|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
2-212 |
3.52e-101 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 294.92 E-value: 3.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGDMNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTS 81
Cdd:PRK09434 4 KVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 82 TVVVDLATSGERSFSFLVNPSADQFLTSRDLPVFGK-DILHYCSLALAAENCREAVVQATSKVKAREGWVSFDLNLREQM 160
Cdd:PRK09434 84 TVVVDLDDQGERSFTFMVRPSADLFLQPQDLPPFRQgEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1403722873 161 WSDKAEMRRVIEQQCRSADILKLSDEELLWMTeeETSDWEEAL-ALLERYPAR 212
Cdd:PRK09434 164 WQDEAELRECLRQALALADVVKLSEEELCFLS--GTSQLEDAIyALADRYPIA 214
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
2-212 |
4.01e-68 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 210.57 E-value: 4.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGD---MNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETY 78
Cdd:cd01167 1 KVVCFGEALIDFIPEGSgapETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 79 RTSTVVVDLATSGERSFSFLVNPSADQFLTSRDLPVFGK--DILHYCSLALAAENCREAVVQATSKVKAREGWVSFDLNL 156
Cdd:cd01167 81 PTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLSeaDILHFGSIALASEPSRSALLELLEAAKKAGVLISFDPNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1403722873 157 REQMWSDKAEMRRVIEQQCRSADILKLSDEELLWMTEEEtsDWEEALALLERYPAR 212
Cdd:cd01167 161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEE--DPEEIAALLLLFGLK 214
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-212 |
2.85e-51 |
|
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: 167.37 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDL------LPAGDM-----NYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAE 70
Cdd:COG0524 1 DVLVIGEALVDLvarvdrLPKGGEtvlagSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 71 FMLTDETYRTSTVVVDLATSGERSFSFlvNPSADQFLTSRDLP---VFGKDILHYCSLALAAENCREAVVQATSKVKARE 147
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVF--YRGANAELTPEDLDealLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403722873 148 GWVSFDLNLREQMWsdkAEMRRVIEQQCRSADILKLSDEELLWMTEEEtsDWEEALA-LLERYPAR 212
Cdd:COG0524 159 VPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGET--DPEEAAAaLLARGVKL 219
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
2-207 |
1.35e-33 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 121.68 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGD---------MNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFM 72
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEglpgelvrvSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 73 LTDETYRTSTVVVDLATSGERSFSFLVNPSADQFLT--SRDLPVFGK-DILHYCSLALAaeNCREAVVQATSKVKAREGw 149
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEelEENEDLLENaDLLYISGSLPL--GLPEATLEELIEAAKNGG- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1403722873 150 vSFDLNLREQMWSDKAEMRRVIEQqcrsADILKLSDEELLWMTEEETSDWEEALALLE 207
Cdd:pfam00294 158 -TFDPNLLDPLGAAREALLELLPL----ADLLKPNEEELEALTGAKLDDIEEALAALH 210
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
22-88 |
9.55e-04 |
|
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: 39.10 E-value: 9.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403722873 22 QACAGGAPLNVAVGVARLAGDSAFIGRVGNDPfGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVDLA 88
Cdd:TIGR03168 31 RKDAGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKESS 96
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
2-212 |
3.52e-101 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 294.92 E-value: 3.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGDMNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTS 81
Cdd:PRK09434 4 KVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 82 TVVVDLATSGERSFSFLVNPSADQFLTSRDLPVFGK-DILHYCSLALAAENCREAVVQATSKVKAREGWVSFDLNLREQM 160
Cdd:PRK09434 84 TVVVDLDDQGERSFTFMVRPSADLFLQPQDLPPFRQgEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1403722873 161 WSDKAEMRRVIEQQCRSADILKLSDEELLWMTeeETSDWEEAL-ALLERYPAR 212
Cdd:PRK09434 164 WQDEAELRECLRQALALADVVKLSEEELCFLS--GTSQLEDAIyALADRYPIA 214
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
2-212 |
4.01e-68 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 210.57 E-value: 4.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGD---MNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETY 78
Cdd:cd01167 1 KVVCFGEALIDFIPEGSgapETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 79 RTSTVVVDLATSGERSFSFLVNPSADQFLTSRDLPVFGK--DILHYCSLALAAENCREAVVQATSKVKAREGWVSFDLNL 156
Cdd:cd01167 81 PTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLSeaDILHFGSIALASEPSRSALLELLEAAKKAGVLISFDPNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1403722873 157 REQMWSDKAEMRRVIEQQCRSADILKLSDEELLWMTEEEtsDWEEALALLERYPAR 212
Cdd:cd01167 161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEE--DPEEIAALLLLFGLK 214
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-212 |
2.85e-51 |
|
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: 167.37 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDL------LPAGDM-----NYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAE 70
Cdd:COG0524 1 DVLVIGEALVDLvarvdrLPKGGEtvlagSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 71 FMLTDETYRTSTVVVDLATSGERSFSFlvNPSADQFLTSRDLP---VFGKDILHYCSLALAAENCREAVVQATSKVKARE 147
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVF--YRGANAELTPEDLDealLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403722873 148 GWVSFDLNLREQMWsdkAEMRRVIEQQCRSADILKLSDEELLWMTEEEtsDWEEALA-LLERYPAR 212
Cdd:COG0524 159 VPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGET--DPEEAAAaLLARGVKL 219
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
26-205 |
2.65e-43 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 147.85 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 26 GGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVDLATSGERSFSFLVNPSADQ 105
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSADM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 106 FLTSRDLP---VFGKDILHYCSLALAAENCREAVVQATSKVKAREGWVSFDLNLREQMWSDKAEMRRVIEQQCRSADILK 182
Cdd:PLN02323 123 LLRESELDldlIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIK 202
|
170 180
....*....|....*....|...
gi 1403722873 183 LSDEELLWMTEEETSDWEEALAL 205
Cdd:PLN02323 203 VSDEEVEFLTGGDDPDDDTVVKL 225
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
2-211 |
3.68e-41 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 141.17 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGD------MNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTD 75
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGgrleqaDSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 76 ETYRTSTVVVDLATSGERSFSFLVNPSADQFLTSRDLPVF---GKDILHYCSLALAA-ENCREAVVQATSKVKAREGWVS 151
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAalaGADHLHLSGITLALsESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403722873 152 FDLNLREQMWSdKAEMRRVIEQQCRSADILKLSDEE--LLWMTEEETSDWEEALALLERYPA 211
Cdd:cd01166 161 FDLNYRPKLWS-AEEAREALEELLPYVDIVLPSEEEaeALLGDEDPTDAAERALALALGVKA 221
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
2-207 |
1.35e-33 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 121.68 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGD---------MNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFM 72
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEglpgelvrvSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 73 LTDETYRTSTVVVDLATSGERSFSFLVNPSADQFLT--SRDLPVFGK-DILHYCSLALAaeNCREAVVQATSKVKAREGw 149
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEelEENEDLLENaDLLYISGSLPL--GLPEATLEELIEAAKNGG- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1403722873 150 vSFDLNLREQMWSDKAEMRRVIEQqcrsADILKLSDEELLWMTEEETSDWEEALALLE 207
Cdd:pfam00294 158 -TFDPNLLDPLGAAREALLELLPL----ADLLKPNEEELEALTGAKLDDIEEALAALH 210
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
26-195 |
8.16e-19 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 83.80 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 26 GGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTST--VVVDLATSGERSFSFLVNPSA 103
Cdd:PLN02543 172 GGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACsrMKIKFRDGGKMVAETVKEAAE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 104 DQFLTSR-DLPVFGK-DILHYCSLALAAENCREAVVQATSKVKAREGWVSFDLNLREQMWSDKAEMRRVIEQQCRSADIL 181
Cdd:PLN02543 252 DSLLASElNLAVLKEaRMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEADII 331
|
170
....*....|....
gi 1403722873 182 KLSDEELLWMTEEE 195
Cdd:PLN02543 332 EVSRQELEFLLDED 345
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
2-119 |
6.39e-15 |
|
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: 71.43 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDL------LP------AGDmNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGA 69
Cdd:cd01174 1 KVVVVGSINVDLvtrvdrLPkpgetvLGS-SFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1403722873 70 EFMLTDETYRTSTVVVDLATSGERsfSFLVNPSADQFLTSRDLPVFGKDI 119
Cdd:cd01174 80 SYVEVVVGAPTGTAVITVDESGEN--RIVVVPGANGELTPADVDAALELI 127
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
26-209 |
8.45e-14 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 68.11 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 26 GGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVdlATSGERSFSFLVNPSADQ 105
Cdd:cd01942 36 GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFI--LTDGDDNQIAYFYPGAMD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 106 FLT-SRDLPVFGK-DILHycslaLAAEncrEAVVQATSKVKAREGWVSFDLNlreQMWS--DKAEMRRVIEQqcrsADIL 181
Cdd:cd01942 114 ELEpNDEADPDGLaDIVH-----LSSG---PGLIELARELAAGGITVSFDPG---QELPrlSGEELEEILER----ADIL 178
|
170 180
....*....|....*....|....*...
gi 1403722873 182 KLSDEELLwMTEEETSDWEEALALLERY 209
Cdd:cd01942 179 FVNDYEAE-LLKERTGLSEAELASGVRV 205
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
2-172 |
1.56e-12 |
|
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: 64.68 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDLLPAGDMNYqacAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMltdETYRTS 81
Cdd:cd01940 1 RLAAIGDNVVDKYLHLGKMY---PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC---RVKEGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 82 TVVVDLATS-GERSFSFL-VNPSADQFLTSRDLPVFGK-DILH---YCSLALAAENCREAVVQATSkvkaregwVSFDLN 155
Cdd:cd01940 75 NAVADVELVdGDRIFGLSnKGGVAREHPFEADLEYLSQfDLVHtgiYSHEGHLEKALQALVGAGAL--------ISFDFS 146
|
170
....*....|....*..
gi 1403722873 156 LReqmWSDKaEMRRVIE 172
Cdd:cd01940 147 DR---WDDD-YLQLVCP 159
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-210 |
1.66e-12 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 64.94 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 1 MKIWALGDAVVDL-------------LPAGDM---------------NYQACAGGAPLNVAVGVARLAGDSAFIGRVGND 52
Cdd:cd01168 2 YDVLGLGNALVDIlaqvddafleklgLKKGDMiladmeeqeellaklPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 53 PFGRFLKRTLEEQGVGAEFMlTDETYRTSTVVVDLATSGERSFSFLVNPSADqfltsrdlpvFGKDILHYCSLALAA--- 129
Cdd:cd01168 82 KLGDFLLKDLRAAGVDTRYQ-VQPDGPTGTCAVLVTPDAERTMCTYLGAANE----------LSPDDLDWSLLAKAKyly 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 130 ------ENCREAVVQATskVKAREGWVSFDLNLreqmwSD-------KAEMRRVIEQqcrsADILKLSDEELLWMTE-EE 195
Cdd:cd01168 151 legyllTVPPEAILLAA--EHAKENGVKIALNL-----SApfivqrfKEALLELLPY----VDILFGNEEEAEALAEaET 219
|
250
....*....|....*
gi 1403722873 196 TSDWEEALALLERYP 210
Cdd:cd01168 220 TDDLEAALKLLALRC 234
|
|
| PLN02967 |
PLN02967 |
kinase |
26-188 |
2.42e-12 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 65.07 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 26 GGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVDLATSGERSFSFLVNPSADQ 105
Cdd:PLN02967 243 GGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVKPCAEDS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 106 FLTSRDLPVFGKD--ILHYCSLALAAENCREAVVQATSKVKAREGWVSFDLNLREQMWSDKAEMRRVIEQQCRSADILKL 183
Cdd:PLN02967 323 LSKSEINIDVLKEakMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNLADIIEV 402
|
....*
gi 1403722873 184 SDEEL 188
Cdd:PLN02967 403 TKQEL 407
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
1-95 |
4.09e-10 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 57.83 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 1 MKIWALGDAVVDLLPAGDMNYqacAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETyRT 80
Cdd:PRK09813 1 KKLATIGDNCVDIYPQLGKAF---SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG-VT 76
|
90
....*....|....*
gi 1403722873 81 STVVVDLaTSGERSF 95
Cdd:PRK09813 77 AQTQVEL-HDNDRVF 90
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-146 |
1.66e-09 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 56.15 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 9 AVVDLLPAGD-----MNYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTSTV 83
Cdd:cd01945 14 YLVASFPGGDgkivaTDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPIS 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403722873 84 VVDLATSGERSFSFlvNPSADQFltsrDLPVFGKDILHYCSLALAAENCREAVVQATSKVKAR 146
Cdd:cd01945 94 SITDITGDRATISI--TAIDTQA----APDSLPDAILGGADAVLVDGRQPEAALHLAQEARAR 150
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
25-82 |
5.80e-09 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 54.82 E-value: 5.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1403722873 25 AGGApLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTST 82
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTT 111
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
26-86 |
2.06e-07 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 50.66 E-value: 2.06e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403722873 26 GGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVgaefmltdetyRTSTVVVD 86
Cdd:COG3892 38 GGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGV-----------DTSGVVTD 87
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
26-127 |
2.82e-07 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 49.74 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 26 GGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRT--STVVVDLATSGErsfSFLVNPSA 103
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTglAMIFVDTKTGNN---EIVIIPGA 128
|
90 100
....*....|....*....|....
gi 1403722873 104 DQFLTSRDLPVFGKDILHYCSLAL 127
Cdd:PTZ00292 129 NNALTPQMVDAQTDNIQNICKYLI 152
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
16-94 |
5.43e-07 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 48.94 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 16 AGDMNYQACAGGAPLN---VAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMlTDETYRTSTVVVdLATSGE 92
Cdd:PLN02548 42 ASKYNVEYIAGGATQNsirVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVNVHYY-EDESTPTGTCAV-LVVGGE 119
|
..
gi 1403722873 93 RS 94
Cdd:PLN02548 120 RS 121
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
25-82 |
1.29e-06 |
|
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: 47.94 E-value: 1.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1403722873 25 AGGApLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFmLTDETYRTST 82
Cdd:cd01172 39 LGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDG-IVDEGRPTTT 94
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
20-94 |
1.80e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 44.48 E-value: 1.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403722873 20 NYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVDLATSGERS 94
Cdd:PRK11142 33 HYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENS 107
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
25-71 |
2.14e-05 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 44.43 E-value: 2.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1403722873 25 AGGAPlNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEF 71
Cdd:PRK11316 50 PGGAA-NVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDF 95
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
20-187 |
9.41e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 42.49 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 20 NYQACAGGAPLNVAVGVARLAGDS--------AFIGRVGNDPFGRFLKRTLEEQGVgaEFM---LTDETyrTSTVVVDLA 88
Cdd:PLN02813 120 SYKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANV--HFLsqpVKDGT--TGTVIVLTT 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 89 TSGERSF------SFLVNPS---ADQFLTSRDLPVFGK--DILHycSLALAAENCREAvVQATSKVKAREGWVSFDLNLR 157
Cdd:PLN02813 196 PDAQRTMlsyqgtSSTVNYDsclASAISKSRVLVVEGYlwELPQ--TIEAIAQACEEA-HRAGALVAVTASDVSCIERHR 272
|
170 180 190
....*....|....*....|....*....|
gi 1403722873 158 EQMWsdkaemrRVIeqqCRSADILKLSDEE 187
Cdd:PLN02813 273 DDFW-------DVM---GNYADILFANSDE 292
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
25-92 |
1.73e-04 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 41.27 E-value: 1.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403722873 25 AGGAPLNVAVGVARLAGDS---AFIGRvgndPFGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVDLATSGE 92
Cdd:COG1105 34 PGGKGINVARVLKALGVDVtalGFLGG----FTGEFIEELLDEEGIPTDFVPIEGETRINIKIVDPSDGTE 100
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
25-94 |
5.37e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 40.01 E-value: 5.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403722873 25 AGGAPLNVAvgvaRLA--------GDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDEtYRTSTVVVdLATSGERS 94
Cdd:PTZ00247 61 PGGSALNTA----RVAqwmlqapkGFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTK-APTGTCAV-LVCGKERS 132
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
25-188 |
6.77e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 39.81 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 25 AGGApLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDetyrTSTVVVDLATSGERSFSFLVNPSAD 104
Cdd:PLN02341 119 AGGN-CNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLIEG----TDAGDSSSASYETLLCWVLVDPLQR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 105 QFLTSR-------------DLPVFGKDILHYCSLALAA-----ENCREAVVQATSKVKAREGWVSFDLNLREQMWSD-KA 165
Cdd:PLN02341 194 HGFCSRadfgpepafswisKLSAEAKMAIRQSKALFCNgyvfdELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVgTP 273
|
170 180
....*....|....*....|...
gi 1403722873 166 EMRRVIEQQCRSADILKLSDEEL 188
Cdd:PLN02341 274 DERRALEHLLRMSDVLLLTSEEA 296
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
26-96 |
7.22e-04 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 39.32 E-value: 7.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403722873 26 GGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVDlaTSGERSFS 96
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFID--PNGERTIT 104
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
22-88 |
9.55e-04 |
|
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: 39.10 E-value: 9.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403722873 22 QACAGGAPLNVAVGVARLAGDSAFIGRVGNDPfGRFLKRTLEEQGVGAEFMLTDETYRTSTVVVDLA 88
Cdd:TIGR03168 31 RKDAGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKESS 96
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
2-212 |
1.62e-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: 38.56 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 2 KIWALGDAVVDL------LPA--GDM--NYQACAGGAPLNVAVGVARLAGDSAFIGRVGNDPFGRFLKRTLEEQGVgaEF 71
Cdd:cd01944 1 KVLVIGAAVVDIvldvdkLPAsgGDIeaKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGI--EI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403722873 72 MLTDETYRTSTVVVDLAT-SGERsfSFLVNPSADQFLTSRD---LPVFGKDILHYCSLALAAENC-REAVVQATSKVKAR 146
Cdd:cd01944 79 LLPPRGGDDGGCLVALVEpDGER--SFISISGAEQDWSTEWfatLTVAPYDYVYLSGYTLASENAsKVILLEWLEALPAG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403722873 147 EGWVsFDLNLREQMWSDkAEMRRVIeqQCRSadILKLSDEELLWMTEEETSdweEALALLERYPAR 212
Cdd:cd01944 157 TTLV-FDPGPRISDIPD-TILQALM--AKRP--IWSCNREEAAIFAERGDP---AAEASALRIYAK 213
|
|
|