|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02323 |
PLN02323 |
probable fructokinase |
7-336 |
0e+00 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 669.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 7 SAGSGNRNSLVVCFGEMLIDFVPTVGGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQN 86
Cdd:PLN02323 3 TAPSTAESSLVVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 87 NVDTSSVRYDSSARTALAFVTLRADGEREFLFFRHPSADMLLHESELDKKLIKQARIFHYGSISLIAEPCKSTHLAAMKI 166
Cdd:PLN02323 83 GVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 167 AKESGSILSYDPNLRLPLWPSEDAAREGIMSIWGQADIIKISEDEITFLTGGDDHNDDNVVlgKLFHPNLKLLVVTEGSK 246
Cdd:PLN02323 163 AKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVV--KLWHPNLKLLLVTEGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 247 GCRYYTKEFRGFVPGVKAISVDTTGAGDAFVSGILSCLASDLSLFKDEKRLREALLFANACGALTVTERGAIPALPTKEA 326
Cdd:PLN02323 241 GCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLEDEERLREALRFANACGAITTTERGAIPALPTKEA 320
|
330
....*....|
gi 2118878663 327 VLKLLEPVAA 336
Cdd:PLN02323 321 VLKLLKKAVA 330
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
16-318 |
4.63e-132 |
|
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: 378.13 E-value: 4.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 16 LVVCFGEMLIDFVPTVGGVSlaeaPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRY 95
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAP----ETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 96 DSSARTALAFVTLRADGEREFLFFRHPSADMLLhESELDKKLIKQARIFHYGSISLIAEPCKSTHLAAMKIAKESGSILS 175
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADLLL-DTELNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 176 YDPNLRLPLWPSEDAAREGIMSIWGQADIIKISEDEITFLTGGDDHnddNVVLGKLFHPNLKLLVVTEGSKGCRYYTKEF 255
Cdd:cd01167 156 FDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDP---EEIAALLLLFGLKLVLVTRGADGALLYTKGG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118878663 256 RGFVPGVKAISVDTTGAGDAFVSGILSCLASDLSLFKDEKRLREALLFANACGALTVTERGAI 318
Cdd:cd01167 233 VGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
17-327 |
2.72e-101 |
|
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: 300.26 E-value: 2.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTV----GGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSS 92
Cdd:COG0524 2 VLVIGEALVDLVARVdrlpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 93 VRYDSSARTALAFVTLRADGEREFLFFRhpSADMLLHESELDKKLIKQARIFHYGSISLIAEPCKSTHLAAMKIAKESGS 172
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 173 ILSYDPNLRLPLWpseDAAREGIMSIWGQADIIKISEDEITFLTGGDDHNDdnvVLGKLFHPNLKLLVVTEGSKGCRYYT 252
Cdd:COG0524 160 PVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEE---AAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118878663 253 KEFRGFVPGVKAISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPALPTKEAV 327
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLD-------LEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
44-324 |
1.64e-92 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 277.97 E-value: 1.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 44 KAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTALAFVTLRADGEREFLFFRHPS 123
Cdd:PRK09434 25 KCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 124 ADMLLHESELDKklIKQARIFHYGSISLIAEPCKSTHLAAMKIAKESGSILSYDPNLRLPLWPSEDAAREGIMSIWGQAD 203
Cdd:PRK09434 105 ADLFLQPQDLPP--FRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALALAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 204 IIKISEDEITFLTGGDDHNDDNVVLGKLFhpNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAISVDTTGAGDAFVSGILSC 283
Cdd:PRK09434 183 VVKLSEEELCFLSGTSQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAG 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2118878663 284 LASdLSLFKDEKRLREALLFANACGALTVTERGAIPALPTK 324
Cdd:PRK09434 261 LSQ-AGLWTDEAELAEIIAQAQACGALATTAKGAMTALPNR 300
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
17-318 |
6.11e-89 |
|
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: 268.29 E-value: 6.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTVGGVsLAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYD 96
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGR-LEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 97 SSARTALAFVTLRADGEREFLFFRHPSADMLLHESELDKKLIKQARIFHYGSISL-IAEPCKSTHLAAMKIAKESGSILS 175
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLaLSESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 176 YDPNLRLPLWpSEDAAREGIMSIWGQADIIKISEDEITFLTGGDDHNDDNVVLgKLFHPNLKLLVVTEGSKGCRYYTKEF 255
Cdd:cd01166 161 FDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERA-LALALGVKAVVVKLGAEGALVYTGGG 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118878663 256 RGFVPGVKAISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAI 318
Cdd:cd01166 239 RVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWD-------LEEALRFANAAAALVVTRPGDI 294
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
16-318 |
1.66e-83 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 254.57 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 16 LVVCFGEMLIDFVPTVGGVS--LAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSV 93
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPgeLVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 94 RYDSSARTALAFVTLRADGEREFLFFRHPSADMLLHESELDKKLIKQARIFHYGSIslIAEPCKSTHLAAMKIAKESGSI 173
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGS--LPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 174 lsYDPNLRLPLWPsedaAREGIMSIWGQADIIKISEDEITFLTG--GDDHNDDNVVLGKLFHPNLKLLVVTEGSKGCRYY 251
Cdd:pfam00294 159 --FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTGakLDDIEEALAALHKLLAKGIKTVIVTLGADGALVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118878663 252 TKEFRGFVPGVKAIS-VDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAI 318
Cdd:pfam00294 233 EGDGEVHVPAVPKVKvVDTTGAGDSFVGGFLAGLLAGKS-------LEEALRFANAAAALVVQKSGAQ 293
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
16-334 |
3.80e-68 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 221.32 E-value: 3.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 16 LVVCFGEMLIDFVPTVGgVS---------------LAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLA 80
Cdd:PLN02543 127 LVCCFGAVQKEFVPTVR-VHdnqmhpdmysqwkmlQWDPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 81 DILKQNNVDTSSVRYDSSARTALAF--VTLRADGEREFLFFRHPSADMLLhESELDKKLIKQARIFHYGSISLIAEPCKS 158
Cdd:PLN02543 206 LMMNKERVQTRAVKFDENAKTACSRmkIKFRDGGKMVAETVKEAAEDSLL-ASELNLAVLKEARMFHFNSEVLTSPSMQS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 159 THLAAMKIAKESGSILSYDPNLRLPLWPSEDAAREGIMSIWGQADIIKISEDEITFLTGGD----------DHNDDNVVL 228
Cdd:PLN02543 285 TLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEADIIEVSRQELEFLLDEDyyerkrnyppQYYAESFEQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 229 GK---------------LFHPNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAI-----SVDTTGAGDAFVSGILSCLASDL 288
Cdd:PLN02543 365 TKnwrdyyhytpeeiapLWHDGLKLLLVTDGTLRIHYYTPKFDGVVVGTEDVlitpfTCDRTGSGDAVVAAIMRKLTTCP 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2118878663 289 SLFKDEKRLREALLFANACGALTVTERGAIPALPTKEAVLKLLEPV 334
Cdd:PLN02543 445 EMFEDQDVLERQLRFAVAAGIISQWTIGAVRGFPTESATQNLKEQV 490
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
17-331 |
7.18e-64 |
|
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: 204.75 E-value: 7.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTVGGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYD 96
Cdd:TIGR04382 4 VITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 97 SSARTALAFVTLRADGEREFLFFRHPSADMLLHESELDKKLIKQARIFHYGSISLIAEPCKSTHLAAMKIAKESGSILSY 176
Cdd:TIGR04382 84 PGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 177 DPNLRLPLWPSEDAAREGIMSIWGQADIIKISEDEITfLTGGddHNDDNVVLGKLFHPNLKLLVVTEGSKGCRYYTKEFR 256
Cdd:TIGR04382 164 DIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFD-IAGG--EGDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118878663 257 GF-VPGVKAISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPALPTKEAVLKLL 331
Cdd:TIGR04382 241 GVeVPGFPVEVLNVLGAGDAFASGFLYGLLAGWD-------LEKALRYGNACGAIVVSRHSCSPAMPTLEELEAFL 309
|
|
| PLN02967 |
PLN02967 |
kinase |
16-333 |
1.74e-58 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 197.96 E-value: 1.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 16 LVVCFGEMLIDFVPT--------------VGGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLAD 81
Cdd:PLN02967 198 LVCCFGAAQHAFVPSgrpanrlldyeiheRMKDAFWAPEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLY 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 82 ILKQNNVDTSSVRYDSSARTALAFVTLRADGEREFLFFRhPSADMLLHESELDKKLIKQARIFHYGSISLIAEPCKSTHL 161
Cdd:PLN02967 278 YLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVK-PCAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 162 AAMKIAKESGSILSYDPNLRLPLWPSEDAAREGIMSIWGQADIIKISEDEITFLTG------GDDHNDDN--------VV 227
Cdd:PLN02967 357 RAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNLADIIEVTKQELEFLCGiepteeFDTKDNDKskfvhyspEV 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 228 LGKLFHPNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAISV-----DTTGAGDAFVSGILSCLASDLSLFKDEKRLREALL 302
Cdd:PLN02967 437 VAPLWHENLKVLFVTNGTSKIHYYTKEHNGAVHGMEDAPItpftsDMSASGDGIVAGLMRMLTVQPHLITDKGYLEKTIK 516
|
330 340 350
....*....|....*....|....*....|.
gi 2118878663 303 FANACGALTVTERGAIPALPTKEAVLKLLEP 333
Cdd:PLN02967 517 YAIDCGVIDQWLLARTRGFPPKEDMEDEVEP 547
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
38-323 |
1.32e-52 |
|
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: 175.05 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 38 EAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTALAFVTLRADGEREFL 117
Cdd:cd01174 27 LGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 118 FfrHPSADMLLHESELD--KKLIKQARIfhygsISLIAEPCKSTHLAAMKIAKESGSILSYDPnlrLPlwpsedaAREGI 195
Cdd:cd01174 107 V--VPGANGELTPADVDaaLELIAAADV-----LLLQLEIPLETVLAALRAARRAGVTVILNP---AP-------ARPLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 196 MSIWGQADIIKISEDEITFLTG-GDDHNDDNVVLGKLFH-PNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAISVDTTGAG 273
Cdd:cd01174 170 AELLALVDILVPNETEAALLTGiEVTDEEDAEKAARLLLaKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2118878663 274 DAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPALPT 323
Cdd:cd01174 250 DTFIGALAAALARGLS-------LEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
38-327 |
2.01e-47 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 161.61 E-value: 2.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 38 EAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTALAFVTLRADGEREFL 117
Cdd:TIGR02152 22 HGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 118 FFrhPSADMLLHESELDKK--LIKQARIfhygsisLIA--EPCKSTHLAAMKIAKESGSILSYDPnlrLPLWPSEDAare 193
Cdd:TIGR02152 102 VV--AGANAELTPEDIDAAeaLIAESDI-------VLLqlEIPLETVLEAAKIAKKHGVKVILNP---APAIKDLDD--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 194 gimSIWGQADIIKISEDEITFLTGGDDHNDDNVVLG--KLFHPNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAISVDTTG 271
Cdd:TIGR02152 167 ---ELLSLVDIITPNETEAEILTGIEVTDEEDAEKAaeKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVDTTA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2118878663 272 AGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPALPTKEAV 327
Cdd:TIGR02152 244 AGDTFNGAFAVALAEGKS-------LEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
17-318 |
2.09e-42 |
|
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: 148.23 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTV----GGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSS 92
Cdd:cd01942 2 VAVVGHLNYDIILKVesfpGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 93 VRYDSSARTALAFVTlrADGEREFLFFRHPSADMLLHESElDKKLIKQARIFHYGSISLIAEpcksthLAamKIAKESGS 172
Cdd:cd01942 82 VRVVDEDSTGVAFIL--TDGDDNQIAYFYPGAMDELEPND-EADPDGLADIVHLSSGPGLIE------LA--RELAAGGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 173 ILSYDPNLRLPLWPSEDAARegimsIWGQADIIKISEDEITFL---TGGDDHNDDNVVlgklfhpnlKLLVVTEGSKGCR 249
Cdd:cd01942 151 TVSFDPGQELPRLSGEELEE-----ILERADILFVNDYEAELLkerTGLSEAELASGV---------RVVVVTLGPKGAI 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 250 YYTKEFRGFVPGVKAIS-VDTTGAGDAFVSGILSCLASDLSLfkdEKRLReallFANACGALTVTERGAI 318
Cdd:cd01942 217 VFEDGEEVEVPAVPAVKvVDTTGAGDAFRAGFLYGLLRGYDL---EESLR----LGNLAASLKVERRGAQ 279
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
17-319 |
3.10e-35 |
|
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: 130.04 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTV------------GGVSLAEAPAF---------KKAPGGAPANVAVGISRLGGSSAFVGKVGDDEF 75
Cdd:cd01168 4 VLGLGNALVDILAQVddafleklglkkGDMILADMEEQeellaklpvKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 76 GYMLADILKQNNVDTSSVR-YDSSARTALAFVTlrADGEREFLFFRHPSADmlLHESELDKKLIKQARIF---HYgsisL 151
Cdd:cd01168 84 GDFLLKDLRAAGVDTRYQVqPDGPTGTCAVLVT--PDAERTMCTYLGAANE--LSPDDLDWSLLAKAKYLyleGY----L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 152 IAEPCKSThLAAMKIAKESGSILS---YDPNLrlplwpsEDAAREGIMSIWGQADIIKISEDEITFLTGGDDHNDDNVVL 228
Cdd:cd01168 156 LTVPPEAI-LLAAEHAKENGVKIAlnlSAPFI-------VQRFKEALLELLPYVDILFGNEEEAEALAEAETTDDLEAAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 229 GKLFHPNlKLLVVTEGSKGCRYYTKEFRGFVPGVK-AISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANAC 307
Cdd:cd01168 228 KLLALRC-RIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEP-------LEECIRLGSYA 299
|
330
....*....|..
gi 2118878663 308 GALTVTERGAIP 319
Cdd:cd01168 300 AAEVIQQLGPRL 311
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
25-325 |
1.11e-31 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 121.00 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 25 IDFVPTVGGVSLAEApaFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTALA 104
Cdd:PTZ00292 32 VDRMPQVGETLHGTS--FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 105 FVTL-RADGEREFLFFrhPSADMLLHESELDKkliKQARIFHYGSIsLIAE---PCKSThLAAMKIAKESGSILSYDPNl 180
Cdd:PTZ00292 110 MIFVdTKTGNNEIVII--PGANNALTPQMVDA---QTDNIQNICKY-LICQneiPLETT-LDALKEAKERGCYTVFNPA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 181 rlPLwPSEDAAREgIMSIWGQADIIKISEDEITFLTGGDdhNDDNVVLGKLFHPNLKL----LVVTEGSKGCRYYTKEFR 256
Cdd:PTZ00292 182 --PA-PKLAEVEI-IKPFLKYVSLFCVNEVEAALITGME--VTDTESAFKASKELQQLgvenVIITLGANGCLIVEKENE 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 257 G-FVPGVKAISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPALPTKE 325
Cdd:PTZ00292 256 PvHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKD-------LKESCKRANRIAAISVTRHGTQSSYPHPS 318
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
45-331 |
2.54e-27 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 108.80 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 45 APGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTALAFVTLRADGEREFLFfrHPSA 124
Cdd:PRK11142 37 AFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGI--HAGA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 125 DMLLHESELDK--KLIKQARIFhygsisLIA-EPCKSTHLAAMKIAKESGS--ILSYDPNLRLPLwpsedaaregimSIW 199
Cdd:PRK11142 115 NAALTPALVEAhrELIANADAL------LMQlETPLETVLAAAKIAKQHGTkvILNPAPARELPD------------ELL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 200 GQADIIKISEDEITFLTGGDDHNDDNVVLG-KLFHPN-LKLLVVTEGSKGCRYYTKEFRGFVPGVKAISVDTTGAGD--- 274
Cdd:PRK11142 177 ALVDIITPNETEAEKLTGIRVEDDDDAAKAaQVLHQKgIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDtfn 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2118878663 275 -AFVSGILsclasdlslfkDEKRLREALLFANACGALTVTERGAIPALPTKEAVLKLL 331
Cdd:PRK11142 257 gALVTALL-----------EGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
42-318 |
1.47e-23 |
|
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: 97.87 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 42 FKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTALAFVTlrADGEREFLFFRH 121
Cdd:cd01947 31 SRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFID--PNGERTITVPGE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 122 PSADMLlheseldkkliKQARIFHYGSISLIAEPCKSThlaAMKIAKESGSILsYDPNLRLPLWPSEDAARegimsiwgQ 201
Cdd:cd01947 109 RLEDDL-----------KWPILDEGDGVFITAAAVDKE---AIRKCRETKLVI-LQVTPRVRVDELNQALI--------P 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 202 ADIIKISEDEITFLTGGDdhnddnvvlgKLFHPNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAISVDTTGAGDAFVSGIL 281
Cdd:cd01947 166 LDILIGSRLDPGELVVAE----------KIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFI 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 2118878663 282 SCLASDLSlfkdekrLREALLFANACGALTVTERGAI 318
Cdd:cd01947 236 YGLLKGWS-------IEEALELGAQCGAICVSHFGPY 265
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
46-320 |
2.81e-23 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 97.96 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 46 PGGApANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTA--LAFVT-----LRADGEREFLF 118
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTtkTRVIAggqqlLRLDFEDRFPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 119 FRHPSADMLlhesELDKKLIKQARI-----FHYGSISliaepckSTHLAAM-KIAKESGSILSYDPNLRlplwpseDAAR 192
Cdd:COG2870 134 SAELEARLL----AALEAALPEVDAvilsdYGKGVLT-------PELIQALiALARAAGKPVLVDPKGR-------DFSR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 193 egimsiWGQADIIKISEDEITFLTGGDDHNDDNVVL--GKLFH-PNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAISV-D 268
Cdd:COG2870 196 ------YRGATLLTPNLKEAEAAVGIPIADEEELVAaaAELLErLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVfD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2118878663 269 TTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPA 320
Cdd:COG2870 270 VTGAGDTVIATLALALAAGAS-------LEEAAELANLAAGIVVGKLGTATV 314
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
17-317 |
1.51e-22 |
|
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: 94.73 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTVGgvslaeapafKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVR-Y 95
Cdd:cd01940 2 LAAIGDNVVDKYLHLG----------KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRvK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 96 DSSarTALAFVTLRaDGEREFLFFRHpSADMLLHESELDKKLIKQARIFH---YGSISLIAEPCKSTHLAAMKIakesgs 172
Cdd:cd01940 72 EGE--NAVADVELV-DGDRIFGLSNK-GGVAREHPFEADLEYLSQFDLVHtgiYSHEGHLEKALQALVGAGALI------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 173 ilSYDPNLRlplWPSEDAAREgimsiwgqadiikISEDEITFLTGGDDHNDD-NVVLGKLFHPNLKLLVVTEGSKGCRYY 251
Cdd:cd01940 142 --SFDFSDR---WDDDYLQLV-------------CPYVDFAFFSASDLSDEEvKAKLKEAVSRGAKLVIVTRGEDGAIAY 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118878663 252 TKEFRGFVPGVKAISVDTTGAGDAFVSG-ILSCLASDlslfkdeKRLREALLFANACGALTVTERGA 317
Cdd:cd01940 204 DGAVFYSVAPRPVEVVDTLGAGDSFIAGfLLSLLAGG-------TAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
17-323 |
1.89e-21 |
|
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: 92.36 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTV----GGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSS 92
Cdd:cd01945 2 VLGVGLAVLDLIYLVasfpGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 93 VRYDSSARTALAFVTLRA-DGEREFLFFRHPSADmllhESELDKKLIKQARIFHYGSISLIAepckSTHLAAMKIAKESG 171
Cdd:cd01945 82 IVVAPGARSPISSITDITgDRATISITAIDTQAA----PDSLPDAILGGADAVLVDGRQPEA----ALHLAQEARARGIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 172 SILSYDpnlRLPLWPSED---AAREGIMSIWGQADIIKISEDEitfltggddhnddnvVLGKLFHPNLKLLVVTEGSKGC 248
Cdd:cd01945 154 IPLDLD---GGGLRVLEEllpLADHAICSENFLRPNTGSADDE---------------ALELLASLGIPFVAVTLGEAGC 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118878663 249 RYYTKE---FRGFVPGVKAisVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPALPT 323
Cdd:cd01945 216 LWLERDgelFHVPAFPVEV--VDTTGAGDVFHGAFAHALAEGMP-------LREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
43-320 |
4.88e-20 |
|
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: 88.77 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 43 KKAPGGApANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRyDSSART-------ALAFVTLRADGERE 115
Cdd:cd01172 36 EIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTttktrviARNQQLLRVDREDD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 116 flffRHPSADmllHESELDKKLIKQARIFH------YG----SISLIAEPCKsthlaamkIAKESGSILSYDPNLRlplw 185
Cdd:cd01172 114 ----SPLSAE---EEQRLIERIAERLPEADvvilsdYGkgvlTPRVIEALIA--------AARELGIPVLVDPKGR---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 186 psedaaregIMSIWGQADIIKISEDEITFLTGGDDHNDDNVVLG--KLFHP-NLKLLVVTEGSKGCRYY--TKEFRGFvP 260
Cdd:cd01172 175 ---------DYSKYRGATLLTPNEKEAREALGDEINDDDELEAAgeKLLELlNLEALLVTLGEEGMTLFerDGEVQHI-P 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 261 GVKAISVDTTGAGDAFVSGILSCLASDLSLFkdekrlrEALLFANACGALTVTERGAIPA 320
Cdd:cd01172 245 ALAKEVYDVTGAGDTVIATLALALAAGADLE-------EAAFLANAAAGVVVGKVGTAPV 297
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
23-316 |
2.21e-18 |
|
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: 83.63 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 23 MLIDFVPTVGGVSLAEAPAFKKapGGApANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTS-SVRYDSSART 101
Cdd:cd01944 14 LDVDKLPASGGDIEAKSKSYVI--GGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILlPPRGGDDGGC 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 102 ALAFVTlrADGEREFLFFrhPSADMLLHESELDKKLIKQARIFHYGSISLIAEPCKSTHLAAMKIAKESGSILSYDPNLR 181
Cdd:cd01944 91 LVALVE--PDGERSFISI--SGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTTLVFDPGPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 182 LPLWPseDAAREGIMSiwgQADIIKISEDEITFLTGGDDHNDDNVVLGkLFHPNLKLLVVTEGSKGCRYYTKEFR-GFVP 260
Cdd:cd01944 167 ISDIP--DTILQALMA---KRPIWSCNREEAAIFAERGDPAAEASALR-IYAKTAAPVVVRLGSNGAWIRLPDGNtHIIP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2118878663 261 GVKAISVDTTGAGDAFVSGILSCLASDLSLFkdekrlrEALLFANACGALTVTERG 316
Cdd:cd01944 241 GFKVKAVDTIGAGDTHAGGMLAGLAKGMSLA-------DAVLLANAAAAIVVTRSG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
37-331 |
1.05e-17 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 83.73 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 37 AEAPAFKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDT--------SSVRYDSSARTALAFVTL 108
Cdd:PLN02341 109 ASPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVvgliegtdAGDSSSASYETLLCWVLV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 109 ----------RADGEREFLF--FRHPSAD--MLLHESeldKKLIKQARIFHYGSISLIAepcksthlAAMKIAKESGSIL 174
Cdd:PLN02341 189 dplqrhgfcsRADFGPEPAFswISKLSAEakMAIRQS---KALFCNGYVFDELSPSAIA--------SAVDYAIDVGTAV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 175 SYDPNLR----LPLWPSEDAAREGIMSIwgqADIIKISEDEITFLTGgddhNDDNVVLGK-LFHPNL--KLLVVTEGSKG 247
Cdd:PLN02341 258 FFDPGPRgkslLVGTPDERRALEHLLRM---SDVLLLTSEEAEALTG----IRNPILAGQeLLRPGIrtKWVVVKMGSKG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 248 CRYYTKEFRGFVPGVKAISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAIPALPTKEAV 327
Cdd:PLN02341 331 SILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLP-------LVNTLTLANAVGAATAMGCGAGRNVATLEKV 403
|
....
gi 2118878663 328 LKLL 331
Cdd:PLN02341 404 LELL 407
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
17-317 |
3.13e-17 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 80.17 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTVGgvslaeapafKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYD 96
Cdd:PRK09813 3 LATIGDNCVDIYPQLG----------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 97 sSARTALAFVTLRaDGEREF-LFFRHPSADMLLheSELDKKLIKQARIFHYGSISLIAEpcksthlaAMKIAKESGSILS 175
Cdd:PRK09813 73 -HGVTAQTQVELH-DNDRVFgDYTEGVMADFAL--SEEDYAWLAQYDIVHAAIWGHAED--------AFPQLHAAGKLTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 176 YDPNLRL--PLW----PSEDAAregimsiWGQADiikiseDEITFLtggDDHNDDNVVLGklfhpnLKLLVVTEGSKGCR 249
Cdd:PRK09813 141 FDFSDKWdsPLWqtlvPHLDYA-------FASAP------QEDEFL---RLKMKAIVARG------AGVVIVTLGENGSI 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 250 YY--TKEFRGfvPGVKAISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGA 317
Cdd:PRK09813 199 AWdgAQFWRQ--APEPVTVVDTMGAGDSFIAGFLCGWLAGMT-------LPQAMAQGTACAAKTIQYHGA 259
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
17-312 |
3.30e-17 |
|
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: 80.44 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTVGGVSLAEA--PA-FKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSV 93
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTsnPGhVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 94 RYdSSARTALAFVTLRADGEREFLFfrhpsADMLLHEsELDKKLIKQARIfhygsiSLIAEPCKsthLAAMKIAKES-GS 172
Cdd:cd01941 82 VF-EGRSTASYTAILDKDGDLVVAL-----ADMDIYE-LLTPDFLRKIRE------ALKEAKPI---VVDANLPEEAlEY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 173 ILSY--DPNLRLPLWPsEDAAR-EGIMSIWGQADIIKISEDE-ITFLTGGDDHNDDNVVLGKLFH-PNLKLLVVTEGSKG 247
Cdd:cd01941 146 LLALaaKHGVPVAFEP-TSAPKlKKLFYLLHAIDLLTPNRAElEALAGALIENNEDENKAAKILLlPGIKNVIVTLGAKG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 248 cRYYTK-----EFRGFVPGVKAISVDTTGAGDAFVSGILSCLASDlslfkdeKRLREALLFANACGALTV 312
Cdd:cd01941 225 -VLLSSreggvETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEG-------MSLDDSLRFAQAAAALTL 286
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
46-334 |
7.51e-17 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 79.79 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 46 PGGAPANVAVGISRLGGSS---AFVGkvGDDefGYMLADILKQNNVDTSSVRYDSSARTALAFVTLRADGEREFLFfrhP 122
Cdd:COG1105 34 PGGKGINVARVLKALGVDVtalGFLG--GFT--GEFIEELLDEEGIPTDFVPIEGETRINIKIVDPSDGTETEINE---P 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 123 SADmlLHESELD---KKLIKQARIFHY----GSI------SLIAEpcksthlaAMKIAKESG--SIL-SYDPNLRlplwp 186
Cdd:COG1105 107 GPE--ISEEELEallERLEELLKEGDWvvlsGSLppgvppDFYAE--------LIRLARARGakVVLdTSGEALK----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 187 seDAAREGimsiwgqADIIKISEDEITFLTGGDDHNDDNVV--LGKLFHPNLKLLVVTEGSKGCRYYTKE--FRGFVPGV 262
Cdd:COG1105 172 --AALEAG-------PDLIKPNLEELEELLGRPLETLEDIIaaARELLERGAENVVVSLGADGALLVTEDgvYRAKPPKV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118878663 263 KAISvdTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERGAipALPTKEAVLKLLEPV 334
Cdd:COG1105 243 EVVS--TVGAGDSMVAGFLAGLARGLD-------LEEALRLAVAAGAAAALSPGT--GLPDREDVEELLAQV 303
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
25-316 |
1.51e-14 |
|
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: 72.95 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 25 IDFV-----PTVGGVSLAEAPAfkKAPGGAPANVAVGISRLGGSSAFVGKVGDDeFGYMLADILKQNNVDTSSVRYDSSA 99
Cdd:cd01164 11 IDLTieldqLQPGEVNRVSSTR--KDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 100 RTALAFVTLRADgEREFLFfrhpsADMLLHESELD---KKLIKQARIFHY----GSISLIAEPCKSTHLAAmkIAKESGs 172
Cdd:cd01164 88 RINVKIKEEDGT-ETEINE-----PGPEISEEELEallEKLKALLKKGDIvvlsGSLPPGVPADFYAELVR--LAREKG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 173 ilsydpnLRLPLWPSEDAAREGIMSiwgQADIIKISEDEITFLTGGDDHNDDNVV-LGKLFHPN-LKLLVVTEGSKGCRY 250
Cdd:cd01164 159 -------ARVILDTSGEALLAALAA---KPFLIKPNREELEELFGRPLGDEEDVIaAARKLIERgAENVLVSLGADGALL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118878663 251 YTKE--FRGFVPGVKAISvdTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERG 316
Cdd:cd01164 229 VTKDgvYRASPPKVKVVS--TVGAGDSMVAGFVAGLAQGLS-------LEEALRLAVAAGSATAFSPG 287
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
161-285 |
3.81e-14 |
|
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: 70.20 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 161 LAAMKIAKESGSILSYDPNlrlplWPSEDAAREGIMSIWGQADIIKISEDEITFLTG--GDDHNDDNVVLGKLFHPNLKL 238
Cdd:cd00287 74 LDALEEARRRGVPVVLDPG-----PRAVRLDGEELEKLLPGVDILTPNEEEAEALTGrrDLEVKEAAEAAALLLSKGPKV 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2118878663 239 LVVTEGSKGCRYYTKEF-RGFVPGVKAISVDTTGAGDAFVSGILSCLA 285
Cdd:cd00287 149 VIVTLGEKGAIVATRGGtEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
38-290 |
5.50e-14 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 72.13 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 38 EAPAFKKAPGGAPANVAVGISR-LGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYdSSARTALAFVTLRADGEREF 116
Cdd:PLN02379 77 DLSPIKTMAGGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRA-KKGPTAQCVCLVDALGNRTM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 117 lffrHP--SADMLLHESELDKKLIKQAR--IFHYG--SISLIaepcksthLAAMKIAKESGSILSYD-------PNLRLP 183
Cdd:PLN02379 156 ----RPclSSAVKLQADELTKEDFKGSKwlVLRYGfyNLEVI--------EAAIRLAKQEGLSVSLDlasfemvRNFRSP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 184 LwpsedaaREGIMSiwGQADIIKISEDEITFLTGGDDHNDDNVVLgKLFHPNLKLLVVTEGSKGC--RYYTKEFRgfVPG 261
Cdd:PLN02379 224 L-------LQLLES--GKIDLCFANEDEARELLRGEQESDPEAAL-EFLAKYCNWAVVTLGSKGCiaRHGKEVVR--VPA 291
|
250 260 270
....*....|....*....|....*....|
gi 2118878663 262 VK-AISVDTTGAGDAFVSGILSCLASDLSL 290
Cdd:PLN02379 292 IGeTNAVDATGAGDLFASGFLYGLIKGLSL 321
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
17-322 |
1.02e-10 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 61.97 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTV------------GGVSLAE------------APAFKKAPGGAPANVAvgisRLG--------GSS 64
Cdd:PTZ00247 8 LLGFGNPLLDISAHVsdeflekyglelGSAILAEekqlpifeelesIPNVSYVPGGSALNTA----RVAqwmlqapkGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 65 AFVGKVGDDEFGYMLADILKQNNVDTSsVRYDSSARTALAFV-------TLRAD-GEREFLFFRHpsadmllHESELDKK 136
Cdd:PTZ00247 84 CYVGCVGDDRFAEILKEAAEKDGVEML-FEYTTKAPTGTCAVlvcgkerSLVANlGAANHLSAEH-------MQSHAVQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 137 LIKQARIFHYGSISLIAEPCKSTHLAamKIAKESGSILSYdpNLRLPLwpSEDAAREGIMSIWGQADIIKISEDEitFLT 216
Cdd:PTZ00247 156 AIKTAQLYYLEGFFLTVSPNNVLQVA--KHARESGKLFCL--NLSAPF--ISQFFFERLLQVLPYVDILFGNEEE--AKT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 217 GGD----DHNDDNVVLGKLF--------HPnlKLLVVTEGSKGCRYYTKEFRGFVPgVKAIS----VDTTGAGDAFVSGI 280
Cdd:PTZ00247 228 FAKamkwDTEDLKEIAARIAmlpkysgtRP--RLVVFTQGPEPTLIATKDGVTSVP-VPPLDqekiVDTNGAGDAFVGGF 304
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2118878663 281 LSCLASDlslfKDEKRLREAllfANACGALTVTERGA-IPALP 322
Cdd:PTZ00247 305 LAQYANG----KDIDRCVEA---GHYSAQVIIQHNGCtYPEKP 340
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
42-317 |
1.95e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 61.36 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 42 FKKAPGGAPANVAVGISRLGGSS--------AFVGKVGDDEFGYMLADILKQNNVDTSSVRYdSSARTALAFVTLRADGE 113
Cdd:PLN02813 121 YKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANVHFLSQPV-KDGTTGTVIVLTTPDAQ 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 114 REFLFFRHPSaDMLLHESELdKKLIKQARIF---HY-----GSISLIAEPCKSTHLAAMKIAKESGsilsyDPNLRlplw 185
Cdd:PLN02813 200 RTMLSYQGTS-STVNYDSCL-ASAISKSRVLvveGYlwelpQTIEAIAQACEEAHRAGALVAVTAS-----DVSCI---- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 186 pseDAAREGIMSIWGQ-ADIIKISEDEITFLTG-GDDHNDDNVVLgKLFHpNLKLLVVTEGSKGCRYYTKEFRGFVPGVK 263
Cdd:PLN02813 269 ---ERHRDDFWDVMGNyADILFANSDEARALCGlGSEESPESATR-YLSH-FCPLVSVTDGARGSYIGVKGEAVYIPPSP 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2118878663 264 AISVDTTGAGDAFVSGILsclasdLSLFKDEKRLREALLFANACGALTVTERGA 317
Cdd:PLN02813 344 CVPVDTCGAGDAYAAGIL------YGLLRGVSDLRGMGELAARVAATVVGQQGT 391
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
239-319 |
3.16e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 57.51 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 239 LVVTEGSKGCRYYTK--EFRgfVPGVKAISVDTTGAGDAFVSGILSCLASDLSlfkdekrLREALLFANACGALTVTERG 316
Cdd:PLN02630 206 VIVTNGKKGCRIYWKdgEMR--VPPFPAIQVDPTGAGDSFLGGFVAGLVQGLA-------VPDAALLGNYFGSLAVEQVG 276
|
...
gi 2118878663 317 aIP 319
Cdd:PLN02630 277 -IP 278
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
17-306 |
6.77e-08 |
|
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: 52.79 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 17 VVCFGEMLIDFVPTVGGVslaeapafKKAPGGAPANVAVGISRLGGSSAFVGKVGDDEfgymlADILKQNNVDTSSVRYD 96
Cdd:cd01937 2 IVIIGHVTIDEIVTNGSG--------VVKPGGPATYASLTLSRLGLTVKLVTKVGRDY-----PDKWSDLFDNGIEVISL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 97 SSARTALAFVTLRADGEREFLffrhpsadMLLHESELDKKLIKQAR---IFHYGSISLIAEPCKSthlaamkiakESGSI 173
Cdd:cd01937 69 LSTETTTFELNYTNEGRTRTL--------LAKCAAIPDTESPLSTItaeIVILGPVPEEISPSLF----------RKFAF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 174 LSYDPNLRLPLWPSEDAAREGIMSiwgQADIIKISEDEI-TFLTGGDdhnddNVVLGKLFHPnlKLLVVTEGSKGCRYYT 252
Cdd:cd01937 131 ISLDAQGFLRRANQEKLIKCVILK---LHDVLKLSRVEAeVISTPTE-----LARLIKETGV--KEIIVTDGEEGGYIFD 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2118878663 253 KEFRGFVPGVKAISVDTTGAGDAFvsgilscLASDLSLFKDEKRLREALLFANA 306
Cdd:cd01937 201 GNGKYTIPASKKDVVDPTGAGDVF-------LAAFLYSRLSGKDIKEAAEFAAA 247
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
46-97 |
7.60e-07 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 50.60 E-value: 7.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2118878663 46 PGGApANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDS 97
Cdd:PRK11316 50 PGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSVPT 100
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
43-313 |
7.56e-06 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 46.90 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 43 KKAPGGAPANVAVGISRLGGSSAFVGKVGDDEFGYMLADILKQNNVDTSSVRYDSSARTALAFVTLRADGE-----REFL 117
Cdd:PRK09850 36 KFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEmlvaiNDMN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 118 FFRHPSADMLLHESEL---------DKKLIKQARIF---HYGSISLIAEPCKSthLAAMKIAKESGSILSYDPNlRLplw 185
Cdd:PRK09850 116 ISNAITAEYLAQHREFiqrakvivaDCNISEEALAWildNAANVPVFVDPVSA--WKCVKVRDRLNQIHTLKPN-RL--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 186 psEDAAREGImSIWGQADIIKISedeitfltggddhnddnvvlgKLFHPN-LKLLVVTEGSKGCrYYTKEF--RGFVPGV 262
Cdd:PRK09850 190 --EAETLSGI-ALSGREDVAKVA---------------------AWFHQHgLNRLVLSMGGDGV-YYSDISgeSGWSAPI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2118878663 263 KAISVDTTGAGDAFVSGILSCLASDLSlFKDEKRlreallFANACGALTVT 313
Cdd:PRK09850 245 KTNVINVTGAGDAMMAGLASCWVDGMP-FAESVR------FAQGCSSMALS 288
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
189-316 |
1.57e-05 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 45.92 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 189 DAAREGIMSIWGQADIIKISEDEITFLTGgddhnDDNVVLG--KLFHPNLKLLVVTEGSKGCRYYTKEFRGFVPGVKAIS 266
Cdd:cd01946 151 SIKPEKLKKVLAKVDVVIINDGEARQLTG-----AANLVKAarLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLES 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2118878663 267 V-DTTGAGDAFVSGILSCLASDLSLfkDEKRLREALLFANACGALTVTERG 316
Cdd:cd01946 226 VfDPTGAGDTFAGGFIGYLASQKDT--SEANMRRAIIYGSAMASFCVEDFG 274
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
39-290 |
4.01e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 41.69 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 39 APAFKkaPGGAPANVAVGISRLGGSSAFVGKVGDDEfGYMLADILKQNNVDTSSVRYDSSARTALaFVTLRADGERefLF 118
Cdd:PRK10294 32 APVFE--PGGGGINVARAIAHLGGSATAIFPAGGAT-GEHLVSLLADENVPVATVEAKDWTRQNL-HVHVEASGEQ--YR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 119 FRHPSADmlLHESELDKKLIKQARIfHYGSISLIA-------EPCKSTHLaaMKIAKESGsilsydpnLRLPLWPSEDAA 191
Cdd:PRK10294 106 FVMPGAA--LNEDEFRQLEEQVLEI-ESGAILVISgslppgvKLEKLTQL--ISAAQKQG--------IRCIIDSSGDAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118878663 192 REGIMSiwGQADIIKISEDEITFLTGGDDHNDDNVVL--------GKlfhpnLKLLVVTEGSKGCRYYTKEfrGFV---- 259
Cdd:PRK10294 173 SAALAI--GNIELVKPNQKELSALVNRDLTQPDDVRKaaqelvnsGK-----AKRVVVSLGPQGALGVDSE--NCIqvvp 243
|
250 260 270
....*....|....*....|....*....|.
gi 2118878663 260 PGVKAISvdTTGAGDAFVSGILSCLASDLSL 290
Cdd:PRK10294 244 PPVKSQS--TVGAGDSMVGAMTLKLAENASL 272
|
|
| |
