|
Name |
Accession |
Description |
Interval |
E-value |
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
1-303 |
1.76e-80 |
|
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: 246.01 E-value: 1.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 1 MYLVCGEALFDVFSlesAARSNELGFTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVP- 79
Cdd:cd01167 1 KVVCFGEALIDFIP---EGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 80 SDAPTTLAMVGLDASGSAQYQFRGEGCADRQVRLEHLPTLDGRIRGLHVGSYTLVVTPVADTLLALVRRESGR-RLVSLD 158
Cdd:cd01167 78 PAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAgVLISFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 159 PNVRLDPQPDIDLWRRRVEAFASHAHLIKASEEDLALLYPGRDPGEVARGWLNPRCRLVFVTHGGAGASVhCTHGSWSRP 238
Cdd:cd01167 158 PNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALL-YTKGGVGEV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597540 239 ADTALPLRDTVGAGDTFQAATLAYLRRldadspAGLAALSREAIDAMLAFAIRAAAVTCSRVGPD 303
Cdd:cd01167 237 PGIPVEVVDTTGAGDAFVAGLLAQLLS------RGLLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-310 |
1.17e-53 |
|
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: 177.38 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 3 LVCGEALFD-VFSLESAARSNEL----GFTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFL 77
Cdd:COG0524 3 LVIGEALVDlVARVDRLPKGGETvlagSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 78 VPS-DAPTTLAMVGLDASGSAQYQF-RGegcADRQVRLEHLPT-LDGRIRGLHVGSYTLVVTPVADTLLALVR--RESGR 152
Cdd:COG0524 83 RRDpGAPTGLAFILVDPDGERTIVFyRG---ANAELTPEDLDEaLLAGADILHLGGITLASEPPREALLAALEaaRAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 153 RlVSLDPNVRLdpqPDIDLWRRRVEAFASHAHLIKASEEDLALLYPGRDPGEVARGWLNPRCRLVFVTHGGAGASVHCTH 232
Cdd:COG0524 160 P-VSLDPNYRP---ALWEPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 233 GSWSRPAdTALPLRDTVGAGDTFQAATLAYLrrldadspaglaaLSREAIDAMLAFAIRAAAVTCSRVG--PDLPFAHEL 310
Cdd:COG0524 236 EVVHVPA-FPVEVVDTTGAGDAFAAGFLAGL-------------LEGLDLEEALRFANAAAALVVTRPGaqPALPTREEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-302 |
6.79e-33 |
|
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: 122.68 E-value: 6.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 3 LVCGEALFDVFSLESAARSNELGFTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGF-LVPSD 81
Cdd:cd01166 3 VTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHvRVDPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 82 APTTLAMVGLDASGSAQYQFRGEGCADRQVRLEHLPTLD-GRIRGLHVGSYTLVVTP-VADTLLALVR--RESGRRlVSL 157
Cdd:cd01166 83 RPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAAlAGADHLHLSGITLALSEsAREALLEALEaaKARGVT-VSF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 158 DPNVRldPQ-PDIDLWRRRVEAFASHAHLIKASEEDLALLYPGRDPGEVARGWL--NPRCRLVFVTHGGAGASVHCTHGS 234
Cdd:cd01166 162 DLNYR--PKlWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKLGAEGALVYTGGGR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597540 235 WSRPAdTALPLRDTVGAGDTFQAATLAylrrldadspaglAALSREAIDAMLAFAIRAAAVTCSRVGP 302
Cdd:cd01166 240 VFVPA-YPVEVVDTTGAGDAFAAGFLA-------------GLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
30-310 |
1.41e-30 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 116.96 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 30 AGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVPSDAPTT-LAMVGLDASGSAQYQFRGEGCAD 108
Cdd:PRK09434 27 PGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTsTVVVDLDDQGERSFTFMVRPSAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 109 RQVRLEHLPTLDgriRG--LHVGSYTLVVTPVADTLLALVRR--ESGRRlVSLDPNVRLDPQPDIDLWRRRVEAFASHAH 184
Cdd:PRK09434 107 LFLQPQDLPPFR---QGewLHLCSIALSAEPSRSTTFEAMRRikAAGGF-VSFDPNLREDLWQDEAELRECLRQALALAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 185 LIKASEEDLALLyPGRDPGEVARGWLNPR--CRLVFVTHGGAGASVHcTHGSWSRPADTALPLRDTVGAGDTFQAATLAY 262
Cdd:PRK09434 183 VVKLSEEELCFL-SGTSQLEDAIYALADRypIALLLVTLGAEGVLVH-TRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAG 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15597540 263 LRRldADSPAGLAALsREAIDamLAFAIRAAAVTCSRVGPDLPFAHEL 310
Cdd:PRK09434 261 LSQ--AGLWTDEAEL-AEIIA--QAQACGALATTAKGAMTALPNRQEL 303
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
3-305 |
1.69e-25 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 103.55 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 3 LVC-GEALFDVFSLESAARSNEL-GFTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDC-GFLVP 79
Cdd:PLN02323 13 VVCfGEMLIDFVPTVSGVSLAEApAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNeGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 80 SDAPTTLAMVGLDASGSAQYQFRGEGCADRQVRLEHLPT-LDGRIRGLHVGSYTLVVTPVADTLLALVR--RESGrRLVS 156
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLdLIRKAKIFHYGSISLITEPCRSAHLAAMKiaKEAG-ALLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 157 LDPNVRLDPQPDIDLWRRRVEAFASHAHLIKASEEDLALLYPGRDPGE--VARGWlNPRCRLVFVTHGGAGASVHcTHGS 234
Cdd:PLN02323 172 YDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDdtVVKLW-HPNLKLLLVTEGEEGCRYY-TKDF 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597540 235 WSRPADTALPLRDTVGAGDTFQAATLAYLrrldADSPAGL---AALsREAidamLAFAIRAAAVTCSRVG--PDLP 305
Cdd:PLN02323 250 KGRVEGFKVKAVDTTGAGDAFVGGLLSQL----AKDLSLLedeERL-REA----LRFANACGAITTTERGaiPALP 316
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
2-302 |
8.38e-24 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 98.57 E-value: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 2 YLVC-GEALFDV--FSLESAARSNELG-FTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFL 77
Cdd:pfam00294 1 KVVViGEANIDLigNVEGLPGELVRVStVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 78 VPS-DAPTTLAMVGLDASG--SAQYQFRGEGCADRQVRLEHLPTLdGRIRGLHVGSytLVVTPVADTLLALVrRESGRRL 154
Cdd:pfam00294 81 VIDeDTRTGTALIEVDGDGerTIVFNRGAAADLTPEELEENEDLL-ENADLLYISG--SLPLGLPEATLEEL-IEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 155 VSLDPNVRlDPQPDIdlwRRRVEAFASHAHLIKASEEDLALLY--PGRDPGEVAR--GWLNPRC-RLVFVTHGGAGASVH 229
Cdd:pfam00294 157 GTFDPNLL-DPLGAA---REALLELLPLADLLKPNEEELEALTgaKLDDIEEALAalHKLLAKGiKTVIVTLGADGALVV 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597540 230 CTHGSWSRPADTALPLRDTVGAGDTFQAATLAylrrldadspaglAALSREAIDAMLAFAIRAAAVTCSRVGP 302
Cdd:pfam00294 233 EGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLA-------------GLLAGKSLEEALRFANAAAALVVQKSGA 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
3-302 |
1.07e-18 |
|
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: 83.90 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 3 LVCGEALFDV-FSLESAARSNElgFTAIA------GGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCG 75
Cdd:cd01942 3 AVVGHLNYDIiLKVESFPGPFE--SVLVKdlrrefGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 76 FLVPS-DAPTTLAMVGLDASGS-AQYQFRGegcADRQVRLEHLPTLDGRIRGLHVGSYTLVVtpvadtLLALVRRESGRR 153
Cdd:cd01942 81 HVRVVdEDSTGVAFILTDGDDNqIAYFYPG---AMDELEPNDEADPDGLADIVHLSSGPGLI------ELARELAAGGIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 154 lVSLDPNvrldpQPDIDLWRRRVEAFASHAH--LIKASEEDLALLYPGRDPGEVARGwlnprCRLVFVTHGGAGASVHCT 231
Cdd:cd01942 152 -VSFDPG-----QELPRLSGEELEEILERADilFVNDYEAELLKERTGLSEAELASG-----VRVVVVTLGPKGAIVFED 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597540 232 HGSWSRPADTALPLRDTVGAGDTFQAATL-AYLRRLDadspaglaalsreaIDAMLAFAIRAAAVTCSRVGP 302
Cdd:cd01942 221 GEEVEVPAVPAVKVVDTTGAGDAFRAGFLyGLLRGYD--------------LEESLRLGNLAASLKVERRGA 278
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
25-267 |
1.10e-14 |
|
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: 73.02 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 25 GFTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVP-SDAPTTLAMVGL-DASGSAQYQFR 102
Cdd:TIGR04382 28 SFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTdPGRRTSLVFLEIkPPDEFPLLFYR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 103 gEGCADRQVRLEHLPTLDGRIRGLHVGSYTLVVTPVAD--TLLALVRRESGRRLVSLDpnvrLDPQPdiDLWRRRVEA-- 178
Cdd:TIGR04382 108 -ENAADLALTPDDVDEDYIASARALLVSGTALSQEPSReaVLKALEYARAAGVRVVLD----IDYRP--YLWKSPEEAgi 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 179 ----FASHAHLIKASEEDLALLYPGRDPGEVARGWLNPRCRLVFVTHGGAGASVHCTHG-SWSRPADTALPLRdTVGAGD 253
Cdd:TIGR04382 181 ylrlVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGeGVEVPGFPVEVLN-VLGAGD 259
|
250
....*....|....*
gi 15597540 254 TFQAATL-AYLRRLD 267
Cdd:TIGR04382 260 AFASGFLyGLLAGWD 274
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
26-301 |
2.02e-14 |
|
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: 71.94 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 26 FTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVP-SDAPTTLAMVGLDASGSAQYQFRge 104
Cdd:cd01945 31 YAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVaPGARSPISSITDITGDRATISIT-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 105 gCADRQVRLEHLPTLD-GRIRGLHVGSYTLvvtPVADTLLALVRRESGRRLVSLDpnvrldpqPDIDLWRRRVEAFASHA 183
Cdd:cd01945 109 -AIDTQAAPDSLPDAIlGGADAVLVDGRQP---EAALHLAQEARARGIPIPLDLD--------GGGLRVLEELLPLADHA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 184 hliKASEEDLALLYPGRDPGEVARGWLnPRCRLVFVTHGGAGAS-VHCTHGSWSRPAdTALPLRDTVGAGDTFQAA-TLA 261
Cdd:cd01945 177 ---ICSENFLRPNTGSADDEALELLAS-LGIPFVAVTLGEAGCLwLERDGELFHVPA-FPVEVVDTTGAGDVFHGAfAHA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15597540 262 YLRRLDadspaglaalsreaIDAMLAFAIRAAAVTCSRVG 301
Cdd:cd01945 252 LAEGMP--------------LREALRFASAAAALKCRGLG 277
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
25-301 |
8.62e-14 |
|
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: 70.27 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 25 GFTAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFL-VPSDAPTTLAMVGLDASGsaqyqfrg 103
Cdd:cd01174 30 SFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVeVVVGAPTGTAVITVDESG-------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 104 EGC------ADRQVRLEHLPTLDGRIRGlhvgsYTLVV----TPVADTLLALVR-RESGRRLVsldpnvrLDPQPDIDLw 172
Cdd:cd01174 102 ENRivvvpgANGELTPADVDAALELIAA-----ADVLLlqleIPLETVLAALRAaRRAGVTVI-------LNPAPARPL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 173 rrrVEAFASHAHLIKASEEDLALL----YPGRDPGEVARGWLNPR-CRLVFVTHGGAGASVHCTHGSWSRPAdTALPLRD 247
Cdd:cd01174 169 ---PAELLALVDILVPNETEAALLtgieVTDEEDAEKAARLLLAKgVKNVIVTLGAKGALLASGGEVEHVPA-FKVKAVD 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15597540 248 TVGAGDTFQAATLAYLRRldadspaglaalsREAIDAMLAFAIRAAAVTCSRVG 301
Cdd:cd01174 245 TTGAGDTFIGALAAALAR-------------GLSLEEAIRFANAAAALSVTRPG 285
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
27-305 |
1.78e-13 |
|
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: 69.57 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 27 TAIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVPSDAPTTLAMVGLDASGSAQYQFRGEGC 106
Cdd:cd01168 51 KYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 107 ADRQVrlEHLPT-LDGRIRGLHVGSYTLVVTPVADTLLALVRRESGRRLV-SL-DPNVrldpqpdIDLWRRRVEAFASHA 183
Cdd:cd01168 131 NELSP--DDLDWsLLAKAKYLYLEGYLLTVPPEAILLAAEHAKENGVKIAlNLsAPFI-------VQRFKEALLELLPYV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 184 HLIKASEEDLALLY--PGRDPGEVARGWLNPRCRLVFVTHGGAGASVHCTHGSWSRPADTALPLRDTVGAGDTFQAATLa 261
Cdd:cd01168 202 DILFGNEEEAEALAeaETTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFL- 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15597540 262 ylrrldadspAGLaaLSREAIDAMLAFAIRAAAVTCSRVGPDLP 305
Cdd:cd01168 281 ----------YGL--VQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
31-301 |
1.82e-13 |
|
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: 68.92 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 31 GGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVPSDAPTTLAMVGLDAsGSAQYQFRGEGCADRQ 110
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADVELVD-GDRIFGLSNKGGVARE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 111 V----RLEHLPTLDgrirGLHVGSYTlvvtpVADTLLALVRRESGR-RLVSLDPNVRLdpqpDIDLWRRRVE----AFAS 181
Cdd:cd01940 101 HpfeaDLEYLSQFD----LVHTGIYS-----HEGHLEKALQALVGAgALISFDFSDRW----DDDYLQLVCPyvdfAFFS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 182 HAHLikASEEDLALLypgrdpGEVArgwlNPRCRLVFVTHGGAGASvhCTHGS--WSRPADTALPLrDTVGAGDTFQAAT 259
Cdd:cd01940 168 ASDL--SDEEVKAKL------KEAV----SRGAKLVIVTRGEDGAI--AYDGAvfYSVAPRPVEVV-DTLGAGDSFIAGF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15597540 260 LAYLrrldadspaglaALSREAIDAMLAFAIRAAAVTCSRVG 301
Cdd:cd01940 233 LLSL------------LAGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
31-276 |
8.87e-11 |
|
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: 61.26 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 31 GGSPFNVAVGLRRLGVEAALFGGLSSDYLGAR-LRRVLEEEgvdcgFLVPSDAPTTLAMVGLDASGSAQYQFRgegCADR 109
Cdd:cd01937 24 GGPATYASLTLSRLGLTVKLVTKVGRDYPDKWsDLFDNGIE-----VISLLSTETTTFELNYTNEGRTRTLLA---KCAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 110 QVRLEhlpTLDGRIRGLHVgsytlVVTPVADTLLALVRRESGrrLVSLDPN--VRlDPQPDidlwRRRVEAFASHAHLIK 187
Cdd:cd01937 96 IPDTE---SPLSTITAEIV-----ILGPVPEEISPSLFRKFA--FISLDAQgfLR-RANQE----KLIKCVILKLHDVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 188 ASEEDLALLypgRDPGEVARGWLNPRCRLVFVTHGGAGASVHCTHGSWSRPAdTALPLRDTVGAGDTFQAATLA-YLRRL 266
Cdd:cd01937 161 LSRVEAEVI---STPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPA-SKKDVVDPTGAGDVFLAAFLYsRLSGK 236
|
250
....*....|
gi 15597540 267 DADSPAGLAA 276
Cdd:cd01937 237 DIKEAAEFAA 246
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
36-301 |
2.68e-10 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 60.21 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 36 NVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVPSDAPTT---LAMVgldasgSAQYQ-FRgegcADRQV 111
Cdd:COG2870 60 NVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTttkTRVI------AGGQQlLR----LDFED 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 112 RLEHLPTLDGRIRGL---HVGSYTLVVtpVAD----TLLALVRRESGRRLVSLDPNVRLDPQPDiDLWRRRveafasHAH 184
Cdd:COG2870 130 RFPLSAELEARLLAAleaALPEVDAVI--LSDygkgVLTPELIQALIALARAAGKPVLVDPKGR-DFSRYR------GAT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 185 LIK--ASEEDLALLYPGRDPGEVARG----WLNPRCRLVFVTHGGAGASVHCTHGSWSRPADTALPLRDTVGAGDTFqAA 258
Cdd:COG2870 201 LLTpnLKEAEAAVGIPIADEEELVAAaaelLERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTV-IA 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15597540 259 TLAylrrldadspAGLAA-LSREaiDAMlAFAIRAAAVTCSRVG 301
Cdd:COG2870 280 TLA----------LALAAgASLE--EAA-ELANLAAGIVVGKLG 310
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
27-301 |
1.05e-09 |
|
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: 58.34 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 27 TAIAGGSPfNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVPSDAPTTlamVGLDASGSAQYQFRgegc 106
Cdd:cd01172 36 EIRLGGAA-NVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPTT---TKTRVIARNQQLLR---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 107 ADRQVRL----EHLPTLDGRIRGlHVGSYTLVVtpVAD----TLLALVRRESGRRLVSLDPNVRLDPQpdidlwrRRVEA 178
Cdd:cd01172 108 VDREDDSplsaEEEQRLIERIAE-RLPEADVVI--LSDygkgVLTPRVIEALIAAARELGIPVLVDPK-------GRDYS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 179 FASHAHLIK--ASEEDLALLYPGRDPGEVARGWLN----PRCRLVFVTHGGAGASVHCTHGS-WSRPAdTALPLRDTVGA 251
Cdd:cd01172 178 KYRGATLLTpnEKEAREALGDEINDDDELEAAGEKllelLNLEALLVTLGEEGMTLFERDGEvQHIPA-LAKEVYDVTGA 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15597540 252 GDTFqAATLAylrrldadspAGLAALSREAIDAMLAFAirAAAVTCSRVG 301
Cdd:cd01172 257 GDTV-IATLA----------LALAAGADLEEAAFLANA--AAGVVVGKVG 293
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
30-305 |
1.06e-09 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 58.22 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 30 AGGSPFNVAVGLRRLGVEA---ALFGGlssdYLGARLRRVLEEEGVDCGFL-VPSDAPTTLAMVglDASGSAQYQFRGEG 105
Cdd:COG1105 34 PGGKGINVARVLKALGVDVtalGFLGG----FTGEFIEELLDEEGIPTDFVpIEGETRINIKIV--DPSDGTETEINEPG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 106 cadrqvrlehlPTLD--------GRIRGLHVGSYTLVVT---P--VADTLLA-LVR--RESGRRLVsLD---PNVRldpq 166
Cdd:COG1105 108 -----------PEISeeeleallERLEELLKEGDWVVLSgslPpgVPPDFYAeLIRlaRARGAKVV-LDtsgEALK---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 167 pdidlwrrrvEAFASHAHLIKASEEDLALLY--PGRDPGEV---ARGWLNPRCRLVFVTHGGAGASVHCTHGSWSRPADt 241
Cdd:COG1105 172 ----------AALEAGPDLIKPNLEELEELLgrPLETLEDIiaaARELLERGAENVVVSLGADGALLVTEDGVYRAKPP- 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597540 242 ALPLRDTVGAGDTFQAA-TLAYLRRLDadspaglaalsreaIDAMLAFAIRAAAVTCSRVGPDLP 305
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGfLAGLARGLD--------------LEEALRLAVAAGAAAALSPGTGLP 291
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
28-302 |
7.13e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 52.43 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 28 AIAGGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVPSDAPTTLAMVGLDaSGSAQYQFRGEGCa 107
Cdd:PRK09813 20 AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELH-DNDRVFGDYTEGV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 108 drqvrLEHLPTLDGRIRGLhvGSYTLVVTPV----ADTLLALvrRESGRRlVSLDpnvrLDPQPDIDLWRRRVE----AF 179
Cdd:PRK09813 98 -----MADFALSEEDYAWL--AQYDIVHAAIwghaEDAFPQL--HAAGKL-TAFD----FSDKWDSPLWQTLVPhldyAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 180 ASHahlikaseedlallyPGRDP-------GEVARGwlnprCRLVFVTHGGAGASVHCTHGSWSRPADTAlPLRDTVGAG 252
Cdd:PRK09813 164 ASA---------------PQEDEflrlkmkAIVARG-----AGVVIVTLGENGSIAWDGAQFWRQAPEPV-TVVDTMGAG 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15597540 253 DTFQAATLAylrrldadspaglAALSREAIDAMLAFAIRAAAVTCSRVGP 302
Cdd:PRK09813 223 DSFIAGFLC-------------GWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
123-263 |
7.48e-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: 51.71 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 123 IRGLHVGSYTLVVTPVADtLLALVRResGRRLVSLDPNVRldpqpDIDLWRRRVEAFASHAHLIKASEEDLALLYPGRDP 202
Cdd:cd00287 58 ADAVVISGLSPAPEAVLD-ALEEARR--RGVPVVLDPGPR-----AVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDL 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597540 203 G-----EVARGWLNPRCRLVFVTHGGAGASVhCTHGSWSRPADTALP-LRDTVGAGDTFQAATLAYL 263
Cdd:cd00287 130 EvkeaaEAAALLLSKGPKVVIVTLGEKGAIV-ATRGGTEVHVPAFPVkVVDTTGAGDAFLAALAAGL 195
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
31-263 |
2.29e-07 |
|
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: 51.26 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 31 GGSPFNVAVGLRRLGVEAALFGGLSSDYLGarlRRVLE--EEGVDCGFLVPSDAPTTLAMVGLDASGsaqyqfrgegcaD 108
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIG---IQSLEelESGGDKHTVAWRDKPTRKTLSFIDPNG------------E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 109 RQVRLEHLPTLDGRIRGLHVGSYTLVVTPVAdTLLALVRRESGRRLVSLD--PNVRLDPQPDIDLwrrrveafasHAHLI 186
Cdd:cd01947 101 RTITVPGERLEDDLKWPILDEGDGVFITAAA-VDKEAIRKCRETKLVILQvtPRVRVDELNQALI----------PLDIL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597540 187 KASEEDlallYPGRDPGEVARGwlnPRCRLVFVTHGGAGASVHCTHGSWSRPADTAlPLRDTVGAGDTFQAATLAYL 263
Cdd:cd01947 170 IGSRLD----PGELVVAEKIAG---PFPRYLIVTEGELGAILYPGGRYNHVPAKKA-KVPDSTGAGDSFAAGFIYGL 238
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
30-275 |
2.58e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 48.67 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 30 AGGSpFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGFLVPSD---------APTTLAMVGLDASGS---- 96
Cdd:PLN02341 119 AGGN-CNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLIEGTdagdsssasYETLLCWVLVDPLQRhgfc 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 97 AQYQFrGEGCADRQVRlehlpTLDGRIR-GLHVGSYTLVVTPVADTLLALVRRESGRRLVSLDPNVRLDPQP-------D 168
Cdd:PLN02341 198 SRADF-GPEPAFSWIS-----KLSAEAKmAIRQSKALFCNGYVFDELSPSAIASAVDYAIDVGTAVFFDPGPrgksllvG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 169 IDLWRRRVEAFASHAHLIKASEEDLALLYPGRDPGEVARGWLNPRCRLVFVT-HGGAGASVHCTHGSWSRPADTALPLRD 247
Cdd:PLN02341 272 TPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTKWVVvKMGSKGSILVTRSSVSCAPAFKVNVVD 351
|
250 260
....*....|....*....|....*....
gi 15597540 248 TVGAGDTFQAA-TLAYLRRLDADSPAGLA 275
Cdd:PLN02341 352 TVGCGDSFAAAiALGYIHNLPLVNTLTLA 380
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
11-305 |
6.49e-06 |
|
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: 46.80 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 11 DVFSLESAARSNELGFTAiaGGSPFNVAVGLRRLGVEAA---LFGGLSSDYLgarlRRVLEEEGVDCGFlVPSDAPTTLA 87
Cdd:TIGR03168 17 DGLTPGEVNRVAAVRKDA--GGKGINVARVLARLGAEVVatgFLGGFTGEFI----EALLAEEGIKNDF-VEVKGETRIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 88 MVGLDASGsAQYQFRGEGCadrQVRLEHLPTLDGRIRGLHVGSYTLVVT---P--VADTLLA-LVR--RESGRRLVsLD- 158
Cdd:TIGR03168 90 VKIKESSG-EETELNEPGP---EISEEELEQLLEKLRELLASGDIVVISgslPpgVPPDFYAqLIAiaRKKGAKVI-LDt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 159 --PNVRldpqpdidlwrrrvEAFASHAHLIKASEEDLALLYpGRDPG------EVARGWLNPRCRLVFVTHGGAGA-SVH 229
Cdd:TIGR03168 165 sgEALR--------------EALAAKPFLIKPNHEELEELF-GRELKtleeiiEAARELLDRGAENVLVSLGADGAlLVT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597540 230 CTHGSWSRPAdtALPLRDTVGAGDTFQAA-TLAYLRRLDadspaglaalsreaIDAMLAFAIRAAAVTCSRVGPDLP 305
Cdd:TIGR03168 230 KEGALKATPP--KVEVVNTVGAGDSMVAGfLAGLARGLS--------------LEEALRFAVAAGSAAAFSPGTGLP 290
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
26-265 |
1.90e-05 |
|
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: 45.49 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 26 FTAIAGGSpFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGV----------DCGFLV----PSDAPTTLAMVGL 91
Cdd:cd01944 31 KSYVIGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIeillpprggdDGGCLValvePDGERSFISISGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 92 DASGSAQYQFRGEGCADRQVrlehlptldgrirglHVGSYTLV-VTPVADTLLALVRRESGRRLVSLDPNVRLDPQPDID 170
Cdd:cd01944 110 EQDWSTEWFATLTVAPYDYV---------------YLSGYTLAsENASKVILLEWLEALPAGTTLVFDPGPRISDIPDTI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 171 LwrRRVEAFAShahLIKASEEDLALLYPGRDPGE--VARGWLNPRCRLVFVTHGGAGASVHCTHGSWSRPADTALPLRDT 248
Cdd:cd01944 175 L--QALMAKRP---IWSCNREEAAIFAERGDPAAeaSALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGFKVKAVDT 249
|
250
....*....|....*..
gi 15597540 249 VGAGDTFQAATLAYLRR 265
Cdd:cd01944 250 IGAGDTHAGGMLAGLAK 266
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
160-303 |
5.27e-05 |
|
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: 43.93 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 160 NVRLDPQP---DIDLWRRRVEAF--ASHAHLIKASEeDLALLYPGRDPGEVARGwLNPRCR---LVFVTHGGAGAS---- 227
Cdd:cd01939 152 NNRRPEIRitiSVEVEKPREELLelAAYCDVVFVSK-DWAQSRGYKSPEECLRG-EGPRAKkaaLLVCTWGDQGAGalgp 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 228 ----VHCthgswsrpaDTALPLR--DTVGAGDTFQAATLAYLrrldADSPAGLAalsrEAIDamlaFAIRAAAVTCSRVG 301
Cdd:cd01939 230 dgeyVHS---------PAHKPIRvvDTLGAGDTFNAAVIYAL----NKGPDDLS----EALD----FGNRVASQKCTGVG 288
|
..
gi 15597540 302 PD 303
Cdd:cd01939 289 FD 290
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
30-301 |
2.25e-04 |
|
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: 42.13 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 30 AGGSPFNVAVGLRRLGVEAALFGGLSSDyLGARLRRVLEEEGVDCGFL-VPSDAPTTLAMVGLDAsgsAQYQFRGEGCad 108
Cdd:cd01164 35 AGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVeVAGETRINVKIKEEDG---TETEINEPGP-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 109 rQVRLEHLPTLDGRIRGLhVGSYTLVV--------TPvADTLLALVR--RESGRRLVsLD---PNVRldpqpdidlwrrr 175
Cdd:cd01164 109 -EISEEELEALLEKLKAL-LKKGDIVVlsgslppgVP-ADFYAELVRlaREKGARVI-LDtsgEALL------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 176 vEAFASHAHLIKASEEDLALLYpGR------DPGEVARGWLNPRCRLVFVTHGGAGAsVHCT-HGSW-SRPAdtALPLRD 247
Cdd:cd01164 172 -AALAAKPFLIKPNREELEELF-GRplgdeeDVIAAARKLIERGAENVLVSLGADGA-LLVTkDGVYrASPP--KVKVVS 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15597540 248 TVGAGDTFQAATLAYLrrldadspaglaALSREAIDAmLAFAIRAAAVTCSRVG 301
Cdd:cd01164 247 TVGAGDSMVAGFVAGL------------AQGLSLEEA-LRLAVAAGSATAFSPG 287
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|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
30-305 |
2.50e-04 |
|
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: 42.19 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 30 AGGSPFNVAVGLRRLGVEAA---LFGGLSSDYLGARLRrvleEEGVDCGFlVPSDAPTTLAmVGLDASGSAQYQFRGEGC 106
Cdd:TIGR03828 34 AGGKGINVSRVLKNLGVDVValgFLGGFTGDFIEALLR----EEGIKTDF-VRVPGETRIN-VKIKEPSGTETKLNGPGP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 107 ADRQVRLEHLPTldgRIRGLHVGSYTLVV---------TPVADTLLALVRrESGRRLV--SLDPNVRldpqpdidlwrrr 175
Cdd:TIGR03828 108 EISEEELEALLE---KLRAQLAEGDWLVLsgslppgvpPDFYAELIALAR-EKGAKVIldTSGEALR------------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597540 176 vEAFASHAHLIKASEEDLALLYpGRDPG------EVARGWLNPRCRLVFVTHGGAGASVHCTHGSW-SRPAdtALPLRDT 248
Cdd:TIGR03828 171 -DGLKAKPFLIKPNDEELEELF-GRELKtleeiiEAARELLDLGAENVLISLGADGALLVTKEGALfAQPP--KGEVVST 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597540 249 VGAGDTFQAATLAYLRRldadspaglaALSREAIdamLAFAIRAAAVTCSRVGPDLP 305
Cdd:TIGR03828 247 VGAGDSMVAGFLAGLES----------GLSLEEA---LRLAVAAGSAAAFSEGTGLP 290
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
31-96 |
2.15e-03 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 39.34 E-value: 2.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597540 31 GGSPFNVAVGLRRLGVEAALFGGLSSDYLGARLRRVLEEEGVDCGF-LVPSDAPTTLAMVGLDASGS 96
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFvSRTENSSTGLAMIFVDTKTG 118
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