|
Name |
Accession |
Description |
Interval |
E-value |
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-304 |
3.17e-117 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 339.56 E-value: 3.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 2 IYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFL 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 82 KVKEPTRINVFTRVLDQNvEYKEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIK 161
Cdd:TIGR03828 81 RVPGETRINVKIKEPSGT-ETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 162 LVIDSSSKVVLDTLQYQPYLLKPNDQELASFFDLNEKlDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA 241
Cdd:TIGR03828 160 VILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELK-TLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743904 242 PKIQALNTAGAGDTMLGTFIGEKSKAKSDTAALKSAIAAASDTASRSG--LTDF-KLEKYLKEIQV 304
Cdd:TIGR03828 239 PKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGtgLPDPeDIEELLPQVTI 304
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-291 |
1.87e-108 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 316.78 E-value: 1.87e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 1 MIYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 81 LKVKEPTRINVFTRVLDqNVEYKEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDI 160
Cdd:cd01164 81 VEVAGETRINVKIKEED-GTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 161 KLVIDSSSKVVLDTLQYQPYLLKPNDQELASFFDLnEKLDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGN 240
Cdd:cd01164 160 RVILDTSGEALLAALAAKPFLIKPNREELEELFGR-PLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489743904 241 APKIQALNTAGAGDTMLGTFIGEKSKAKSDTAALKSAIAAASDTASRSGLT 291
Cdd:cd01164 239 PPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-261 |
4.59e-99 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 293.58 E-value: 4.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 2 IYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFL 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 82 KVKEPTRINVFTRVLDQNVEYKEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIK 161
Cdd:COG1105 81 PIEGETRINIKIVDPSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 162 LVIDSSSKVVLDTLQYQPYLLKPNDQELASFFDLNEKlDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA 241
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLE-TLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKP 239
|
250 260
....*....|....*....|
gi 489743904 242 PKIQALNTAGAGDTMLGTFI 261
Cdd:COG1105 240 PKVEVVSTVGAGDSMVAGFL 259
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
4-261 |
1.31e-41 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 146.38 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 4 TITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFLKV 83
Cdd:PRK09513 7 TITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 84 KEPTRINVftRVLDQNVEYKEVN-PGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIKL 162
Cdd:PRK09513 87 QGRTRINV--KLTEKDGEVTDFNfSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQCPCI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 163 VIDSSSKVVLDTLQYQPYLLKPNDQELASFfdLNEKL-DQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA 241
Cdd:PRK09513 165 IFDSSREALVAGLKAAPWLVKPNRRELEIW--AGRKLpELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKP 242
|
250 260
....*....|....*....|
gi 489743904 242 PKIQALNTAGAGDTMLGTFI 261
Cdd:PRK09513 243 PACDVVSTVGAGDSMVGGLI 262
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
11-261 |
3.03e-35 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 129.00 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 11 IDLVIITKKLEANTVnRTENFELQPNGKGVNVSFILKKMGIKNMATG-IGGGFTLDYITAGLEEKGIKTKFLKVKEPTRI 89
Cdd:pfam00294 10 IDLIGNVEGLPGELV-RVSTVEKGPGGKGANVAVALARLGGDVAFIGaVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 90 NVFTRVLDQNVEYkEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKIT-AEKDIKLVIDSSS 168
Cdd:pfam00294 89 GTALIEVDGDGER-TIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAkNGGTFDPNLLDPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 169 ---KVVLDTLQYQPYLLKPNDQELASFFDLNEKlDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA-PKI 244
Cdd:pfam00294 168 gaaREALLELLPLADLLKPNEEELEALTGAKLD-DIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAvPKV 246
|
250
....*....|....*..
gi 489743904 245 QALNTAGAGDTMLGTFI 261
Cdd:pfam00294 247 KVVDTTGAGDSFVGGFL 263
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-304 |
3.17e-117 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 339.56 E-value: 3.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 2 IYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFL 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 82 KVKEPTRINVFTRVLDQNvEYKEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIK 161
Cdd:TIGR03828 81 RVPGETRINVKIKEPSGT-ETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 162 LVIDSSSKVVLDTLQYQPYLLKPNDQELASFFDLNEKlDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA 241
Cdd:TIGR03828 160 VILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELK-TLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743904 242 PKIQALNTAGAGDTMLGTFIGEKSKAKSDTAALKSAIAAASDTASRSG--LTDF-KLEKYLKEIQV 304
Cdd:TIGR03828 239 PKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGtgLPDPeDIEELLPQVTI 304
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-303 |
9.03e-115 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 333.39 E-value: 9.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 2 IYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFL 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 82 KVKEPTRINVFTrVLDQNVEYKEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIK 161
Cdd:TIGR03168 81 EVKGETRINVKI-KESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 162 LVIDSSSKVVLDTLQYQPYLLKPNDQELASFFDLnEKLDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA 241
Cdd:TIGR03168 160 VILDTSGEALREALAAKPFLIKPNHEELEELFGR-ELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489743904 242 PKIQALNTAGAGDTMLGTFIGEKSKAKSDTAALKSAIAAASDTASRSGLTDF---KLEKYLKEIQ 303
Cdd:TIGR03168 239 PKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPdpeDVEELLDQVT 303
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-291 |
1.87e-108 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 316.78 E-value: 1.87e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 1 MIYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 81 LKVKEPTRINVFTRVLDqNVEYKEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDI 160
Cdd:cd01164 81 VEVAGETRINVKIKEED-GTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 161 KLVIDSSSKVVLDTLQYQPYLLKPNDQELASFFDLnEKLDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGN 240
Cdd:cd01164 160 RVILDTSGEALLAALAAKPFLIKPNREELEELFGR-PLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489743904 241 APKIQALNTAGAGDTMLGTFIGEKSKAKSDTAALKSAIAAASDTASRSGLT 291
Cdd:cd01164 239 PPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-261 |
4.59e-99 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 293.58 E-value: 4.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 2 IYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFL 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 82 KVKEPTRINVFTRVLDQNVEYKEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIK 161
Cdd:COG1105 81 PIEGETRINIKIVDPSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 162 LVIDSSSKVVLDTLQYQPYLLKPNDQELASFFDLNEKlDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA 241
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLE-TLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKP 239
|
250 260
....*....|....*....|
gi 489743904 242 PKIQALNTAGAGDTMLGTFI 261
Cdd:COG1105 240 PKVEVVSTVGAGDSMVAGFL 259
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
4-261 |
1.31e-41 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 146.38 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 4 TITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFLKV 83
Cdd:PRK09513 7 TITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 84 KEPTRINVftRVLDQNVEYKEVN-PGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIKL 162
Cdd:PRK09513 87 QGRTRINV--KLTEKDGEVTDFNfSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQCPCI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 163 VIDSSSKVVLDTLQYQPYLLKPNDQELASFfdLNEKL-DQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA 241
Cdd:PRK09513 165 IFDSSREALVAGLKAAPWLVKPNRRELEIW--AGRKLpELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKP 242
|
250 260
....*....|....*....|
gi 489743904 242 PKIQALNTAGAGDTMLGTFI 261
Cdd:PRK09513 243 PACDVVSTVGAGDSMVGGLI 262
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-255 |
1.03e-39 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 141.01 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 1 MIYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKgIKTKF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLDDQ-IKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 81 LKVKEPTRINVFTRVLDQNVEYKEvnPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDI 160
Cdd:PRK13508 80 YKIKGETRNCIAILHEGQQTEILE--KGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 161 KLVIDSSSKVVLDTL--QYQPYLLKPNDQELASFFDLNEKLDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYF 238
Cdd:PRK13508 158 PVVLDCSGAALQAVLesPYKPTVIKPNIEELSQLLGKEVSEDLDELKEVLQQPLFEGIEWIIVSLGADGAFAKHNDTFYK 237
|
250
....*....|....*..
gi 489743904 239 GNAPKIQALNTAGAGDT 255
Cdd:PRK13508 238 VDIPKIEVVNPVGSGDS 254
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
11-261 |
3.03e-35 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 129.00 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 11 IDLVIITKKLEANTVnRTENFELQPNGKGVNVSFILKKMGIKNMATG-IGGGFTLDYITAGLEEKGIKTKFLKVKEPTRI 89
Cdd:pfam00294 10 IDLIGNVEGLPGELV-RVSTVEKGPGGKGANVAVALARLGGDVAFIGaVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 90 NVFTRVLDQNVEYkEVNPGPEVGPEVQDKFLKYLKDTLKADDTLIISGSFSKGIKAEYLVEIAKIT-AEKDIKLVIDSSS 168
Cdd:pfam00294 89 GTALIEVDGDGER-TIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAkNGGTFDPNLLDPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 169 ---KVVLDTLQYQPYLLKPNDQELASFFDLNEKlDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA-PKI 244
Cdd:pfam00294 168 gaaREALLELLPLADLLKPNEEELEALTGAKLD-DIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAvPKV 246
|
250
....*....|....*..
gi 489743904 245 QALNTAGAGDTMLGTFI 261
Cdd:pfam00294 247 KVVDTTGAGDSFVGGFL 263
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-258 |
3.79e-30 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 115.65 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 2 IYTITLNPAIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGIGGGFTLDYITAGLEEKGIKTKFL 81
Cdd:PRK10294 4 IYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 82 KVKEPTRINVFTRVLDQNVEYKEVNPGPEVGPEVQDKFLKYLkDTLKADDTLIISGSFSKGIKAEYLVEIAKITAEKDIK 161
Cdd:PRK10294 84 EAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQV-LEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 162 LVIDSSSKVVLDTL-QYQPYLLKPNDQELASFfdLNEKLDQ-EKIIELARKLISAG-CQNVLVSLGENGAALINKDHAYF 238
Cdd:PRK10294 163 CIIDSSGDALSAALaIGNIELVKPNQKELSAL--VNRDLTQpDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQ 240
|
250 260
....*....|....*....|
gi 489743904 239 GNAPKIQALNTAGAGDTMLG 258
Cdd:PRK10294 241 VVPPPVKSQSTVGAGDSMVG 260
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
10-261 |
2.85e-19 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 86.09 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 10 AIDLVIITKKL-EANTVNRTENFELQPNGKGVNVSFILKKMGIK-NMATGIGGGFTLDYITAGLEEKGIKTKFLKVKE-- 85
Cdd:COG0524 9 LVDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGARvALVGAVGDDPFGDFLLAELRAEGVDTSGVRRDPga 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 86 PT------------RINVFTRVLDQNVEYKEVNPgpevgpevqdkflkylkDTLKADDTLIISG-SFSKGIKAEYLVEIA 152
Cdd:COG0524 89 PTglafilvdpdgeRTIVFYRGANAELTPEDLDE-----------------ALLAGADILHLGGiTLASEPPREALLAAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 153 KITAEKDIKLVIDSSSKVVLDTlQYQPYL---------LKPNDQELASFFDLNEkldqekIIELARKLISAGCQNVLVSL 223
Cdd:COG0524 152 EAARAAGVPVSLDPNYRPALWE-PARELLrellalvdiLFPNEEEAELLTGETD------PEEAAAALLARGVKLVVVTL 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 489743904 224 GENGAALINKDHAYFGNAPKIQALNTAGAGDTMLGTFI 261
Cdd:COG0524 225 GAEGALLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFL 262
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
71-260 |
2.80e-13 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 68.74 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 71 LEEKGIKTKFLKVKE-PTriNVFTRVLDQN-----VEYKEVNPGPEvgpEVQDKFLKYLKDTLKADDTLIISgSFSKGIK 144
Cdd:cd01172 75 LEKEGIDTDGIVDEGrPT--TTKTRVIARNqqllrVDREDDSPLSA---EEEQRLIERIAERLPEADVVILS-DYGKGVL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 145 AEYLV-EIAKITAEKDIKLVIDSSSKvvlDTLQYQ-PYLLKPNDQELASFFDlNEKLDQEKIIELARKLIS-AGCQNVLV 221
Cdd:cd01172 149 TPRVIeALIAAARELGIPVLVDPKGR---DYSKYRgATLLTPNEKEAREALG-DEINDDDELEAAGEKLLElLNLEALLV 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489743904 222 SLGENGAALINKDHAYFgNAPKI--QALNTAGAGDTMLGTF 260
Cdd:cd01172 225 TLGEEGMTLFERDGEVQ-HIPALakEVYDVTGAGDTVIATL 264
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
131-262 |
6.24e-11 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 60.57 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 131 DTLIISGSFSKGikaEYLVEIAKITAEKDIKLVIDSSSKVVLDTLQY------QPYLLKPNDQELASFFDLNEkLDQEKI 204
Cdd:cd00287 59 DAVVISGLSPAP---EAVLDALEEARRRGVPVVLDPGPRAVRLDGEElekllpGVDILTPNEEEAEALTGRRD-LEVKEA 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489743904 205 IELARKLISAGCQNVLVSLGENGAALINKDHAYF-GNAPKIQALNTAGAGDTMLGTFIG 262
Cdd:cd00287 135 AEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVhVPAFPVKVVDTTGAGDAFLAALAA 193
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
35-261 |
2.27e-10 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 60.06 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 35 PNGKGVNVSFILKKMGIKNMATG-IGGGFTLDYITAGLEEKGIKTKFLKVKEptRINVFTRVL--DQNVEYKEVNPGPEV 111
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGaVGNDDAGAHVRSTLKRLGVDISHCRVKE--GENAVADVElvDGDRIFGLSNKGGVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 112 GPEVQDKFLKYLKdtlKADdtLIISGSFSKGikaEYLVEIAKITAEKDIKLVIDSSSKVVLDTLQYQ-PYLlkpndqELA 190
Cdd:cd01940 99 REHPFEADLEYLS---QFD--LVHTGIYSHE---GHLEKALQALVGAGALISFDFSDRWDDDYLQLVcPYV------DFA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489743904 191 sFFDLNEkLDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNAPKIQALNTAGAGDTMLGTFI 261
Cdd:cd01940 165 -FFSASD-LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFL 233
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
181-260 |
2.91e-09 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 56.79 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 181 LLKPNDQELASFFDLnEKLDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNAPKIQALNTAGAGDTMLGTF 260
Cdd:cd01174 178 ILVPNETEAALLTGI-EVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGAL 256
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
118-261 |
6.35e-07 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 50.00 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 118 KFLKYLKDTLKADDTLIISGSFSKgikaEYLVEIAKITAEKDIKLVIDSSSKVVLDTLQY---QPYLLKPNDQELASFFD 194
Cdd:cd01941 117 DFLRKIREALKEAKPIVVDANLPE----EALEYLLALAAKHGVPVAFEPTSAPKLKKLFYllhAIDLLTPNRAELEALAG 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489743904 195 LNEKLDQEKIIELARKLISaGCQNVLVSLGENGAALINKDHA-YFGNAPKIQ---ALNTAGAGDTMLGTFI 261
Cdd:cd01941 193 ALIENNEDENKAAKILLLP-GIKNVIVTLGAKGVLLSSREGGvETKLFPAPQpetVVNVTGAGDAFVAGLV 262
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
160-261 |
4.38e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 47.01 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 160 IKLVIDSSSKVVLDTlqyQPYLLKPNDQELASFFDLNE----KLDQEKII------ELARKLISAGCQNVLVSLGENGAA 229
Cdd:cd01937 121 SPSLFRKFAFISLDA---QGFLRRANQEKLIKCVILKLhdvlKLSRVEAEvistptELARLIKETGVKEIIVTDGEEGGY 197
|
90 100 110
....*....|....*....|....*....|..
gi 489743904 230 LINKDHAYFGNAPKIQALNTAGAGDTMLGTFI 261
Cdd:cd01937 198 IFDGNGKYTIPASKKDVVDPTGAGDVFLAAFL 229
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
124-262 |
6.97e-05 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 43.61 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 124 KDTLKADdtLIISGSFSKGIKAEY----LVEIAKITAEKDIKLV--IDSSSKVVLDTLQY----QPYLLKPNDQeLASFF 193
Cdd:cd01946 91 ADTLDTD--LNVFADFDPQLPEHYkdseFVFLGNIAPELQREVLeqVKDPKLVVMDTMNFwisiKPEKLKKVLA-KVDVV 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489743904 194 DLNEK-----LDQEKIIELARKLISAGCQNVLVSLGENGAALINKDHAYFGNA-PKIQALNTAGAGDTMLGTFIG 262
Cdd:cd01946 168 IINDGearqlTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAyPLESVFDPTGAGDTFAGGFIG 242
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
27-260 |
8.71e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 40.49 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 27 RTENFELQPNGKGVNVSFILKKMGIK-NMATGIGG-GFTLDYItAGLEEKGIKTKFLKVKEPTRINVFTRVLDQNVEYKE 104
Cdd:PTZ00292 43 HGTSFHKGFGGKGANQAVMASKLGAKvAMVGMVGTdGFGSDTI-KNFKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 105 VNPGPEVGPEVQDKFLKYLKDTLKADDTLIISgsfSKGIKAEYLVEIAKITAEKDIKLVIDSS-------SKVVLDTLQY 177
Cdd:PTZ00292 122 IVIIPGANNALTPQMVDAQTDNIQNICKYLIC---QNEIPLETTLDALKEAKERGCYTVFNPApapklaeVEIIKPFLKY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 178 qPYLLKPNDQELASFFDLnEKLDQEKIIELARKLISAGCQNVLVSLGENGAALINKdhayfGNAP------KIQALNTAG 251
Cdd:PTZ00292 199 -VSLFCVNEVEAALITGM-EVTDTESAFKASKELQQLGVENVIITLGANGCLIVEK-----ENEPvhvpgkRVKAVDTTG 271
|
....*....
gi 489743904 252 AGDTMLGTF 260
Cdd:PTZ00292 272 AGDCFVGSM 280
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
10-269 |
5.27e-03 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 37.79 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 10 AIDLVIITKKLEANTVNRTENFELQPNGKGVNVSFILKKMGIKNMATGI-GGGFTLDYITAGLEEKGIKTKFlkvkePTR 88
Cdd:cd01944 9 VVDIVLDVDKLPASGGDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPlGNGNWADQIRQAMRDEGIEILL-----PPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 89 INVFTRVLDQNVEykevnPGPE------VGPEVQDKFLKYLKDTLKADDTLIISG------SFSKGIKAEYLVEIAKITA 156
Cdd:cd01944 84 GGDDGGCLVALVE-----PDGErsfisiSGAEQDWSTEWFATLTVAPYDYVYLSGytlaseNASKVILLEWLEALPAGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743904 157 ekdikLVIDSS------SKVVLDTLQYQPYLLKPNDQELASFfdlNEKLDQEkiIELARKLISAGCQN-VLVSLGENGAA 229
Cdd:cd01944 159 -----LVFDPGprisdiPDTILQALMAKRPIWSCNREEAAIF---AERGDPA--AEASALRIYAKTAApVVVRLGSNGAW 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489743904 230 LINKDhayfGN-----APKIQALNTAGAGDTMLGTFIGEKSKAKS 269
Cdd:cd01944 229 IRLPD----GNthiipGFKVKAVDTIGAGDTHAGGMLAGLAKGMS 269
|
|
| |
