|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
12-299 |
1.78e-95 |
|
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: 285.24 E-value: 1.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 12 VVCIGETMAALAPDPPSPLQNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDP 91
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 92 HRPTGLLVKDPGPAGTR-VHYYRSGSAASALGPDALDSPPMRTAALVHLTGITPALSQSCRELVTRALATAdGERRYAVS 170
Cdd:cd01166 82 GRPTGLYFLEIGAGGERrVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALSESAREALLEALEAA-KARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 171 FDVNHRPALWPDGTAPAVLRELADQADIVFVGLDEAQGLWGADL---TAADIRALLPRPRILVVKDGASTATAVTDDGQC 247
Cdd:cd01166 161 FDLNYRPKLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDptdAAERALALALGVKAVVVKLGAEGALVYTGGGRV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1697838644 248 TVPALRTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGHitAVSALEVTR 299
Cdd:cd01166 241 FVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFAN--AAAALVVTR 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
12-309 |
4.61e-66 |
|
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: 210.13 E-value: 4.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 12 VVCIGETMA---ALAPDPPSP--LQNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSH 86
Cdd:COG0524 2 VLVIGEALVdlvARVDRLPKGgeTVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 87 VRTDPHRPTGLLVKDPGPAGTR-VHYYRSgsAASALGPDALDSPPMRTAALVHLTGITPAlSQSCRELVTRALATADgER 165
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERtIVFYRG--ANAELTPEDLDEALLAGADILHLGGITLA-SEPPREALLAALEAAR-AA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 166 RYAVSFDVNHRPALWPDgtAPAVLRELADQADIVFVGLDEAQGLWGADLTAADIRALLPR-PRILVVKDGASTATAVTDD 244
Cdd:COG0524 158 GVPVSLDPNYRPALWEP--ARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARgVKLVVVTLGAEGALLYTGG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1697838644 245 GQCTVPALRTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGHitAVSALEVTR--DHGPLPDEKE 309
Cdd:COG0524 236 EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFAN--AAAALVVTRpgAQPALPTREE 300
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
12-299 |
6.79e-47 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 160.59 E-value: 6.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 12 VVCIGETMAALAPD---PPSPLQNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVR 88
Cdd:pfam00294 2 VVVIGEANIDLIGNvegLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 89 TDPHRPTGLLVKDPGPAGTR-VHYYRSGSAASALGPDALDSPPMRTAALVHLTGItpaLSQSCRELVTRALATAdgeRRY 167
Cdd:pfam00294 82 IDEDTRTGTALIEVDGDGERtIVFNRGAAADLTPEELEENEDLLENADLLYISGS---LPLGLPEATLEELIEA---AKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 168 AVSFDVNHRPALWPdgtAPAVLRELADQADIVFVGLDEAQGLWGADL-TAADIRALLP-----RPRILVVKDGASTATAV 241
Cdd:pfam00294 156 GGTFDPNLLDPLGA---AREALLELLPLADLLKPNEEELEALTGAKLdDIEEALAALHkllakGIKTVIVTLGADGALVV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1697838644 242 TDDGQCTVPALR-TTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGHitAVSALEVTR 299
Cdd:pfam00294 233 EGDGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFAN--AAAALVVQK 289
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
12-299 |
9.41e-44 |
|
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: 152.41 E-value: 9.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 12 VVCIGETMAA-LAPDPPSPLQNAAHLrlsvAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTD 90
Cdd:cd01167 2 VVCFGEALIDfIPEGSGAPETFTKAP----GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 91 PHRPTGLLVKDPGPAGTRVHYYRSGSAASALGPDALDSPPMRTAALVHlTGITPALSQSCRELVTRALATADGERRYaVS 170
Cdd:cd01167 78 PAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLSEADILH-FGSIALASEPSRSALLELLEAAKKAGVL-IS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 171 FDVNHRPALWPDGT-APAVLRELADQADIVFVGLDEAQGLWG-ADLTAADIRALLPRPRILVVKDGASTATAVTDDGQCT 248
Cdd:cd01167 156 FDPNLRPPLWRDEEeARERIAELLELADIVKLSDEELELLFGeEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1697838644 249 VPALRTTVVEAVGAGDAFAAGFLAGLLKG-------ATTERALRLGHitAVSALEVTR 299
Cdd:cd01167 236 VPGIPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFAN--AVGALTCTK 291
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
12-314 |
2.08e-39 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 141.20 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 12 VVCIGETMAALAPDPP-SPLQNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTD 90
Cdd:TIGR04382 4 VITIGRVGVDLYPQQIgVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 91 PHRPTGLL---VKDPGPAGtrVHYYRSGSAASALGPDALDSPPMRTAALVHLTGITPALSQScRELVTRALATADgERRY 167
Cdd:TIGR04382 84 PGRRTSLVfleIKPPDEFP--LLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPS-REAVLKALEYAR-AAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 168 AVSFDVNHRPALWPDGT-APAVLRELADQADIVFVGLDEAQGLWGADLTAADIRALLPR-PRILVVKDGASTATAVTDDG 245
Cdd:TIGR04382 160 RVVLDIDYRPYLWKSPEeAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAgVEILVVKRGPEGSLVYTGDG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1697838644 246 QC-TVPALRTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGhiTAVSALEVTRdHG---PLPDEKETERLL 314
Cdd:TIGR04382 240 EGvEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYG--NACGAIVVSR-HScspAMPTLEELEAFL 309
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-299 |
1.01e-35 |
|
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: 130.89 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 24 PDPPSPLqNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHRPTGLLVkdpg 103
Cdd:cd01942 20 PGPFESV-LVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 104 pagtrVHYYRSGSAASALGPDALD-------SPPMRTAALVHLTgitpalsqSCRELVTRALATADGERRyaVSFDVNHR 176
Cdd:cd01942 95 -----ILTDGDDNQIAYFYPGAMDelepndeADPDGLADIVHLS--------SGPGLIELARELAAGGIT--VSFDPGQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 177 paLWPDGTApaVLRELADQADIVFVGLDEAQGLwgADLTAADIRALLPRPRILVVKDGASTATAVTDDGQCTVPAL-RTT 255
Cdd:cd01942 160 --LPRLSGE--ELEEILERADILFVNDYEAELL--KERTGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVpAVK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1697838644 256 VVEAVGAGDAFAAGFLAGLLKGATTERALRLGHITAvsALEVTR 299
Cdd:cd01942 234 VVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAA--SLKVER 275
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
41-274 |
7.36e-26 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 105.02 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 41 AGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHRPTGLLVKDPGPAGTR-----VHyyrsG 115
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsftfmVR----P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 116 SAASALGPDalDSPPMRTAALVHLTGItpALSQ-----SCRELVTRALAtADGErryaVSFDVNHRPALWPDgtaPAVLR 190
Cdd:PRK09434 104 SADLFLQPQ--DLPPFRQGEWLHLCSI--ALSAepsrsTTFEAMRRIKA-AGGF----VSFDPNLREDLWQD---EAELR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 191 ELADQ----ADIVFVGLDEAQGLWGADLTAADIRALLPR--PRILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGD 264
Cdd:PRK09434 172 ECLRQalalADVVKLSEEELCFLSGTSQLEDAIYALADRypIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGD 251
|
250
....*....|
gi 1697838644 265 AFAAGFLAGL 274
Cdd:PRK09434 252 AFVAGLLAGL 261
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
42-291 |
1.31e-24 |
|
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: 101.54 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 42 GAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVsHVRTDPHRPTG---LLVkDPGPAGTRVHYyrsGSAA 118
Cdd:cd01168 56 GSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTGtcaVLV-TPDAERTMCTY---LGAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 119 SALGPDALDSPPMRTAALVHLTG--ITPAlSQSCRELVTRAlatADGERRYAVSF-DVN----HRPALWpdgtapavlrE 191
Cdd:cd01168 131 NELSPDDLDWSLLAKAKYLYLEGylLTVP-PEAILLAAEHA---KENGVKIALNLsAPFivqrFKEALL----------E 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 192 LADQADIVFVGLDEAQGLWGADLTA---ADIRALLPRPRILVVKDGASTATAVTDDGQCTVPALR-TTVVEAVGAGDAFA 267
Cdd:cd01168 197 LLPYVDILFGNEEEAEALAEAETTDdleAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFA 276
|
250 260
....*....|....*....|....
gi 1697838644 268 AGFLAGLLKGATTERALRLGHITA 291
Cdd:cd01168 277 GGFLYGLVQGEPLEECIRLGSYAA 300
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
1-315 |
5.99e-21 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 91.61 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 1 MTTSWRPAPGPVVCIGETMAALAPDPPS-PLQNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAA 79
Cdd:PLN02323 2 MTAPSTAESSLVVCFGEMLIDFVPTVSGvSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 80 AGVDVSHVRTDPHRPTGL----LVKDpgpaGTR-VHYYRSGSAASALGPDALDSPPMRTAALVHLTGITpALSQSCRELV 154
Cdd:PLN02323 82 NGVNNEGVRFDPGARTALafvtLRSD----GEReFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSIS-LITEPCRSAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 155 TRALATADgERRYAVSFDVNHRPALWPdgtAPAVLRE----LADQADIVFVGLDEAQGLWGADLTAADIRALL--PRPRI 228
Cdd:PLN02323 157 LAAMKIAK-EAGALLSYDPNLRLPLWP---SAEAAREgimsIWDEADIIKVSDEEVEFLTGGDDPDDDTVVKLwhPNLKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 229 LVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAAGFLAGLLKGATT---ERALR--LGHITAVSALEVT-RDHG 302
Cdd:PLN02323 233 LLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLledEERLReaLRFANACGAITTTeRGAI 312
|
330
....*....|....
gi 1697838644 303 P-LPDEKETERLLG 315
Cdd:PLN02323 313 PaLPTKEAVLKLLK 326
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
40-291 |
1.20e-19 |
|
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: 87.02 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 40 VAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDpHRPTGL-LVKDPGpaGTRVH-YYRSGSA 117
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK-EGENAVaDVELVD--GDRIFgLSNKGGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 118 ASALgPDALDSPPMRTAALVH--LTGITPALSQSCRELVtralatADGERryaVSFDVNHRpalWPDgtapAVLRELADQ 195
Cdd:cd01940 98 AREH-PFEADLEYLSQFDLVHtgIYSHEGHLEKALQALV------GAGAL---ISFDFSDR---WDD----DYLQLVCPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 196 ADIVFVGldeaqglwGADLTAADIRALLPR-----PRILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAAGF 270
Cdd:cd01940 161 VDFAFFS--------ASDLSDEEVKAKLKEavsrgAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGF 232
|
250 260
....*....|....*....|..
gi 1697838644 271 LAGLLKGATT-ERALRLGHITA 291
Cdd:cd01940 233 LLSLLAGGTAiAEAMRQGAQFA 254
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
23-296 |
6.43e-19 |
|
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: 84.78 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 23 APDPPSPLQNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGV-DVSHVRTDPHRPTGLLVKd 101
Cdd:cd01947 18 APPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDkHTVAWRDKPTRKTLSFID- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 102 pgPAGTRVhYYRSGSAASalgpDALDSPPMRTAALVHLTGITP--ALSQSCRELVTRALATADGERryavsfdVNHRpal 179
Cdd:cd01947 97 --PNGERT-ITVPGERLE----DDLKWPILDEGDGVFITAAAVdkEAIRKCRETKLVILQVTPRVR-------VDEL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 180 wpdgtapavlRELADQADIVFVGLDEAQGLWGADltaadiRALLPRPRILVVKDGASTATAVTDDGQCTVPALRTTVVEA 259
Cdd:cd01947 160 ----------NQALIPLDILIGSRLDPGELVVAE------KIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDS 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 1697838644 260 VGAGDAFAAGFLAGLLKGATTERALRLGHITAVSALE 296
Cdd:cd01947 224 TGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVS 260
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
55-299 |
6.24e-16 |
|
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: 76.82 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 55 GVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHRPTG--LLVKDPGPAGTRVHYyrsGSAASALGPDALD--SPP 130
Cdd:cd01174 50 GARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGtaVITVDESGENRIVVV---PGANGELTPADVDaaLEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 131 MRTAALVHLTGITPAlsqscrELVTRALATAdgeRRYAVSFDVNhrPAlwPdgtAPAVLRELADQADIVFVGLDEAQGLW 210
Cdd:cd01174 127 IAAADVLLLQLEIPL------ETVLAALRAA---RRAGVTVILN--PA--P---ARPLPAELLALVDILVPNETEAALLT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 211 GADLTAAD-----IRALLPR-PRILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAAGFLAGLLKGATTERAL 284
Cdd:cd01174 191 GIEVTDEEdaekaARLLLAKgVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAI 270
|
250
....*....|....*
gi 1697838644 285 RLGhiTAVSALEVTR 299
Cdd:cd01174 271 RFA--NAAAALSVTR 283
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
203-314 |
2.22e-13 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 69.78 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 203 LDEAQGLWGADL-TAADI----RALLPR-PRILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAAGFLAGLLK 276
Cdd:COG1105 185 LEELEELLGRPLeTLEDIiaaaRELLERgAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLAR 264
|
90 100 110
....*....|....*....|....*....|....*...
gi 1697838644 277 GATTERALRLGhiTAVSALEVTRDHGPLPDEKETERLL 314
Cdd:COG1105 265 GLDLEEALRLA--VAAGAAAALSPGTGLPDREDVEELL 300
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
11-296 |
9.47e-13 |
|
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: 67.72 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 11 PVVCIGETMAALAPDPPSPLQ----NAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVsH 86
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVpgtsNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 87 VRTDPHRPTG--LLVKDpgpagtrvhyyRSGSAASALG-PDALDSPPMRTaalvhLTGITPALSQS--------CRELVT 155
Cdd:cd01941 80 GIVFEGRSTAsyTAILD-----------KDGDLVVALAdMDIYELLTPDF-----LRKIREALKEAkpivvdanLPEEAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 156 RALATADGERRYAVSFDvnhrPAlwpDGTAPAVLRELADQADIVFVGLDEAQGLWGA------DLTAADIRALLPRPRIL 229
Cdd:cd01941 144 EYLLALAAKHGVPVAFE----PT---SAPKLKKLFYLLHAIDLLTPNRAELEALAGAlienneDENKAAKILLLPGIKNV 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1697838644 230 VVKDGASTATAVTDDGQCTV----PALRTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGHITAVSALE 296
Cdd:cd01941 217 IVTLGAKGVLLSSREGGVETklfpAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
31-299 |
4.22e-12 |
|
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: 65.78 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 31 QNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHRPT---GLLVKDPGPAGT 107
Cdd:cd01945 26 IVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSpisSITDITGDRATI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 108 RVHYYRSGSAASALGPDALDSppmrtAALVHLTGITPALSQScrelvtraLATADGERRYAVSFDVnhrpalwpDGTAPA 187
Cdd:cd01945 106 SITAIDTQAAPDSLPDAILGG-----ADAVLVDGRQPEAALH--------LAQEARARGIPIPLDL--------DGGGLR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 188 VLRELADQADIVFVGLDEAQGLWGADLTAADIRALLPRPRILVVKDGASTATAVTDDGQ-CTVPALRTTVVEAVGAGDAF 266
Cdd:cd01945 165 VLEELLPLADHAICSENFLRPNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGElFHVPAFPVEVVDTTGAGDVF 244
|
250 260 270
....*....|....*....|....*....|...
gi 1697838644 267 AAGFLAGLLKGATTERALRLGhiTAVSALEVTR 299
Cdd:cd01945 245 HGAFAHALAEGMPLREALRFA--SAAAALKCRG 275
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
46-303 |
4.44e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 65.14 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 46 NVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPhrptgllvkdpgpagtrvhyyrsgsaasalGPDA 125
Cdd:PRK09813 28 NVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKH------------------------------GVTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 126 LDSPPMRTAALVHltgitpalsQSCRELVTRALATADGERRYAVSFDVNHrPALWpdGTAPAVLREL-ADQADIVFVGLD 204
Cdd:PRK09813 78 QTQVELHDNDRVF---------GDYTEGVMADFALSEEDYAWLAQYDIVH-AAIW--GHAEDAFPQLhAAGKLTAFDFSD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 205 EAQG-LWGADLTAAD------------IRALLPRprilVVKDGASTATA-------VTDDGQ--CTVPALRTTVVEAVGA 262
Cdd:PRK09813 146 KWDSpLWQTLVPHLDyafasapqedefLRLKMKA----IVARGAGVVIVtlgengsIAWDGAqfWRQAPEPVTVVDTMGA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1697838644 263 GDAFAAGFLAGLLKGATTERALRLGHITAVSALEVtrdHGP 303
Cdd:PRK09813 222 GDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQY---HGA 259
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
182-314 |
3.01e-11 |
|
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: 63.36 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 182 DGTAPAVLRELADQADIVFVGLDEAQGLWGADL-TAADI----RALLPR-PRILVVKDGASTATAVTDDGQCTVPALRTT 255
Cdd:TIGR03168 163 DTSGEALREALAAKPFLIKPNHEELEELFGRELkTLEEIieaaRELLDRgAENVLVSLGADGALLVTKEGALKATPPKVE 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1697838644 256 VVEAVGAGDAFAAGFLAGLLKGATTERALRLGhiTAVSALEVTRDHGPLPDEKETERLL 314
Cdd:TIGR03168 243 VVNTVGAGDSMVAGFLAGLARGLSLEEALRFA--VAAGSAAAFSPGTGLPDPEDVEELL 299
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
42-291 |
4.05e-10 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 60.04 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 42 GAESNVA-----MYLADHGvRATWLSAVGDDPLGRRVRATVAAAGVDVsHVRTDPHRPTGLLvkdpgpAGTRVHYYRSG- 115
Cdd:PTZ00247 63 GSALNTArvaqwMLQAPKG-FVCYVGCVGDDRFAEILKEAAEKDGVEM-LFEYTTKAPTGTC------AVLVCGKERSLv 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 116 ---SAASALGPDALDSPPM----RTAALVHLTGITPALSqscrelVTRALATADGERRYAVSFDVN-HRPALWPDGTAPa 187
Cdd:PTZ00247 135 anlGAANHLSAEHMQSHAVqeaiKTAQLYYLEGFFLTVS------PNNVLQVAKHARESGKLFCLNlSAPFISQFFFER- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 188 vLRELADQADIVFVGLDEAQGL-----WG-ADLT--AADIRALLP----RPRILVVKDGASTATAVTDDGQCT--VPALR 253
Cdd:PTZ00247 208 -LLQVLPYVDILFGNEEEAKTFakamkWDtEDLKeiAARIAMLPKysgtRPRLVVFTQGPEPTLIATKDGVTSvpVPPLD 286
|
250 260 270
....*....|....*....|....*....|....*....
gi 1697838644 254 TT-VVEAVGAGDAFAAGFLAGLLKGATTERALRLGHITA 291
Cdd:PTZ00247 287 QEkIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSA 325
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
190-299 |
1.56e-09 |
|
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: 57.93 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 190 RELADQADIVFVGldeaqglwgadltaadiRALLPR-PRILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAA 268
Cdd:cd01164 194 RPLGDEEDVIAAA-----------------RKLIERgAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVA 256
|
90 100 110
....*....|....*....|....*....|.
gi 1697838644 269 GFLAGLLKGATTERALRLGhiTAVSALEVTR 299
Cdd:cd01164 257 GFVAGLAQGLSLEEALRLA--VAAGSATAFS 285
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
58-291 |
5.26e-09 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 56.65 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 58 ATWLSAVGDDPLGRRVRATVAAAGVDVsHVRTDPHRPTG---LLVKDpgpaGTR--VHYYrsgSAASALGPDALDSPpmR 132
Cdd:PLN02548 72 TSYMGCIGKDKFGEEMKKCATAAGVNV-HYYEDESTPTGtcaVLVVG----GERslVANL---SAANCYKVEHLKKP--E 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 133 TAALVH------LTGITPALSQSCRELVTRAlATADGErryavSFDVNHrpalwpdgTAPAVLRELADQ-------ADIV 199
Cdd:PLN02548 142 NWALVEkakfyyIAGFFLTVSPESIMLVAEH-AAANNK-----TFMMNL--------SAPFICEFFKDQlmealpyVDFL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 200 FVGLDEA------QGLWGADL--TAADIRALlP-----RPRILVVKDGAStATAVTDDGQCT----VPALRTTVVEAVGA 262
Cdd:PLN02548 208 FGNETEArtfakvQGWETEDVeeIALKISAL-PkasgtHKRTVVITQGAD-PTVVAEDGKVKefpvIPLPKEKLVDTNGA 285
|
250 260
....*....|....*....|....*....
gi 1697838644 263 GDAFAAGFLAGLLKGATTERALRLGHITA 291
Cdd:PLN02548 286 GDAFVGGFLSQLVQGKDIEECVRAGNYAA 314
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
182-314 |
6.72e-09 |
|
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: 56.06 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 182 DGTAPAVLRELADQADIVFVGLDEAQGLWGADL-TAADI----RALLPR-PRILVVKDGASTATAVTDDGQCTVPALRTT 255
Cdd:TIGR03828 163 DTSGEALRDGLKAKPFLIKPNDEELEELFGRELkTLEEIieaaRELLDLgAENVLISLGADGALLVTKEGALFAQPPKGE 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1697838644 256 VVEAVGAGDAFAAGFLAGLLKGATTERALRLGhiTAVSALEVTRDHGPLPDEKETERLL 314
Cdd:TIGR03828 243 VVSTVGAGDSMVAGFLAGLESGLSLEEALRLA--VAAGSAAAFSEGTGLPDPEDIEELL 299
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
40-299 |
8.52e-09 |
|
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: 55.89 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 40 VAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVshvrTDPHRP---TGLLVKDPGPAGTRVHYYRSGs 116
Cdd:cd01944 34 VIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEI----LLPPRGgddGGCLVALVEPDGERSFISISG- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 117 AASALGPDALDSPPMRTAALVHLTGITPALSQSCRELVTRALAtaDGERRYAVSFDVNHRPALWPDgtapAVLRELADQA 196
Cdd:cd01944 109 AEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLE--ALPAGTTLVFDPGPRISDIPD----TILQALMAKR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 197 DIVFVGLDEAQGLWGADLTAADIRAL---LPRPRILVVKDGASTATAVTDDGQC-TVPALRTTVVEAVGAGDAFAAGFLA 272
Cdd:cd01944 183 PIWSCNREEAAIFAERGDPAAEASALriyAKTAAPVVVRLGSNGAWIRLPDGNThIIPGFKVKAVDTIGAGDTHAGGMLA 262
|
250 260
....*....|....*....|....*..
gi 1697838644 273 GLLKGATTERALRLGHitAVSALEVTR 299
Cdd:cd01944 263 GLAKGMSLADAVLLAN--AAAAIVVTR 287
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
39-313 |
2.05e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 55.20 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 39 SVAGAESNVAMyladhgvratwLSAVGDDPLGRRVRATVAAAGVD-VSHVRTDPHRPTGLLVKDPGPAGTRVHYyrSGSA 117
Cdd:PLN02813 143 SAAGPALNVAM-----------AGSVGSDPLGDFYRTKLRRANVHfLSQPVKDGTTGTVIVLTTPDAQRTMLSY--QGTS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 118 ASALGPDALDSPPMRTAALV------HLTGITPALSQSCREL----VTRALATADgerryaVSFDVNHRPALWpdgtapa 187
Cdd:PLN02813 210 STVNYDSCLASAISKSRVLVvegylwELPQTIEAIAQACEEAhragALVAVTASD------VSCIERHRDDFW------- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 188 vlRELADQADIVFVGLDEAQGLWGADLTAADIRALLPRPR---ILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGD 264
Cdd:PLN02813 277 --DVMGNYADILFANSDEARALCGLGSEESPESATRYLSHfcpLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGD 354
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1697838644 265 AFAAGFLAGLLKGATTERAlrLGHITAVSALEVTRDHGPLPDEKETERL 313
Cdd:PLN02813 355 AYAAGILYGLLRGVSDLRG--MGELAARVAATVVGQQGTRLRVEDAVEL 401
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
132-285 |
2.55e-08 |
|
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: 54.39 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 132 RTAALVHLTGITPALSQSCRELVtralatadgERRYAVSFDVNHrpaLWPDGTAPAVLRELAdQADIVFVGLDEAQGLWG 211
Cdd:cd01946 113 KDSEFVFLGNIAPELQREVLEQV---------KDPKLVVMDTMN---FWISIKPEKLKKVLA-KVDVVIINDGEARQLTG 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1697838644 212 -ADL--TAADIRALlpRPRILVVKDGASTATAVTDDGQCTVPALR-TTVVEAVGAGDAFAAGFLAGLLK-GATTERALR 285
Cdd:cd01946 180 aANLvkAARLILAM--GPKALIIKRGEYGALLFTDDGYFAAPAYPlESVFDPTGAGDTFAGGFIGYLASqKDTSEANMR 256
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
12-287 |
4.47e-08 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 53.56 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 12 VVCIGET---MAALAPDPPSP--LQNAAHLRLSVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSH 86
Cdd:cd01939 2 VLCVGLTvldFITTVDKYPFEdsDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 87 V-RTDPHRPTGLLVKDPGpAGTR--VHYYRSGSAASAlgpDALDSPPMRTAALVHLTGITPALSQSCRELVtRALATADG 163
Cdd:cd01939 82 CyRKDIDEPASSYIIRSR-AGGRttIVNDNNLPEVTY---DDFSKIDLTQYGWIHFEGRNPDETLRMMQHI-EEHNNRRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 164 ERRYAVSFDV-NHRPALWpdgtapavlrELADQADIVFVGLDEAQGLwGADLTAADIRALLPR---PRILVVKDGASTAT 239
Cdd:cd01939 157 EIRITISVEVeKPREELL----------ELAAYCDVVFVSKDWAQSR-GYKSPEECLRGEGPRakkAALLVCTWGDQGAG 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1697838644 240 AVTDDGQCT-VPALR-TTVVEAVGAGDAFAAGFLAGLLKGATT-ERALRLG 287
Cdd:cd01939 226 ALGPDGEYVhSPAHKpIRVVDTLGAGDTFNAAVIYALNKGPDDlSEALDFG 276
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
133-275 |
4.76e-08 |
|
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: 52.48 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 133 TAALVHLTGITPALsqscrELVTRALATADgERRYAVSFDVNHRPALWPDGTapavLRELADQADIVFVGLDEA------ 206
Cdd:cd00287 57 GADAVVISGLSPAP-----EAVLDALEEAR-RRGVPVVLDPGPRAVRLDGEE----LEKLLPGVDILTPNEEEAealtgr 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 207 QGLWGADLTAADIRALLPRPRILVVKDGASTATAVTDDG-QCTVPALRTTVVEAVGAGDAFAAGFLAGLL 275
Cdd:cd00287 127 RDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGtEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
41-291 |
1.30e-07 |
|
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: 52.18 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 41 AGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRtDPHRPTglLVKdpgpagTRVH---------Y 111
Cdd:cd01172 39 LGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPT--TTK------TRVIarnqqllrvD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 112 YRSGSAASALGPDALDSPPMRTAALVHLT--------GITPALSQS----CRELVTRALATADGE--RRY--AVSFDVNH 175
Cdd:cd01172 110 REDDSPLSAEEEQRLIERIAERLPEADVVilsdygkgVLTPRVIEAliaaARELGIPVLVDPKGRdySKYrgATLLTPNE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 176 RPAlwpdgtAPAVLRELADQADIVFVGLDeaqglwgadltaadIRALLPRpRILVVKDGASTATAVTDDGQCT-VPALRT 254
Cdd:cd01172 190 KEA------REALGDEINDDDELEAAGEK--------------LLELLNL-EALLVTLGEEGMTLFERDGEVQhIPALAK 248
|
250 260 270
....*....|....*....|....*....|....*..
gi 1697838644 255 TVVEAVGAGDAFAAGFLAGLLKGATTERALRLGHITA 291
Cdd:cd01172 249 EVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAA 285
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
23-302 |
2.46e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 51.72 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 23 APDPPSPLQNAAhlrlsvAGAESNVAMYL-ADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHrPTG---LL 98
Cdd:PLN02379 74 SPDDLSPIKTMA------GGSVANTIRGLsAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKG-PTAqcvCL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 99 VKDPGPAGTRVHYyrsgSAASALGPDALDSPPMRTAALVHLTgitpaLSQSCRELVTRALATADGERrYAVSFDV----- 173
Cdd:PLN02379 147 VDALGNRTMRPCL----SSAVKLQADELTKEDFKGSKWLVLR-----YGFYNLEVIEAAIRLAKQEG-LSVSLDLasfem 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 174 --NHRPALwpdgtapavLREL-ADQADIVFVGLDEAQGLWGADLTA---ADIRALLPRPRILVVKDGASTATAVTDDGQC 247
Cdd:PLN02379 217 vrNFRSPL---------LQLLeSGKIDLCFANEDEARELLRGEQESdpeAALEFLAKYCNWAVVTLGSKGCIARHGKEVV 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1697838644 248 TVPAL-RTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGhitAVSALEVTRDHG 302
Cdd:PLN02379 288 RVPAIgETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVG---ACSGGSVVRALG 340
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
39-287 |
2.58e-07 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 51.35 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 39 SVAGAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHRPTglLVKdpgpagTRVhyyrSGSAA 118
Cdd:COG2870 53 ERPGGAANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPT--TTK------TRV----IAGGQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 119 SALGPDALDSPPmrtaalvhltgITPALSQSCRELVTRALATADG----------------ERRYAVSFDVNHRPALWPD 182
Cdd:COG2870 121 QLLRLDFEDRFP-----------LSAELEARLLAALEAALPEVDAvilsdygkgvltpeliQALIALARAAGKPVLVDPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 183 GTAPAVLREladqADIVFVGLDEAQGLWGADLT--------AADIRALLPRPRILVV--KDGASTATAvtDDGQCTVPAL 252
Cdd:COG2870 190 GRDFSRYRG----ATLLTPNLKEAEAAVGIPIAdeeelvaaAAELLERLGLEALLVTrgEEGMTLFDA--DGPPHHLPAQ 263
|
250 260 270
....*....|....*....|....*....|....*
gi 1697838644 253 RTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLG 287
Cdd:COG2870 264 AREVFDVTGAGDTVIATLALALAAGASLEEAAELA 298
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
181-302 |
3.22e-07 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 50.92 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 181 PDGTAPAVLRELADQADIVFVGLDEAQGLWGADLTAAD-----IRALLPR-PRILVVK-------DGASTATAVTDDGQC 247
Cdd:COG2240 124 FPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEealaaARALLALgPKIVVVTsvplddtPADKIGNLAVTADGA 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1697838644 248 TVpaLRTTVVEA--VGAGDAFAAGFLAGLLKGATTERALRLGHITAVSALEVTRDHG 302
Cdd:COG2240 204 WL--VETPLLPFspNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLERTAAAG 258
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
168-294 |
4.87e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 50.99 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 168 AVSFDVNHRPALWPDGTAP--AVLRELADQADIVFVGLDEAQGLWG-ADLTAADIRALLP--RPRILVVKDGASTATAVT 242
Cdd:PLN02341 256 AVFFDPGPRGKSLLVGTPDerRALEHLLRMSDVLLLTSEEAEALTGiRNPILAGQELLRPgiRTKWVVVKMGSKGSILVT 335
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1697838644 243 DDGQCTVPALRTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGhiTAVSA 294
Cdd:PLN02341 336 RSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLA--NAVGA 385
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
189-296 |
6.55e-07 |
|
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: 49.71 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 189 LRELADQADIVFVGLDEAQGLWGAD------LTAADIRALLPR--PRILVVKDGASTATAVTDDGQCTVPALRTTVVEAV 260
Cdd:cd01937 139 LRRANQEKLIKCVILKLHDVLKLSRveaeviSTPTELARLIKEtgVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPT 218
|
90 100 110
....*....|....*....|....*....|....*.
gi 1697838644 261 GAGDAFAAGFLAGLLKGATTERALRLGHITAVSALE 296
Cdd:cd01937 219 GAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFIE 254
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
55-314 |
1.17e-06 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 49.48 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 55 GVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHRPTG---LLVKDPGPAGTRVHyyrsGSAASALGPDALDSppm 131
Cdd:PRK11142 53 GADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGvalIFVNDEGENSIGIH----AGANAALTPALVEA--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 132 rtaalvHLTGITPA---LSQ--SCRELVTRALATAdgeRRYAVsfdvnhRPALWPdgtAPAvlRELADQ----ADIVFVG 202
Cdd:PRK11142 126 ------HRELIANAdalLMQleTPLETVLAAAKIA---KQHGT------KVILNP---APA--RELPDEllalVDIITPN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 203 LDEAQGLWGA----DLTAADIRALLPR--PRILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAAGFLAGLLK 276
Cdd:PRK11142 186 ETEAEKLTGIrvedDDDAAKAAQVLHQkgIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLE 265
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1697838644 277 GATTERALRLGHitAVSALEVTRdHG---PLPDEKETERLL 314
Cdd:PRK11142 266 GKPLPEAIRFAH--AAAAIAVTR-KGaqpSIPWREEIDAFL 303
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
229-287 |
2.24e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 48.65 E-value: 2.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1697838644 229 LVVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLG 287
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLG 264
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
230-298 |
1.17e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 46.23 E-value: 1.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1697838644 230 VVKDGASTATAVTDDGQCTVPALRTTVVEAVGAGDAFAAGFLAGLLKGATTERALRLGhiTAVSALEVT 298
Cdd:PRK09513 221 VISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLA--TAVSALAVS 287
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
42-307 |
1.94e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 42.80 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 42 GAESNVAMYLADHGVRATWLSAVGDDPLGRRVRATVAAAGVDVSHVRTDPHRPTGL--LVKDPGPAGTRVHYyrSGSAAS 119
Cdd:PTZ00292 53 GKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLamIFVDTKTGNNEIVI--IPGANN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 120 ALGPDALDSPpmrtaalvhltgiTPALSQSCRELVTR----------ALATADGERRYAVsfdVNHRPAlwPDGTAPAVL 189
Cdd:PTZ00292 131 ALTPQMVDAQ-------------TDNIQNICKYLICQneiplettldALKEAKERGCYTV---FNPAPA--PKLAEVEII 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 190 RELADQADIVFVGLDEAQGLWGADLT-------AADIRALLPRPRILVVKDGASTATAVTDDGQCTVPALRTTVVEAVGA 262
Cdd:PTZ00292 193 KPFLKYVSLFCVNEVEAALITGMEVTdtesafkASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGA 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1697838644 263 GDAFAAGFLAGLLKGATTERALRLGhiTAVSALEVTRdHG-----PLPDE 307
Cdd:PTZ00292 273 GDCFVGSMAYFMSRGKDLKESCKRA--NRIAAISVTR-HGtqssyPHPSE 319
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
181-291 |
5.51e-04 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 41.01 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 181 PDGTAPAVLRELADQADIVFVGLDEAQGLWGADL-TAADI----RALLPR-PRILVVKDGASTAT--------AVTDDG- 245
Cdd:PRK05756 124 APGVAEFLRDRALPAADIITPNLFELEWLSGRPVeTLEDAvaaaRALIARgPKIVLVTSLARAGYpadrfemlLVTADGa 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1697838644 246 -QCTVPALrTTVVEAVGAGDAFAAGFLAGLLKGATTERAlrLGHITA 291
Cdd:PRK05756 204 wHISRPLV-DFMRQPVGVGDLTSALFLARLLQGGSLEEA--LEHTTA 247
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
181-300 |
1.04e-03 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 40.26 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697838644 181 PDGTAPAVLRELADQADIVFVGLDEAQGLWG------ADLTAAdIRALL-PRPRILVVK-----DGASTATAVTDDGQCT 248
Cdd:cd01173 122 AEEIVPVYRDLLVPLADIITPNQFELELLTGkkindlEDAKAA-ARALHaKGPKTVVVTsvelaDDDRIEMLGSTATEAW 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1697838644 249 VPALRTTVVEA--VGAGDAFAAGFLAGLLKGATTERALR--LGHITAVsaLEVTRD 300
Cdd:cd01173 201 LVQRPKIPFPAyfNGTGDLFAALLLARLLKGKSLAEALEkaLNFVHEV--LEATYE 254
|
|
| |
