPPMKSAGEKIGTLLPTLAEELGLSADISVLSCGHDTQFAIFGSGAGYNQ--PVLSSGTWEILMARTQQ 274
Cdd:PRK04123 228 pllarGLRDKLFTETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGAEPGTlvKVMGTSTCDILLADKQR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 275 AKPEWQYVKDGLTIefdsqAGYFnpGVQWVSSG---IMEWlgkrfFSDVAGTADYYPTMINEGSQV-----------PAG 340
Cdd:PRK04123 308 AVPGICGQVDGSIV-----PGLI--GYEAGQSAvgdIFAW-----FARLLVPPEYKDEAEARGKQLlellteaaakqPPG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 341 SNGLKLVGNFDGT------SQQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEvlqqvgQFNAESI----ICVGGG-- 408
Cdd:PRK04123 376 EHGLVALDWFNGRrtpladQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIME------CFEDQGVpveeVIAAGGia 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1130437276 409 SKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKR-MEPSGD-VRVYQ 477
Cdd:PRK04123 450 RKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASPVEKtYQPDPEnVARYE 520
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
8-469 |
5.30e-25 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 107.71 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEATDYHIWDIEEIWSKLMTCAKQTLaqltpeQRQDIVGISVTTFGVDG 87
Cdd:cd07768 6 DVGTSSARAGVYDLYAGLEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLN------IREGVDAYEVKGCGVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 88 ----AIFDKHGKQL---YP------IISWKCPRTQPIMQALGDYLDvEKLYQRNGVGHYSFNTLFKLLWLKQHKPELYAQ 154
Cdd:cd07768 80 tcslAIFDREGTPLmalIPypnednVIFWMDHSAVNEAQWINMQCP-QQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 155 AESFLFISSILTYRLTGVQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHF------PPMKSAGEKIGTLLPTLAEE 228
Cdd:cd07768 159 HFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEHLtttknlPSNVPIGTTSGVALPEMAEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 229 LGLSADISVLSCGHDTQFAIFGSGaGYNQP---VLSSGTWEILMARTQQAKP---EWQYVKDGLTIEFdsqagYFNPGVQ 302
Cdd:cd07768 239 MGLHPGTAVVVSCIDAHASWFAVA-SPHLEtslFMIAGTSSCHMYGTTISDRipgVWGPFDTIIDPDY-----SVYEAGQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 303 WVSSGIMEWLGK------RFFSDVAGTADYYPTMINEGSQV---PAGSNGLKLVGNFDGTSQQ------TGSIEGLSMHT 367
Cdd:cd07768 313 SATGKLIEHLFEshpcarKFDEALKKGADIYQVLEQTIRQIeknNGLSIHILTLDMFFGNRSEfadprlKGSFIGESLDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 368 QR---GEIYRAGLEYMAHRLKAGLEVLQQVGqFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTL 444
Cdd:cd07768 393 SMlnlTYKYIAILEALAFGTRLIIDTFQNEG-IHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAK 471
|
490 500
....*....|....*....|....*...
gi 1130437276 445 TGAGVF---ENIEQAQQAMKPAFKRMEP 469
Cdd:cd07768 472 VAAGKKqlaDSITEADISNDRKSETFEP 499
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
8-454 |
3.52e-23 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 102.25 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNT---QQGeeatdyhiW---DIEEIWSKLMTCAKQTL--AQLTPEqrqDIVGIS 79
Cdd:cd07793 6 DVGTTNIRCHIFDKKGKIIGSSSEKVEVlypEPG--------WveiDPEELWQQFVKVIKEALknAGLTPE---DIAAIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 80 VTTFGVDGAIFDKH-GKQLYPIISWKCPRTQPIMQALGDYLDVEKLyqrNGVG----------------HYSFNT---LF 139
Cdd:cd07793 75 ISTQRNTFLTWDKKtGKPLHNFITWQDLRAAELCESWNRSLLLKAL---RGGSkflhfltrnkrflaasVLKFSTahvSI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 140 KLLWLKQHKPELYAQAE--SFLF--ISSILTYRLTG--VQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKS 213
Cdd:cd07793 152 RLLWILQNNPELKEAAEkgELLFgtIDTWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 214 AGEKIGTLLPTLaeelgLSADISVLSCGHDTQFAIFGSGA-GYNQPVLSSGT---WEI-----LMARTQQAKP--EWQYv 282
Cdd:cd07793 232 TSGDFGSTDPSI-----FGAEIPITAVVADQQAALFGECCfDKGDVKITMGTgtfIDIntgskPHASVKGLYPlvGWKI- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 283 KDGLT--IEfdsqaGYFNpgvqwvSSG-IMEWLGKR-FFSDVAGTADyyptMInegSQVPAgSNGLKLVGNFDGTS---- 354
Cdd:cd07793 306 GGEITylAE-----GNAS------DTGtVIDWAKSIgLFDDPSETED----IA---ESVED-TNGVYFVPAFSGLQapyn 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 355 --QQTGSIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMS 432
Cdd:cd07793 367 dpTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNT 446
|
490 500
....*....|....*....|..
gi 1130437276 433 ETTVLGAAMFTLTGAGVFENIE 454
Cdd:cd07793 447 EMSALGAAFLAGLASGIWKSKE 468
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
8-472 |
2.15e-20 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 93.74 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHhianntqQGEEATDY-------HiwDIEEIWSKLMTCAKQTL--AQLTPEQrqdIVGI 78
Cdd:PRK00047 11 DQGTTSSRAIIFDHDGNIVSVA-------QKEFTQIFpqpgwveH--DPNEIWASQLSVIAEALakAGISPDQ---IAAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 79 SVT-----TFgvdgaIFDKH-GKQLYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGVghySFNTLF---KLLWLKQHKP 149
Cdd:PRK00047 79 GITnqretTV-----VWDKEtGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGL---VIDPYFsgtKIKWILDNVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 150 ELYAQAES--FLF--ISSILTYRLTG--VQSTDRTMAGTSMMTNIASDSWDSEVLDVLGLTANHFPPMKSAGEKIGTLLP 223
Cdd:PRK00047 151 GARERAEKgeLLFgtIDTWLVWKLTGgkVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 224 T--LAEELGLSADISvlscghDTQFAIFG-----SGAGYNqpvlSSGTWEILMARTQQaKPewQYVKDGL--TI--EFDS 292
Cdd:PRK00047 231 YgfFGGEVPIAGIAG------DQQAALFGqlcfePGMAKN----TYGTGCFMLMNTGE-KA--VKSENGLltTIawGIDG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 293 QAGY------FNPG--VQWVSSGImewlgkRFFSDvAGTADYYPTminegsQVPaGSNGLKLVGNFDG------TSQQTG 358
Cdd:PRK00047 298 KVVYalegsiFVAGsaIQWLRDGL------KIISD-ASDSEALAR------KVE-DNDGVYVVPAFTGlgapywDSDARG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 359 SIEGLSMHTQRGEIYRAGLEYMAHRLKAGLEVLQQVGQFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLG 438
Cdd:PRK00047 364 AIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALG 443
|
490 500 510
....*....|....*....|....*....|....
gi 1130437276 439 AAMFTLTGAGVFENIEQAQQAMKPAfKRMEPSGD 472
Cdd:PRK00047 444 AAYLAGLAVGFWKDLDELKEQWKID-RRFEPQMD 476
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
20-476 |
1.89e-16 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 81.81 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 20 DHHGKLLAVHhiANNTQQGEEATDYHIWDIEEIWSKLMTCAKQTL--AQLTPEQrqdIVGIsvttfGVDG----AIFDKH 93
Cdd:cd07782 18 DLDGRLLATA--SQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLegAGVDPEQ---VKGI-----GFDAtcslVVLDAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 94 GKQL---------YPIISW----------KCPRT-QPIMQALGDYLDVEklyqrngvghysfNTLFKLLWLKQHKPELYA 153
Cdd:cd07782 88 GKPVsvspsgddeRNVILWmdhraveeaeRINATgHEVLKYVGGKISPE-------------MEPPKLLWLKENLPETWA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 154 QAESFLFISSILTYRLTGvqSTDR---TMAG--TSMMTNIASDSWDSEVLDVLGL---TANHFppmksagEKIGT----- 220
Cdd:cd07782 155 KAGHFFDLPDFLTWKATG--SLTRslcSLVCkwTYLAHEGSEGGWDDDFFKEIGLedlVEDNF-------AKIGSvvlpp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 221 -------LLPTLAEELGLSADISVlscghdtqfaifGSG-----AGYnqpvlsSGTweiLMARTQQAKPEWQYVKDGLTI 288
Cdd:cd07782 226 gepvgggLTAEAAKELGLPEGTPV------------GVSlidahAGG------LGT---LGADVGGLPCEADPLTRRLAL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 289 EFD--------SQAGYFNPGV-----------QWVSSG-----------IMEW------LGKRffSDVAGTADYypTMIN 332
Cdd:cd07782 285 ICGtsschmavSPEPVFVPGVwgpyysamlpgLWLNEGgqsatgalldhIIEThpaypeLKEE--AKAAGKSIY--EYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 333 EGSQVPAGSNGLKL-------------VGN----FDGTSqqTGSIEGLSMHTQRGE---IYRAGLEYMAHRLKAGLEVLQ 392
Cdd:cd07782 361 ERLEQLAEEKGLPLayltrdlhvlpdfHGNrsplADPTL--RGMISGLTLDTSLDDlalLYLATLQALAYGTRHIIEAMN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 393 QVGQfNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAMFTLTGAGVFENIEQAQQAMKPAFKRMEPSGD 472
Cdd:cd07782 439 AAGH-KIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEE 517
|
....
gi 1130437276 473 VRVY 476
Cdd:cd07782 518 LKKY 521
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
8-239 |
1.96e-07 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. 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: 466797 [Multi-domain] Cd Length: 544 Bit Score: 53.56 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 8 DCGATNLRIVAMDHHGKLLAVHHIANNTQQGEEATDYHIWDIEEIWSKLMTCAKQTLAQLtPEQRQDIVGISVTT----- 82
Cdd:cd07778 6 DVGSTSVRIGIFDYHGTLLATSERPISYKQDPKDLWFVTQSSTEIWKAIKTALKELIEEL-SDYIVSGIGVSATCsmvvm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 83 --------FGVDGAIFDKHGKQlYPIISWKCPRTQPIMQALGDYLDVEKLYQRNGvghySFN---TLFKLLWLKQHKPEL 151
Cdd:cd07778 85 qrdsdtsyLVPYNVIHEKSNPD-QDIIFWMDHRASEETQWLNNILPDDILDYLGG----GFIpemAIPKLKYLIDLIKED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 152 YAQAESFLFISSILTYRLTGVQSTDRTM-AGTSMMTNIASD----SWDSEVL---------DVLGLTANHFPPMKSAGEK 217
Cdd:cd07778 160 TFKKLEVFDLHDWISYMLATNLGHSNIVpVNAPPSIGIGIDgslkGWSKDFYsklkistkvCNVGNTFKEAPPLPYAGIP 239
|
250 260
....*....|....*....|..
gi 1130437276 218 IGTLLPTLAEELGLSADISVLS 239
Cdd:cd07778 240 IGKVNVILASYLGIDKSTVVGH 261
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
371-478 |
6.45e-06 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; 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. The subfamily includes XKs mainly from eukaryote. 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: 466795 [Multi-domain] Cd Length: 514 Bit Score: 48.71 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130437276 371 EIYRAGLEY--MAHRLKAglevlQQVG-QFNAESIICVGGGSKNGLWNQIRADVLNRPIDVVDMSETTVLGAAM---FTL 444
Cdd:cd07776 400 VEVRAVVESqfLSMRLHA-----ERLGsDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALraaHGL 474
|
90 100 110
....*....|....*....|....*....|....*.
gi 1130437276 445 TGAGVFENIEQAQQAMKPAFKRM-EPS-GDVRVYQS 478
Cdd:cd07776 475 LCAGSGDFSPEFVVFSAEEPKLVaEPDpEAAEVYDK 510
|
|
| |
