|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
7-644 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1037.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 7 AKHAPLDIITIGRASVDLYGQQIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVC 86
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 87 VDGLKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKA 166
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RGGKVVFDIDYRPNLWGLAGHAEGFERYVKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIV 246
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 247 LKRGAMGCIVYDGPISDDLEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEY 326
Cdd:COG3892 241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 327 PTFEELRFFLKNGSKHMALRKDEAINHIHWATTRRRDIPALMALACDHRVQLEDVAAKAGADVSRIPAFKVLTVKAAARV 406
Cdd:COG3892 321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 407 AAGRAG---YGMLLDEKYGRDAMFEFARHPFtWLGRPVELPGSRPLRFEFSQDIGSQLVEWPVDHCIKCLCFYHPDDPAA 483
Cdd:COG3892 401 AAGAGLrggIGVLIDDRYGQDALNAATGRGW-WIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDDPAE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 484 LKEEQQQKLRGLFEAARKVGRELLVEIIAGKHGKLDDTTIPRALEELYALGIKPDWWKLEPQaSANAWARIEAVILKHDP 563
Cdd:COG3892 480 LRLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPM-SAAAWQAIDALIAERDP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 564 WCRGVVLLGLEAPQDELEAAFAATAKAPIVRGFAVGRTIFINAAEQWLAGRMSDDEAVADMASRFEKLTDAWLAARDRKA 643
Cdd:COG3892 559 YCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQAAA 638
|
.
gi 493369371 644 A 644
Cdd:COG3892 639 A 639
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
11-336 |
1.65e-147 |
|
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: 429.71 E-value: 1.65e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 11 PLDIITIGRASVDLYGQQIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGL 90
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 91 KTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKARGGK 170
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 171 VVFDIDYRPNLWGlaghaegferyvKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLKRG 250
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 251 AMGCIVYDGPisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEYPTFE 330
Cdd:TIGR04382 229 PEGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 493369371 331 ELRFFL 336
Cdd:TIGR04382 304 ELEAFL 309
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
331-639 |
8.11e-147 |
|
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various prokaryotic carbohydrate kinases, has no known function.
Pssm-ID: 430888 Cd Length: 310 Bit Score: 427.85 E-value: 8.11e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 331 ELRFFLKNGSKHMALRKDEAINHIHWATTRRRDIPALMALACDHRVQLEDVAAKAGADVSRIPAFKVLTVKAAARVAAGR 410
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 411 ---AGYGMLLDEKYGRDAMFEFARHPFtWLGRPVELPGSRPLRFEFSQDIGSQLVEWPVDHCIKCLCFYHPDDPAALKEE 487
Cdd:pfam09863 81 glqGGAGVLIDGRYGQDALNAATGRGW-WIGRPIELPGSRPLRFEHGRSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 488 QQQKLRGLFEAARKVGRELLVEIIAGKHGKLDDTTIPRALEELYALGIKPDWWKLEPQASAnAWARIEAVILKHDPWCRG 567
Cdd:pfam09863 160 QEAQLRELYDACRKSGHELLLEVIPPKDGPVDDETYARAIRRFYNLGVKPDWWKLPPLSAA-AWEQIDALIEERDPYCRG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493369371 568 VVLLGLEAPQDELEAAFAATAKAPIVRGFAVGRTIFINAAEQWLAGRMSDDEAVADMASRFEKLTDAWLAAR 639
Cdd:pfam09863 239 VVILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
13-320 |
1.46e-85 |
|
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: 269.83 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 13 DIITIGRASVDLYGQQIGsRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKT 92
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 93 DPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSR-PNSDAAQRKAIRIMKARGGKV 171
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALsESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 172 VFDIDYRPNLWGLaghaegferyvksDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRS--LSSATIVLKR 249
Cdd:cd01166 160 SFDLNYRPKLWSA-------------EEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493369371 250 GAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01166 227 GAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRP 291
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-332 |
9.90e-84 |
|
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: 265.21 E-value: 9.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 13 DIITIGRASVDLYGQ----QIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVD 88
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 89 GLKTDPDRLTALVLLSVEEEGVSPMIFYRtdCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKARG 168
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 169 GKVVFDIDYRPNLWglaghaegferyvksDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLK 248
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 249 RGAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEYPT 328
Cdd:COG0524 224 LGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 493369371 329 FEEL 332
Cdd:COG0524 298 REEV 301
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
14-319 |
1.46e-47 |
|
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: 168.97 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 14 IITIGRASVDLYGQQIGSRLEditsFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTD 93
Cdd:cd01167 2 VVCFGEALIDFIPEGSGAPET----FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 94 PDRLTALVLLSVEEEGVSPMIFYRTDCADMALsEDDIDEAFIASARaIVVTGTH-FSRPNSDAAQRKAIRIMKARGGKVV 172
Cdd:cd01167 78 PAAPTTLAFVTLDADGERSFEFYRGPAADLLL-DTELNPDLLSEAD-ILHFGSIaLASEPSRSALLELLEAAKKAGVLIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 173 FDIDYRPNLWGlaghaegferyvKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLKRGAM 252
Cdd:cd01167 156 FDPNLRPPLWR------------DEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGAD 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493369371 253 GCIVYDGpisddledGVVG--KGFPIEVYNVLGAGDAFMSGFLRG-WLGGESFATAATW------ANACGAFAVSR 319
Cdd:cd01167 224 GALLYTK--------GGVGevPGIPVEVVDTTGAGDAFVAGLLAQlLSRGLLALDEDELaealrfANAVGALTCTK 291
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
13-319 |
5.11e-46 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 164.82 E-value: 5.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 13 DIITIGRASVDLYGQQIGSRLEDIT--SFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGL 90
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRvsTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 91 KTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGThFSRPNSDAAQRKAIRIMKARGgk 170
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGS-LPLGLPEATLEELIEAAKNGG-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 171 vVFDIDYRPNLWGLAGhaegferyvksdrvsaQLKTVLPHCDLIVGTEEEIMIASGA-----DDCLSALKTIRSLSSATI 245
Cdd:pfam00294 158 -TFDPNLLDPLGAARE----------------ALLELLPLADLLKPNEEELEALTGAklddiEEALAALHKLLAKGIKTV 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493369371 246 VLKRGAMGCIVYDGpisddleDGVVG--KGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:pfam00294 221 IVTLGADGALVVEG-------DGEVHvpAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQK 289
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
17-318 |
1.29e-31 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 125.05 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 17 IGRASVDLYGqqigsrlEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDR 96
Cdd:PRK09434 8 LGDAVVDLIP-------EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 97 LTALVLLSVEEEGVSPMIFYRTDCADMALSEDDI-----DEAFIASARAIVvtgthfSRPNSDAAqRKAIRIMKARGGKV 171
Cdd:PRK09434 81 RTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLppfrqGEWLHLCSIALS------AEPSRSTT-FEAMRRIKAAGGFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 172 VFDIDYRPNLWglaghaegferyvksdRVSAQLKTVLPH----CDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVL 247
Cdd:PRK09434 154 SFDPNLREDLW----------------QDEAELRECLRQalalADVVKLSEEELCFLSGTSQLEDAIYALADRYPIALLL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493369371 248 -KRGAMGCIVYDGPISDDledgVVGKgfPIEVYNVLGAGDAFMSGFLRG------WLGGESFATAATWANACGAFAVS 318
Cdd:PRK09434 218 vTLGAEGVLVHTRGQVQH----FPAP--SVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATT 289
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
30-341 |
1.09e-28 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 117.03 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 30 GSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEG 109
Cdd:PLN02323 29 GVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 110 VSPMIFYRTDCADMALSEDDIDEAFIASARAIvvtgtHF------SRPnSDAAQRKAIRIMKARGGKVVFDIDYRPNLWG 183
Cdd:PLN02323 109 EREFMFYRNPSADMLLRESELDLDLIRKAKIF-----HYgsisliTEP-CRSAHLAAMKIAKEAGALLSYDPNLRLPLWP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 184 LAGHAEgferyvksdrvsAQLKTVLPHCDLIVGTEEEIMIASGADDCL--SALKTIRSLSSATIVLKrGAMGCIVYDGPI 261
Cdd:PLN02323 183 SAEAAR------------EGIMSIWDEADIIKVSDEEVEFLTGGDDPDddTVVKLWHPNLKLLLVTE-GEEGCRYYTKDF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 262 SddledGVVGkGFPIEVYNVLGAGDAFMSGFL------RGWLGGES-FATAATWANACGAFAVSRLLCAPEYPTFEELRF 334
Cdd:PLN02323 250 K-----GRVE-GFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFANACGAITTTERGAIPALPTKEAVLK 323
|
....*..
gi 493369371 335 FLKNGSK 341
Cdd:PLN02323 324 LLKKAVA 330
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
41-319 |
4.21e-27 |
|
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: 111.25 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 41 KSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEGVSPMIFYRtdc 120
Cdd:cd01942 33 REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYP--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 121 ADMALSEDDIDEAFIASARAIvvtgtHFSrpNSDAAQRKAiRIMKARGGKVVFDidyrPnlwglaGHAEgferyvkSDRV 200
Cdd:cd01942 110 GAMDELEPNDEADPDGLADIV-----HLS--SGPGLIELA-RELAAGGITVSFD----P------GQEL-------PRLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 201 SAQLKTVLPHCDLIVGTEEEIMIASGaddcLSALKT-IRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGKGFP-IEV 278
Cdd:cd01942 165 GEELEEILERADILFVNDYEAELLKE----RTGLSEaELASGVRVVVVTLGPKGAIVFED------GEEVEVPAVPaVKV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493369371 279 YNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:cd01942 235 VDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVER 275
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
13-328 |
2.46e-26 |
|
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: 109.18 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 13 DIITIGRASVDLYgqqigSRLEDI---------TSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKRE 83
Cdd:cd01174 1 KVVVVGSINVDLV-----TRVDRLpkpgetvlgSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 84 GVCVDGLKTDPDRLTALVLLSVEEEG-----VSPMifyrtdcADMALSEDDIDEA--FIASARAIVV---TgthfsrpnS 153
Cdd:cd01174 76 GIDVSYVEVVVGAPTGTAVITVDESGenrivVVPG-------ANGELTPADVDAAleLIAAADVLLLqleI--------P 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 154 DAAQRKAIRIMKARGGKVVFDidyrpnlwgLAGhaegferyvksdrVSAQLKTVLPHCDLIVGTEEEIMIASGA-----D 228
Cdd:cd01174 141 LETVLAALRAARRAGVTVILN---------PAP-------------ARPLPAELLALVDILVPNETEAALLTGIevtdeE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 229 DCLSALKTIRSLSSATIVLKRGAMGCIVYDGPISDDLEdgvvgkGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATW 308
Cdd:cd01174 199 DAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVP------AFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRF 272
|
330 340
....*....|....*....|
gi 493369371 309 ANACGAFAVSRLLCAPEYPT 328
Cdd:cd01174 273 ANAAAALSVTRPGAQPSIPT 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
11-320 |
3.48e-22 |
|
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: 97.68 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 11 PLDIITIGRASVDL-----------YGQQIGS-------RLEDITSFAKSV---GGCPANISVGTARLGLRSALLTRVGD 69
Cdd:cd01168 1 RYDVLGLGNALVDIlaqvddaflekLGLKKGDmiladmeEQEELLAKLPVKyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 70 EQMGRFIREQLKREGVCVDgLKTDPDRLTA--LVLLSVEEEgvspmifyRTDCADMA----LSEDDIDEAFIASARAIVV 143
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTR-YQVQPDGPTGtcAVLVTPDAE--------RTMCTYLGaaneLSPDDLDWSLLAKAKYLYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 144 TGTHFsRPNSDAAQrKAIRIMKARGGKVVFDIdyrpnlwglaghAEGFEryvkSDRVSAQLKTVLPHCDLIVGTEEEIMI 223
Cdd:cd01168 152 EGYLL-TVPPEAIL-LAAEHAKENGVKIALNL------------SAPFI----VQRFKEALLELLPYVDILFGNEEEAEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 224 ASGADDCLS---ALKTIRSLSSaTIVLKRGAMGCIVYDGpisddledgvvGKGFPIEVYNV------LGAGDAFMSGFLR 294
Cdd:cd01168 214 LAEAETTDDleaALKLLALRCR-IVVITQGAKGAVVVEG-----------GEVYPVPAIPVekivdtNGAGDAFAGGFLY 281
|
330 340
....*....|....*....|....*.
gi 493369371 295 GWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01168 282 GLVQGEPLEECIRLGSYAAAEVIQQL 307
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
16-318 |
6.32e-18 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 84.02 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 16 TIGRASVDLYgQQIGSRLEditsfaksvGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPD 95
Cdd:PRK09813 5 TIGDNCVDIY-PQLGKAFS---------GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 96 RlTALVLLSVE---------EEGVspmifyrtdCADMALSEDDIDeaFIASaRAIVVTGThFSRPNSDAAQrkairiMKA 166
Cdd:PRK09813 75 V-TAQTQVELHdndrvfgdyTEGV---------MADFALSEEDYA--WLAQ-YDIVHAAI-WGHAEDAFPQ------LHA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RGGKVVFDIDYRPN--LWglaghaegferyvksdrvsaqlKTVLPHCDLIVGTeeeimiASGADDCL-SALKTIRSLSSA 243
Cdd:PRK09813 135 AGKLTAFDFSDKWDspLW----------------------QTLVPHLDYAFAS------APQEDEFLrLKMKAIVARGAG 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493369371 244 TIVLKRGAMGCIVYDGpisDDLEDGVVgkgFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVS 318
Cdd:PRK09813 187 VVIVTLGENGSIAWDG---AQFWRQAP---EPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQ 255
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
14-315 |
7.70e-18 |
|
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: 83.94 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 14 IITIGRASVDLYGQQIGSRleditsfaksVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTD 93
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKMY----------PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 94 P-DRLTALVLLS-------VEEEGVspmifyrtdCADMALSEDDIdeAFIASARaIVVTGTHfSRPNSdaaQRKAIRIMK 165
Cdd:cd01940 72 EgENAVADVELVdgdrifgLSNKGG---------VAREHPFEADL--EYLSQFD-LVHTGIY-SHEGH---LEKALQALV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 166 ARGGKVVFDIDYRpnlwglaghaegferyvksdRVSAQLKTVLPHCDlivgteeeIMIASGADD----CLSALKTIRSLS 241
Cdd:cd01940 136 GAGALISFDFSDR--------------------WDDDYLQLVCPYVD--------FAFFSASDLsdeeVKAKLKEAVSRG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 242 SATIVLKRGAMGCIVYDGpiSDDLEDGVVgkgfPIEVYNVLGAGDAFMSGFLRGWL-GGESFATAA-----TWANAC--- 312
Cdd:cd01940 188 AKLVIVTRGEDGAIAYDG--AVFYSVAPR----PVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMrqgaqFAAKTCghe 261
|
...
gi 493369371 313 GAF 315
Cdd:cd01940 262 GAF 264
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
13-332 |
4.84e-16 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 79.78 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 13 DIITIGRASVDLYG-----QQIGSRLEDiTSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCV 87
Cdd:PTZ00292 17 DVVVVGSSNTDLIGyvdrmPQVGETLHG-TSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 88 DGLKTDPDRLTALVLLSVEEE-GVSPMIFyrTDCADMALSEDDIDEAF--IASARAIVVTGTHFSRPNSDAaqrkAIRIM 164
Cdd:PTZ00292 96 SFVSRTENSSTGLAMIFVDTKtGNNEIVI--IPGANNALTPQMVDAQTdnIQNICKYLICQNEIPLETTLD----ALKEA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 165 KARGGKVVFDIDYRPNLWGLaghaegferyvksdrvsAQLKTVLPHCDLIVGTEEEIMIASGAD--DCLSALKTIRS--- 239
Cdd:PTZ00292 170 KERGCYTVFNPAPAPKLAEV-----------------EIIKPFLKYVSLFCVNEVEAALITGMEvtDTESAFKASKElqq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 240 LSSATIVLKRGAMGC-IVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVS 318
Cdd:PTZ00292 233 LGVENVIITLGANGClIVEKE------NEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVT 306
|
330
....*....|....
gi 493369371 319 RLLCAPEYPTFEEL 332
Cdd:PTZ00292 307 RHGTQSSYPHPSEL 320
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
37-320 |
2.77e-15 |
|
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: 76.56 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 37 TSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEGVSPMIFY 116
Cdd:cd01945 29 TDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 117 rtdCADMALSEDDIDEAFIASARAIVVTGTHfsrpnSDAAQrKAIRIMKARGGKVVFDIDyrpnlwglAGHAEGFERyvk 196
Cdd:cd01945 109 ---AIDTQAAPDSLPDAILGGADAVLVDGRQ-----PEAAL-HLAQEARARGIPIPLDLD--------GGGLRVLEE--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 197 sdrvsaqlktVLPHCDLIVGTEEEIMIASGADDcLSALKTIRSLSSATIVLKRGAMGCIVYDgpisddlEDGVVGKG--F 274
Cdd:cd01945 169 ----------LLPLADHAICSENFLRPNTGSAD-DEALELLASLGIPFVAVTLGEAGCLWLE-------RDGELFHVpaF 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 493369371 275 PIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGL 276
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
14-318 |
5.05e-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: 70.04 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 14 IITIGRASVDLYGQqIGSRLEDITSFA----KSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDG 89
Cdd:cd01941 2 IVVIGAANIDLRGK-VSGSLVPGTSNPghvkQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 90 LKtDPDRLTALVLLSVEEEGVSPMIFyrtdcADMA----LSEDDIDEA--FIASARAIVVTGthfsrpN--SDAAQRkai 161
Cdd:cd01941 81 IV-FEGRSTASYTAILDKDGDLVVAL-----ADMDiyelLTPDFLRKIreALKEAKPIVVDA------NlpEEALEY--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 162 rIMKARGGKVVfdidyrpnlwglaghAEGFERyVKSDRVSAqLKTVLPHCDLIVGTEEEI-----MIASGADDCLSALKT 236
Cdd:cd01941 146 -LLALAAKHGV---------------PVAFEP-TSAPKLKK-LFYLLHAIDLLTPNRAELealagALIENNEDENKAAKI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 237 IRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGKGFPI----EVYNVLGAGDAFMSGFLRGWLGGESFATAATWANAC 312
Cdd:cd01941 208 LLLPGIKNVIVTLGAKGVLLSSR------EGGVETKLFPApqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAA 281
|
....*.
gi 493369371 313 GAFAVS 318
Cdd:cd01941 282 AALTLE 287
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
14-319 |
1.51e-12 |
|
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: 68.21 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 14 IITIGRASVDLYGQ-----QIGSRLEdITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVC-V 87
Cdd:cd01947 2 IAVVGHVEWDIFLSldappQPGGISH-SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKhT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 88 DGLKTDPDRLTALVLLSVEEEGVSpmIFYRTDCADMALSE-DDIDEAFIASARAivvtgthfsrpnsDAAQRKAIRIMKA 166
Cdd:cd01947 81 VAWRDKPTRKTLSFIDPNGERTIT--VPGERLEDDLKWPIlDEGDGVFITAAAV-------------DKEAIRKCRETKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RggkvvfdidyrpnLWGLAGHAEgferyvksdrvSAQLKTVLPHCDLIVGTEEEIMIASGADDclSALKTIRslssaTIV 246
Cdd:cd01947 146 V-------------ILQVTPRVR-----------VDELNQALIPLDILIGSRLDPGELVVAEK--IAGPFPR-----YLI 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493369371 247 LKRGAMGCIVYDGpisddLEDGVVgKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:cd01947 195 VTEGELGAILYPG-----GRYNHV-PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
|
|
| PLN02967 |
PLN02967 |
kinase |
7-182 |
8.24e-12 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 68.15 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 7 AKHApldIITIGRASVDLYGQQIGSRLEDI----TSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKR 82
Cdd:PLN02967 205 AQHA---FVPSGRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 83 EGVCVDGLKTDPDRLTALVLLSVEEEGVSPMIFYRTdCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIR 162
Cdd:PLN02967 282 NKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIK 360
|
170 180
....*....|....*....|
gi 493369371 163 IMKARGGKVVFDIDYRPNLW 182
Cdd:PLN02967 361 ISKKLGGVIFYDLNLPLPLW 380
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
49-325 |
1.24e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 65.93 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 49 NISVGTARLGLRSALLTRVGDEQmGRFIREQLKREGVCVDGLKTDPD-RLTalVLLSVEEEGVSPMIFYRTdcadMALSE 127
Cdd:COG1105 40 NVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGEtRIN--IKIVDPSDGTETEINEPG----PEISE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 128 DDIDEAF------IASARAIVVTGthfSRPN--SDAAQRKAIRIMKARGGKVVFDIDyrpnlwglaGHAegferyvksdr 199
Cdd:COG1105 113 EELEALLerleelLKEGDWVVLSG---SLPPgvPPDFYAELIRLARARGAKVVLDTS---------GEA----------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 200 vsaqLKTVLPHC-DLIVGTEEEIMIASG-----ADDCLSALKTIRSLSSATIVLKRGAMGCIVYDgpisddlEDGVV-GK 272
Cdd:COG1105 170 ----LKAALEAGpDLIKPNLEELEELLGrpletLEDIIAAARELLERGAENVVVSLGADGALLVT-------EDGVYrAK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 493369371 273 GFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL---LCAPE 325
Cdd:COG1105 239 PPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPgtgLPDRE 294
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
14-333 |
2.39e-11 |
|
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: 65.27 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 14 IITIGRASVD--LYGQQIGSRLE------DITSFAKSVGGCpANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGV 85
Cdd:cd01172 2 VLVVGDVILDeyLYGDVERISPEapvpvvKVEREEIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 86 CVDGLkTDPDRLT---------ALVLLSVEEEGVSPMifyrtdcadMALSEDDIDEAF---IASARAIVVT----GThFS 149
Cdd:cd01172 81 DTDGI-VDEGRPTttktrviarNQQLLRVDREDDSPL---------SAEEEQRLIERIaerLPEADVVILSdygkGV-LT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 150 RPNSDAAQRKAirimKARGGKVVFDidyrpnlwgLAGHaeGFERYvksdrvsaqlktvlPHCDLIVGTEEEIMIASGADD 229
Cdd:cd01172 150 PRVIEALIAAA----RELGIPVLVD---------PKGR--DYSKY--------------RGATLLTPNEKEAREALGDEI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 230 C-----LSALKTIRSLSSATIVL-KRGAMGCIVYDGpisddlEDGVVGkgFP---IEVYNVLGAGDAFMSGFLRGWLGGE 300
Cdd:cd01172 201 NdddelEAAGEKLLELLNLEALLvTLGEEGMTLFER------DGEVQH--IPalaKEVYDVTGAGDTVIATLALALAAGA 272
|
330 340 350
....*....|....*....|....*....|...
gi 493369371 301 SFATAATWANACGAFAVSRLLCAPeyPTFEELR 333
Cdd:cd01172 273 DLEEAAFLANAAAGVVVGKVGTAP--VTPKELL 303
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
49-319 |
7.83e-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: 63.75 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 49 NISVGTARLGLRSALLTRVGDEQmGRFIREQLKREGVCVDGLKTDPD-RL-TALVLLSVEEegvspmifYRTDCADMALS 126
Cdd:TIGR03168 40 NVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGEtRInVKIKESSGEE--------TELNEPGPEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 127 EDDIDE------AFIASARAIVVTGthfSRPN--SDAAQRKAIRIMKARGGKVVFD---------IDYRPNLwglaghae 189
Cdd:TIGR03168 111 EEELEQlleklrELLASGDIVVISG---SLPPgvPPDFYAQLIAIARKKGAKVILDtsgealreaLAAKPFL-------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 190 gferyVKSDRvsAQLKTvlpHCDLIVGTEEEImiasgaddcLSALKTIRSLSSATIVLKRGAMGCIVYDGpisddlEDGV 269
Cdd:TIGR03168 180 -----IKPNH--EELEE---LFGRELKTLEEI---------IEAARELLDRGAENVLVSLGADGALLVTK------EGAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 493369371 270 VGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:TIGR03168 235 KATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFS 284
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
130-297 |
8.04e-11 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 61.73 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 130 IDEAFIASARAIVVTGTHFSRpnsdAAQRKAIRIMKARGGKVVFDIDYRPNLWglaghaegferyvksdrVSAQLKTVLP 209
Cdd:cd00287 50 GVSVTLVGADAVVISGLSPAP----EAVLDALEEARRRGVPVVLDPGPRAVRL-----------------DGEELEKLLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 210 HCDLIVGTEEEIMIASGADD-----CLSALKTIRSLSSATIVLKRGAMGCIVYDGPisddlEDGVVGKGFPIEVYNVLGA 284
Cdd:cd00287 109 GVDILTPNEEEAEALTGRRDlevkeAAEAAALLLSKGPKVVIVTLGEKGAIVATRG-----GTEVHVPAFPVKVVDTTGA 183
|
170
....*....|...
gi 493369371 285 GDAFMSGFLRGWL 297
Cdd:cd00287 184 GDAFLAALAAGLA 196
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
48-333 |
8.51e-11 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 63.68 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 48 ANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTAL---------VLLSVEEEGVSPmifyrt 118
Cdd:COG2870 59 ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTktrviaggqQLLRLDFEDRFP------ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 119 dcadmaLSEDDID------EAFIASARAIVV--------TGTHFsrpnsdaaqRKAIRIMKARGGKVVFD------IDYR 178
Cdd:COG2870 133 ------LSAELEArllaalEAALPEVDAVILsdygkgvlTPELI---------QALIALARAAGKPVLVDpkgrdfSRYR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 179 ------PNLwglaghAEgFERYVKSDRVsaqlktvlphcdlivgTEEEIMIAsgaddclsALKTIRSLSSATIVLKRGAM 252
Cdd:COG2870 198 gatlltPNL------KE-AEAAVGIPIA----------------DEEELVAA--------AAELLERLGLEALLVTRGEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 253 GCIVYDgpisddlEDGVVgKGFPI---EVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPeyPTF 329
Cdd:COG2870 247 GMTLFD-------ADGPP-HHLPAqarEVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTAT--VSP 316
|
....
gi 493369371 330 EELR 333
Cdd:COG2870 317 EELL 320
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
44-314 |
5.39e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 62.16 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 44 GGCpaNISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPD-----RLTALVLLS-VEEEGVSPMIF-Y 116
Cdd:PLN02341 121 GNC--NFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLIEGTDagdssSASYETLLCwVLVDPLQRHGFcS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 117 RTD-CADMALS-----EDDIDEAfIASARAIVVTGTHFSRPNSDAAQrKAIRIMKARGGKVVFDIDYRpnlwglaghaeG 190
Cdd:PLN02341 199 RADfGPEPAFSwisklSAEAKMA-IRQSKALFCNGYVFDELSPSAIA-SAVDYAIDVGTAVFFDPGPR-----------G 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 191 FERYVKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSAT--IVLKRGAMGCIVYDgpisddlEDG 268
Cdd:PLN02341 266 KSLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVT-------RSS 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 493369371 269 VVGKG-FPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGA 314
Cdd:PLN02341 339 VSCAPaFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
44-320 |
7.62e-10 |
|
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: 60.24 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 44 GGCPANISVGTARLGLRSALLTRVGDEqMGRFIREQLKREGVCVDGLKTDPDRLTALVLlsVEEEGVSpmifYRTDCADM 123
Cdd:cd01164 36 GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKI--KEEDGTE----TEINEPGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 124 ALSEDDIdEAFIASARAIVVTGTHF----SRPNS--DAAQRKAIRIMKARGGKVVFDIDYRPNLWGLAGHAegferyvks 197
Cdd:cd01164 109 EISEEEL-EALLEKLKALLKKGDIVvlsgSLPPGvpADFYAELVRLAREKGARVILDTSGEALLAALAAKP--------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 198 drvsaqlktvlphcDLIVGTEEEIMIASGA-----DDCLSALKTIRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGK 272
Cdd:cd01164 179 --------------FLIKPNREELEELFGRplgdeEDVIAAARKLIERGAENVLVSLGADGALLVTK------DGVYRAS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 493369371 273 GFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01164 239 PPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSP 286
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
14-332 |
1.60e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 59.62 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 14 IITIGRASVDLYGQQIGSrlediTSFAKS--------VGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGV 85
Cdd:PRK09850 7 VVIIGSANIDVAGYSHES-----LNYADSnpgkikftPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 86 CVDGLKTDPDRLTALVLLSVEEEGvsPMIfyrTDCADMALSeDDIDEAFIASARAIVvtgthfsrpnsdaaqrkairimk 165
Cdd:PRK09850 82 YVDKCLIVPGENTSSYLSLLDNTG--EML---VAINDMNIS-NAITAEYLAQHREFI----------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 166 aRGGKVVF---DIDYRPNLWGL--AGHAEGFERYVKS-------DRVSaQLKTVLPHcDLIVGTEEEIMIaSGADDCLSA 233
Cdd:PRK09850 133 -QRAKVIVadcNISEEALAWILdnAANVPVFVDPVSAwkcvkvrDRLN-QIHTLKPN-RLEAETLSGIAL-SGREDVAKV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 234 LKTIRSLSSATIVLKRGAMGciVYDGPISddledGVVGKGFPIE--VYNVLGAGDAFMSGFLRGWLGGESFATAATWANA 311
Cdd:PRK09850 209 AAWFHQHGLNRLVLSMGGDG--VYYSDIS-----GESGWSAPIKtnVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQG 281
|
330 340
....*....|....*....|.
gi 493369371 312 CGAFAVsrllcAPEYPTFEEL 332
Cdd:PRK09850 282 CSSMAL-----SCEYTNNPDL 297
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
39-182 |
3.45e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 59.54 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 39 FAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVE-EEGVSPMIFYR 117
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKfRDGGKMVAETV 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493369371 118 TDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKARGGKVVFDIDYRPNLW 182
Cdd:PLN02543 247 KEAAEDSLLASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLW 311
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
44-336 |
5.13e-09 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 57.96 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 44 GGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEG-----VSPMifyrt 118
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGensigIHAG----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 119 dcADMALSEDDID--EAFIASARAIVVtgtHFSRPNSDAAqrKAIRIMKARGGKVVFDidyrPnlwglAGHAEgferyvk 196
Cdd:PRK11142 114 --ANAALTPALVEahRELIANADALLM---QLETPLETVL--AAAKIAKQHGTKVILN----P-----APARE------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 197 sdrVSAQLktvLPHCDLIVGTEEEIMIASG-----ADDCLSALKTIRSLSSATIVLKRGAMGciVYdgpISDDLEDGVVg 271
Cdd:PRK11142 171 ---LPDEL---LALVDIITPNETEAEKLTGirvedDDDAAKAAQVLHQKGIETVLITLGSRG--VW---LSENGEGQRV- 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493369371 272 KGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEYPTFEELRFFL 336
Cdd:PRK11142 239 PGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
13-301 |
6.15e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 58.67 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 13 DIITIGRASVDLYG----------------------QQIGSRLE--DITSFAKSVGGCPANISVGTARLGLRS------- 61
Cdd:PLN02813 71 DVLGLGQAMVDFSGmvddeflerlglekgtrkvinhEERGKVLRalDGCSYKASAGGSLSNTLVALARLGSQSaagpaln 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 62 -ALLTRVGDEQMGRFIREQLKREGVCVDGlKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEdDIDEAfIASARA 140
Cdd:PLN02813 151 vAMAGSVGSDPLGDFYRTKLRRANVHFLS-QPVKDGTTGTVIVLTTPDAQRTMLSYQGTSSTVNYDS-CLASA-ISKSRV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 141 IVVTGTHFSRPNSDAAQRKAIRIMKARGGKVVF---DID----YRPNLWGLAGHAEGFeRYVKSDRVSAQlktvlphCDL 213
Cdd:PLN02813 228 LVVEGYLWELPQTIEAIAQACEEAHRAGALVAVtasDVScierHRDDFWDVMGNYADI-LFANSDEARAL-------CGL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 214 ivGTEEEIMIASGADDCLSALKTIRSLSSATIVlkrGAMGCIVYDGPisddledgvvgkgFPIEVYNVLGAGDAFMSGFL 293
Cdd:PLN02813 300 --GSEESPESATRYLSHFCPLVSVTDGARGSYI---GVKGEAVYIPP-------------SPCVPVDTCGAGDAYAAGIL 361
|
....*...
gi 493369371 294 RGWLGGES 301
Cdd:PLN02813 362 YGLLRGVS 369
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
37-319 |
6.72e-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: 57.43 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 37 TSFAKSVGGCpANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSveeEGVSPMIFY 116
Cdd:cd01944 29 KSKSYVIGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALV---EPDGERSFI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 117 RTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPN-SDAAQRKAIRIMKARggkVVFDIDYRPNLWGLAGHaegferyv 195
Cdd:cd01944 105 SISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENaSKVILLEWLEALPAG---TTLVFDPGPRISDIPDT-------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 196 ksdrvsaQLKTVLPHCDLIVGTEEEIMIASGADDcLSALKTIRSLSS---ATIVLKRGAMGCIVYDGpisdDLEDGVVgK 272
Cdd:cd01944 174 -------ILQALMAKRPIWSCNREEAAIFAERGD-PAAEASALRIYAktaAPVVVRLGSNGAWIRLP----DGNTHII-P 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 493369371 273 GFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:cd01944 241 GFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTR 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
161-319 |
2.16e-08 |
|
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: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 161 IRIMKARGGKVVFD---------IDYRPNLwglaghaegferyVKSDRvsAQLKTvlpHCDLIVGTEEEImiasgaddcL 231
Cdd:TIGR03828 150 IALAREKGAKVILDtsgealrdgLKAKPFL-------------IKPND--EELEE---LFGRELKTLEEI---------I 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 232 SALKTIRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANA 311
Cdd:TIGR03828 203 EAARELLDLGAENVLISLGADGALLVTK------EGALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVA 276
|
....*...
gi 493369371 312 CGAFAVSR 319
Cdd:TIGR03828 277 AGSAAAFS 284
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
14-317 |
5.81e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 48.17 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 14 IITIGRASVDLYgQQIGSRleditsfAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDG---- 89
Cdd:cd01937 2 IVIIGHVTIDEI-VTNGSG-------VVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVISLLstet 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 90 ------LKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTgthfsrpnsdaaqrkairi 163
Cdd:cd01937 74 ttfelnYTNEGRTRTLLAKCAAIPDTESPLSTITAEIVILGPVPEEISPSLFRKFAFISLD------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 164 mkarggkvvfdidyrpnlwglaghAEGFERYVKSDRVSAQlkTVLPHCDLIVGTEEEIMIASgadDCLSALKTIRSLSSA 243
Cdd:cd01937 135 ------------------------AQGFLRRANQEKLIKC--VILKLHDVLKLSRVEAEVIS---TPTELARLIKETGVK 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493369371 244 TIVLKRGAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAV 317
Cdd:cd01937 186 EIIVTDGEEGGYIFDG------NGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
204-297 |
7.38e-06 |
|
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: 48.23 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 204 LKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLKRGAMGCIVYDgpisddlEDGV-VGKGFPIE-VYNV 281
Cdd:cd01946 157 LKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFT-------DDGYfAAPAYPLEsVFDP 229
|
90
....*....|....*.
gi 493369371 282 LGAGDAFMSGFLrGWL 297
Cdd:cd01946 230 TGAGDTFAGGFI-GYL 244
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
201-329 |
7.43e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 42.32 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 201 SAQLKTVLPHCDLIVGTEEEIMIASGADDC-LSALKTIrSLSSATIVLKRGAMGCIVYdgpISDDLEDGVVGKGFPIEVY 279
Cdd:PTZ00247 205 FERLLQVLPYVDILFGNEEEAKTFAKAMKWdTEDLKEI-AARIAMLPKYSGTRPRLVV---FTQGPEPTLIATKDGVTSV 280
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493369371 280 NVL-----------GAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCA-PEYPTF 329
Cdd:PTZ00247 281 PVPpldqekivdtnGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKPPF 342
|
|
|