|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02323 |
PLN02323 |
probable fructokinase |
13-343 |
0e+00 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 682.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 13 LTIDTRDSETLVVCFGEMLIDFVPTVGGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRL 92
Cdd:PLN02323 2 MTAPSTAESSLVVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 93 NNVDNSGMRFDHNARTALAFVTLRGDGEREFLFFRHPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAMK 172
Cdd:PLN02323 82 NGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 173 IAKAAGSLLSYDPNLRLPLWPSEEAARKEIMSIWNLADVIKISEDEITFLTGGDDPYDDDVVlqKLFHPNLKLLVVSEGP 252
Cdd:PLN02323 162 IAKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVV--KLWHPNLKLLLVTEGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 253 NGCRYYTQEFKGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTLLKDEKKLREALLFANACGAITVTERGAIPAMPSMD 332
Cdd:PLN02323 240 EGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLEDEERLREALRFANACGAITTTERGAIPALPTKE 319
|
330
....*....|.
gi 15242193 333 AVQDLLSSTRS 343
Cdd:PLN02323 320 AVLKLLKKAVA 330
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
23-325 |
2.27e-131 |
|
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: 376.59 E-value: 2.27e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 23 LVVCFGEMLIDFVPTVGGVSlaeaPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRF 102
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAP----ETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 103 DHNARTALAFVTLRGDGEREFLFFRHPSADMlLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAMKIAKAAGSLLS 182
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADL-LLDTELNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 183 YDPNLRLPLWPSEEAARKEIMSIWNLADVIKISEDEITFLTGGDDPyddDVVLQKLFHPNLKLLVVSEGPNGCRYYTQEF 262
Cdd:cd01167 156 FDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDP---EEIAALLLLFGLKLVLVTRGADGALLYTKGG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242193 263 KGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTLLKDEKKLREALLFANACGAITVTERGAI 325
Cdd:cd01167 233 VGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
24-334 |
3.77e-100 |
|
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: 297.57 E-value: 3.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTV----GGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSG 99
Cdd:COG0524 2 VLVIGEALVDLVARVdrlpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 100 MRFDHNARTALAFVTLRGDGEREFLFFRhpSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAMKIAKAAGS 179
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 180 LLSYDPNLRLPLWpseEAARKEIMSIWNLADVIKISEDEITFLTGGDDPyddDVVLQKLFHPNLKLLVVSEGPNGCRYYT 259
Cdd:COG0524 160 PVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDP---EEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242193 260 QEFKGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITVTERGAIPAMPSMDAV 334
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLD-------LEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
51-335 |
2.12e-93 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 280.28 E-value: 2.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 51 KAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFDHNARTALAFVTLRGDGEREFLFFRHPS 130
Cdd:PRK09434 25 KCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 131 ADMLLLESELDKnlIQKAKIFHYGSISLIEEPCRSTQLVAMKIAKAAGSLLSYDPNLRLPLWPSEEAARKEIMSIWNLAD 210
Cdd:PRK09434 105 ADLFLQPQDLPP--FRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALALAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 211 VIKISEDEITFLTGGDDPYDDDVVLQKLFhpNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTTGAGDAFVSGLLNS 290
Cdd:PRK09434 183 VVKLSEEELCFLSGTSQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAG 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15242193 291 LASdLTLLKDEKKLREALLFANACGAITVTERGAIPAMPSMDAVQ 335
Cdd:PRK09434 261 LSQ-AGLWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
24-325 |
1.60e-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: 270.22 E-value: 1.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTVGGVsLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFD 103
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGR-LEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 104 HNARTALAFVTLRGDGEREFLFFRHPSADMLLLESELDKNLIQKAKIFHYGSISL-IEEPCRSTQLVAMKIAKAAGSLLS 182
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLaLSESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 183 YDPNLRLPLWpSEEAARKEIMSIWNLADVIKISEDEITFLTGGDDPYDDDVVLQKLfHPNLKLLVVSEGPNGCRYYTQEF 262
Cdd:cd01166 161 FDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAL-ALGVKAVVVKLGAEGALVYTGGG 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242193 263 KGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITVTERGAI 325
Cdd:cd01166 239 RVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWD-------LEEALRFANAAAALVVTRPGDI 294
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
23-325 |
1.67e-79 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 244.56 E-value: 1.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 23 LVVCFGEMLIDFVPTVGGVS--LAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGM 100
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPgeLVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 101 RFDHNARTALAFVTLRGDGEREFLFFRHPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAmKIAKAAGsl 180
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELI-EAAKNGG-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 181 lSYDPNLRLPLWPseeaARKEIMSIWNLADVIKISEDEITFLTG--GDDPYDDDVVLQKLFHPNLKLLVVSEGPNGCRYY 258
Cdd:pfam00294 158 -TFDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTGakLDDIEEALAALHKLLAKGIKTVIVTLGADGALVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242193 259 TQEFKGRVGGV-KVKPVDTTGAGDAFVSGLLNSLASdltllkdEKKLREALLFANACGAITVTERGAI 325
Cdd:pfam00294 233 EGDGEVHVPAVpKVKVVDTTGAGDSFVGGFLAGLLA-------GKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
24-338 |
5.29e-69 |
|
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: 218.24 E-value: 5.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTVGGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFD 103
Cdd:TIGR04382 4 VITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 104 HNARTALAFVTLRGDGEREFLFFRHPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAMKIAKAAGSLLSY 183
Cdd:TIGR04382 84 PGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 184 DPNLRLPLWPSEEAARKEIMSIWNLADVIKISEDEITFLTGGDDPyddDVVLQKLFHPNLKLLVVSEGPNGCRYYTQEFK 263
Cdd:TIGR04382 164 DIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDD---EAAARALLDAGVEILVVKRGPEGSLVYTGDGE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242193 264 G-RVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTLlkdekklREALLFANACGAITVTERGAIPAMPSMDAVQDLL 338
Cdd:TIGR04382 241 GvEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDL-------EKALRYGNACGAIVVSRHSCSPAMPTLEELEAFL 309
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
23-337 |
3.23e-64 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 211.30 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 23 LVVCFGEMLIDFVPTVGgVS---------------LAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLa 87
Cdd:PLN02543 127 LVCCFGAVQKEFVPTVR-VHdnqmhpdmysqwkmlQWDPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEEL- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 88 dILRLN--NVDNSGMRFDHNARTALAFVTLR-GDGEREFLFFRHPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCR 164
Cdd:PLN02543 205 -VLMMNkeRVQTRAVKFDENAKTACSRMKIKfRDGGKMVAETVKEAAEDSLLASELNLAVLKEARMFHFNSEVLTSPSMQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 165 STQLVAMKIAKAAGSLLSYDPNLRLPLWPSEEAARKEIMSIWNLADVIKISEDEITFLTGGD--------DP--YDDDVV 234
Cdd:PLN02543 284 STLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEADIIEVSRQELEFLLDEDyyerkrnyPPqyYAESFE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 235 LQK---------------LFHPNLKLLVVSEGPNGCRYYTQEFKGRVGG---VKVKP--VDTTGAGDAFVSGLLNSLASD 294
Cdd:PLN02543 364 QTKnwrdyyhytpeeiapLWHDGLKLLLVTDGTLRIHYYTPKFDGVVVGtedVLITPftCDRTGSGDAVVAAIMRKLTTC 443
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15242193 295 LTLLKDEKKLREALLFANACGAITVTERGAIPAMPSMDAVQDL 337
Cdd:PLN02543 444 PEMFEDQDVLERQLRFAVAAGIISQWTIGAVRGFPTESATQNL 486
|
|
| PLN02967 |
PLN02967 |
kinase |
23-317 |
1.50e-57 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 195.65 E-value: 1.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 23 LVVCFGEMLIDFVPT--------------VGGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLAD 88
Cdd:PLN02967 198 LVCCFGAAQHAFVPSgrpanrlldyeiheRMKDAFWAPEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLY 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 89 ILRLNNVDNSGMRFDHNARTALAFVTLRGDGEREFLFFRhPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQL 168
Cdd:PLN02967 278 YLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVK-PCAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 169 VAMKIAKAAGSLLSYDPNLRLPLWPSEEAARKEIMSIWNLADVIKISEDEITFLTGGD-----DPYDDD---------VV 234
Cdd:PLN02967 357 RAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNLADIIEVTKQELEFLCGIEpteefDTKDNDkskfvhyspEV 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 235 LQKLFHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPV-----DTTGAGDAFVSGLLNSLASDLTLLKDEKKLREALL 309
Cdd:PLN02967 437 VAPLWHENLKVLFVTNGTSKIHYYTKEHNGAVHGMEDAPItpftsDMSASGDGIVAGLMRMLTVQPHLITDKGYLEKTIK 516
|
....*...
gi 15242193 310 FANACGAI 317
Cdd:PLN02967 517 YAIDCGVI 524
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
45-330 |
9.69e-50 |
|
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: 167.73 E-value: 9.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 45 EAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFDHNARTALAFVTLRGDGEREFL 124
Cdd:cd01174 27 LGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 125 FfrHPSADMLLLESELD--KNLIQKAKIfhygsisLI---EEPcRSTQLVAMKIAKAAGSLLSYDPnlrLPlwpseeaAR 199
Cdd:cd01174 107 V--VPGANGELTPADVDaaLELIAAADV-------LLlqlEIP-LETVLAALRAARRAGVTVILNP---AP-------AR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 200 KEIMSIWNLADVIKISEDEITFLTG--GDDPYDDDVVLQKLFHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTT 277
Cdd:cd01174 167 PLPAELLALVDILVPNETEAALLTGieVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTT 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15242193 278 GAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITVTERGAIPAMPS 330
Cdd:cd01174 247 GAGDTFIGALAAALARGLS-------LEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
45-335 |
8.33e-46 |
|
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: 157.76 E-value: 8.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 45 EAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFDHNARTALAFVTLRGDGEREFL 124
Cdd:TIGR02152 22 HGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 125 FFrhPSADMLLLESELDK--NLIQKAKIFhygsISLIEEPcRSTQLVAMKIAKAAGSLLSYDPNlrlplwPSEEAARKEI 202
Cdd:TIGR02152 102 VV--AGANAELTPEDIDAaeALIAESDIV----LLQLEIP-LETVLEAAKIAKKHGVKVILNPA------PAIKDLDDEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 203 msiWNLADVIKISEDEITFLTG--GDDPYDDDVVLQKLFHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTTGAG 280
Cdd:TIGR02152 169 ---LSLVDIITPNETEAEILTGieVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVDTTAAG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15242193 281 DAFVSGLLNSLASDltllkdeKKLREALLFANACGAITVTERGAIPAMPSMDAVQ 335
Cdd:TIGR02152 246 DTFNGAFAVALAEG-------KSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-325 |
6.18e-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: 147.07 E-value: 6.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTV----GGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSG 99
Cdd:cd01942 2 VAVVGHLNYDIILKVesfpGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 100 MRFDHNARTALAFVTLRGDGERefLFFRHPSAdMLLLESELDKNLIQKAKIFHYGSISLIEEPCRStqlvamkiAKAAGS 179
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQ--IAYFYPGA-MDELEPNDEADPDGLADIVHLSSGPGLIELARE--------LAAGGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 180 LLSYDPNLRLPLWPSEEAARkeimsIWNLADVIKISEDEITFL---TGGDDPYDDDVVlqklfhpnlKLLVVSEGPNGCR 256
Cdd:cd01942 151 TVSFDPGQELPRLSGEELEE-----ILERADILFVNDYEAELLkerTGLSEAELASGV---------RVVVVTLGPKGAI 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 257 YYTQEFKGRVGGVK-VKPVDTTGAGDAFVSGLLNSLASDLTLLkdekklrEALLFANACGAITVTERGAI 325
Cdd:cd01942 217 VFEDGEEVEVPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYDLE-------ESLRLGNLAASLKVERRGAQ 279
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
17-339 |
4.25e-35 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 135.02 E-value: 4.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 17 TRDSETLVVCFGEMLIDFVPTVGGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVD 96
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 97 NSGMRFDHNARTALAFVTLRGDGEREFLFFRHPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAMKIAKA 176
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 177 AGSLLSYDPNLRLPLW-------------PSEEAARKeIMSIWNLADVIKISEDEITFLTGGDDpydDDVVLQKLFHPNL 243
Cdd:COG3892 161 HGGKVVLDIDYRPVLWgltghgdgetrfvASDAVTAH-LQEVLPLFDLIVGTEEEFHIAGGSTD---TLAALRAVRRVST 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 244 KLLVVSEGPNGCRYYT--------QEFKGRvgGVKVKPVDTTGAGDAFVSGLLnslasdLTLLKDEKkLREALLFANACG 315
Cdd:COG3892 237 ATLVCKRGALGCVVFEgaipddldDGITGP--GFPVEVFNVLGAGDAFMSGFL------RGWLRGES-WETACAYANACG 307
|
330 340
....*....|....*....|....
gi 15242193 316 AITVTERGAIPAMPSMDAVQDLLS 339
Cdd:COG3892 308 ALVVSRHGCAPAMPTWEELDYFLA 331
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
24-326 |
1.36e-32 |
|
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: 123.49 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTV------------GGVSLAEAPAF---------KKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEF 82
Cdd:cd01168 4 VLGLGNALVDILAQVddafleklglkkGDMILADMEEQeellaklpvKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 83 GRMLADILRLNNVDNSGMRfDHNARTALAFVTLRGDGEREFLFF----RHPSADmlllesELDKNLIQKAKIF---HYgs 155
Cdd:cd01168 84 GDFLLKDLRAAGVDTRYQV-QPDGPTGTCAVLVTPDAERTMCTYlgaaNELSPD------DLDWSLLAKAKYLyleGY-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 156 isLIEEPCRSTQLVAmKIAKAAGSLLS---YDPNLrlplwpsEEAARKEIMSIWNLADVIKISEDEITFLTGGdDPYDDD 232
Cdd:cd01168 155 --LLTVPPEAILLAA-EHAKENGVKIAlnlSAPFI-------VQRFKEALLELLPYVDILFGNEEEAEALAEA-ETTDDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 233 VVLQKLFHPNLKLLVVSEGPNGC--RYYTQEFKgrVGGVK-VKPVDTTGAGDAFVSGLLNSLASDLTllkdekkLREALL 309
Cdd:cd01168 224 EAALKLLALRCRIVVITQGAKGAvvVEGGEVYP--VPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEP-------LEECIR 294
|
330
....*....|....*..
gi 15242193 310 FANACGAITVTERGAIP 326
Cdd:cd01168 295 LGSYAAAEVIQQLGPRL 311
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
24-330 |
6.32e-29 |
|
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: 112.77 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTV----GGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSG 99
Cdd:cd01945 2 VLGVGLAVLDLIYLVasfpGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 100 MRFDHNARTALAFVTLR-GDGEREFLFFRHPSADMLLLESELDKNLiqkakifhygSISLIEEPCRSTQLVAMKIAKAAG 178
Cdd:cd01945 82 IVVAPGARSPISSITDItGDRATISITAIDTQAAPDSLPDAILGGA----------DAVLVDGRQPEAALHLAQEARARG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 179 --SLLSYDpnlRLPLWPSEEAARkeimsiwnLADVIKISEDEITFLTGGddpyDDDVVLQKLFHPNLKLLVVSEGPNGCR 256
Cdd:cd01945 152 ipIPLDLD---GGGLRVLEELLP--------LADHAICSENFLRPNTGS----ADDEALELLASLGIPFVAVTLGEAGCL 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242193 257 YYtqEFKGRVGGV---KVKPVDTTGAGDAFVSGLLNSLASDLtllkdekKLREALLFANACGAITVTERGAIPAMPS 330
Cdd:cd01945 217 WL--ERDGELFHVpafPVEVVDTTGAGDVFHGAFAHALAEGM-------PLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
17-339 |
1.64e-27 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 109.83 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 17 TRDSETLVV--CFGEMLI--DFVPTVGGVSLAEApaFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRL 92
Cdd:PTZ00292 13 EAEPDVVVVgsSNTDLIGyvDRMPQVGETLHGTS--FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 93 NNVDNSGMRFDHNARTALAFVTL-RGDGEREFLFFrhPSADMLLLESELDKnliQKAKIFHYGSISLI--EEPCRSTqLV 169
Cdd:PTZ00292 91 NGVNTSFVSRTENSSTGLAMIFVdTKTGNNEIVII--PGANNALTPQMVDA---QTDNIQNICKYLICqnEIPLETT-LD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 170 AMKIAKAAGSLLSYDPNlrlplwPSEEAARKE-IMSIWNLADVIKISEDEITFLTGGDdpYDDDVVLQKLFHPNLKL--- 245
Cdd:PTZ00292 165 ALKEAKERGCYTVFNPA------PAPKLAEVEiIKPFLKYVSLFCVNEVEAALITGME--VTDTESAFKASKELQQLgve 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 246 -LVVSEGPNGCRY-YTQEFKGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTLLkdekklrEALLFANACGAITVTERG 323
Cdd:PTZ00292 237 nVIITLGANGCLIvEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLK-------ESCKRANRIAAISVTRHG 309
|
330
....*....|....*.
gi 15242193 324 AIPAMPSMDAVQDLLS 339
Cdd:PTZ00292 310 TQSSYPHPSELPADVK 325
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
52-339 |
1.76e-27 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 109.19 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 52 APGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFDHNARTALAFVTLRGDGEREFLFfrHPSA 131
Cdd:PRK11142 37 AFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGI--HAGA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 132 DMLLLESELDK--NLIQKAKIFhygsisLI--EEPCRSTQLvAMKIAKAAGS--LLSYDPNLRLPlwpseeaarKEIMSi 205
Cdd:PRK11142 115 NAALTPALVEAhrELIANADAL------LMqlETPLETVLA-AAKIAKQHGTkvILNPAPARELP---------DELLA- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 206 wnLADVIKISEDEITFLTGGDDPYDDDVVL--QKLFHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTTGAGDAF 283
Cdd:PRK11142 178 --LVDIITPNETEAEKLTGIRVEDDDDAAKaaQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTF 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15242193 284 VSGLlnslasdLTLLKDEKKLREALLFANACGAITVTERGAIPAMPSMDAVQDLLS 339
Cdd:PRK11142 256 NGAL-------VTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
24-324 |
1.85e-27 |
|
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: 108.21 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTVGgvslaeapafKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFD 103
Cdd:cd01940 2 LAAIGDNVVDKYLHLG----------KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 104 HnARTALAFVTLRgDGEREFLF-------FRHPSADmllleselDKNLIQKAKIFH---YGSISLIEEPCRSTQlvamki 173
Cdd:cd01940 72 E-GENAVADVELV-DGDRIFGLsnkggvaREHPFEA--------DLEYLSQFDLVHtgiYSHEGHLEKALQALV------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 174 akAAGSLLSYDPNLRlplWPSEEAARkeimsiwnlaDVIKIsedEITFLTGGDDpyDDDVVLQKL--FHPN-LKLLVVSE 250
Cdd:cd01940 136 --GAGALISFDFSDR---WDDDYLQL----------VCPYV---DFAFFSASDL--SDEEVKAKLkeAVSRgAKLVIVTR 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242193 251 GPNGCRYYTQEFKGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTLLKdekklrEALLFANACGAITVTERGA 324
Cdd:cd01940 196 GEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTAIA------EAMRQGAQFAAKTCGHEGA 263
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
49-325 |
5.31e-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: 96.33 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 49 FKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNV-DNSGMRfDHNARTALAFVTlrGDGERefLFFR 127
Cdd:cd01947 31 SRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDkHTVAWR-DKPTRKTLSFID--PNGER--TITV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 128 HPSADMLLLE-SELDKNliqkAKIFHYGSISLIE--EPCRSTQLVAMkiakaagsllsyDPNLRLPLwpseeaarkeims 204
Cdd:cd01947 106 PGERLEDDLKwPILDEG----DGVFITAAAVDKEaiRKCRETKLVIL------------QVTPRVRV------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 205 iwnlaDVIKISEDEITFLTGGDDPYDDDVVLQKLFHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTTGAGDAFV 284
Cdd:cd01947 157 -----DELNQALIPLDILIGSRLDPGELVVAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15242193 285 SGLLNSLASDLTllkdekkLREALLFANACGAITVTERGAI 325
Cdd:cd01947 232 AGFIYGLLKGWS-------IEEALELGAQCGAICVSHFGPY 265
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
30-323 |
2.26e-22 |
|
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: 95.18 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 30 MLIDFVPTVGGVSLAEAPAFKKapGGApANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGM-RFDHNART 108
Cdd:cd01944 14 LDVDKLPASGGDIEAKSKSYVI--GGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPpRGGDDGGC 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 109 ALAFVTlrGDGEREFLFFrhPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAMKIAKAAGSLLSYDPNLR 188
Cdd:cd01944 91 LVALVE--PDGERSFISI--SGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTTLVFDPGPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 189 LPLWPSEEAARkeIM---SIWNLadvikiSEDEITFLTGGDDPYDDDVVLQkLFHPNLKLLVVSEGPNGCRYYTQEFKGR 265
Cdd:cd01944 167 ISDIPDTILQA--LMakrPIWSC------NREEAAIFAERGDPAAEASALR-IYAKTAAPVVVRLGSNGAWIRLPDGNTH 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15242193 266 -VGGVKVKPVDTTGAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITVTERG 323
Cdd:cd01944 238 iIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMS-------LADAVLLANAAAAIVVTRSG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
44-339 |
1.96e-21 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 94.90 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 44 AEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGM--------RFDHNARTALAFVTL 115
Cdd:PLN02341 109 ASPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLiegtdagdSSSASYETLLCWVLV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 116 RGDGEREFL----FFRHPS-ADMLLLESELDKNLIQKAKIFHYGSIslIEEpcRSTQLV--AMKIAKAAGSLLSYDPNLR 188
Cdd:PLN02341 189 DPLQRHGFCsradFGPEPAfSWISKLSAEAKMAIRQSKALFCNGYV--FDE--LSPSAIasAVDYAIDVGTAVFFDPGPR 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 189 ----LPLWPSEEAARKEIMSiwnLADVIKISEDEITFLTGGDDPYDddvVLQKLFHPNL--KLLVVSEGPNGCRYYTQEF 262
Cdd:PLN02341 265 gkslLVGTPDERRALEHLLR---MSDVLLLTSEEAEALTGIRNPIL---AGQELLRPGIrtKWVVVKMGSKGSILVTRSS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 263 KGRVGGVKVKPVDTTGAGDAFVS----GLLNSLASDLTllkdekklreaLLFANACGAITVTERGAIPAMPSMDAVQDLL 338
Cdd:PLN02341 339 VSCAPAFKVNVVDTVGCGDSFAAaialGYIHNLPLVNT-----------LTLANAVGAATAMGCGAGRNVATLEKVLELL 407
|
.
gi 15242193 339 S 339
Cdd:PLN02341 408 R 408
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
24-324 |
4.78e-19 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 85.17 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTVGgvslaeapafKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFD 103
Cdd:PRK09813 3 LATIGDNCVDIYPQLG----------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 104 HnARTALAFVTLRgDGEREF-LFFRHPSADMLLleSELDKNLIQKAKIFHYGSISLIEEpcrstqlvAMKIAKAAGSLLS 182
Cdd:PRK09813 73 H-GVTAQTQVELH-DNDRVFgDYTEGVMADFAL--SEEDYAWLAQYDIVHAAIWGHAED--------AFPQLHAAGKLTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 183 YDPNLRL--PLWpseeaaRKEIMSIwnlaDVIKISEDeitfltgGDDPYDDDVvLQKLFHPNLKLLVVSEGPNGCRYY-- 258
Cdd:PRK09813 141 FDFSDKWdsPLW------QTLVPHL----DYAFASAP-------QEDEFLRLK-MKAIVARGAGVVIVTLGENGSIAWdg 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242193 259 TQEFKGrvGGVKVKPVDTTGAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITVTERGA 324
Cdd:PRK09813 203 AQFWRQ--APEPVTVVDTMGAGDSFIAGFLCGWLAGMT-------LPQAMAQGTACAAKTIQYHGA 259
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
50-329 |
3.10e-18 |
|
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: 83.76 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 50 KKAPGGApANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRfDHNART-------ALAFVTLRGDGERE 122
Cdd:cd01172 36 EIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTttktrviARNQQLLRVDREDD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 123 flffRHPSADMLLLESELDKNLIQKAKI-----FHYGSIS--LIEEPCrstqlvamKIAKAAGSLLSYDPNLRlplwpse 195
Cdd:cd01172 114 ----SPLSAEEEQRLIERIAERLPEADVvilsdYGKGVLTprVIEALI--------AAARELGIPVLVDPKGR------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 196 eaarkeIMSIWNLADVIKISEDEITFLTGGDDPYDDDV--VLQKLFHP-NLKLLVVSEGPNGCRYY--TQEFKgRVGGVK 270
Cdd:cd01172 175 ------DYSKYRGATLLTPNEKEAREALGDEINDDDELeaAGEKLLELlNLEALLVTLGEEGMTLFerDGEVQ-HIPALA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15242193 271 VKPVDTTGAGDAFVSGLLNSLASDLTLLkdekklrEALLFANACGAITVTERGAIPAMP 329
Cdd:cd01172 248 KEVYDVTGAGDTVIATLALALAAGADLE-------EAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
53-327 |
1.58e-17 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 81.78 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 53 PGGApANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFDHNARTA--LAFVT-----LRGDGEREFlf 125
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTtkTRVIAggqqlLRLDFEDRF-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 126 frHPSADmllLESELDKNLIQKAKIFH------YGSISLIEEPCRStqlvAMKIAKAAGSLLSYDPNLRLPlwpseEAAR 199
Cdd:COG2870 132 --PLSAE---LEARLLAALEAALPEVDavilsdYGKGVLTPELIQA----LIALARAAGKPVLVDPKGRDF-----SRYR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 200 KeimsiwnlADVIKISEDEITFLTGGDDPYDDDVVL--QKLFH-PNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPV-D 275
Cdd:COG2870 198 G--------ATLLTPNLKEAEAAVGIPIADEEELVAaaAELLErLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVfD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15242193 276 TTGAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITVTERGAIPA 327
Cdd:COG2870 270 VTGAGDTVIATLALALAAGAS-------LEEAAELANLAAGIVVGKLGTATV 314
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
24-319 |
1.83e-16 |
|
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: 78.51 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTVGGVSLAEA--PA-FKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGM 100
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTsnPGhVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 101 RFdHNARTALAFVTLRGDGEREFLFfrhpsADMLLLEsELDKNLIQKAKIfhygsiSLIEEPCrstQLVAMKIAKAA-GS 179
Cdd:cd01941 82 VF-EGRSTASYTAILDKDGDLVVAL-----ADMDIYE-LLTPDFLRKIRE------ALKEAKP---IVVDANLPEEAlEY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 180 LLSY--DPNLRLPLWPSEEAARKEIMSIWNLADVIKISEDE-ITFLTGGDDPYDDDVVLQKLFH-PNLKLLVVSEGPNGc 255
Cdd:cd01941 146 LLALaaKHGVPVAFEPTSAPKLKKLFYLLHAIDLLTPNRAElEALAGALIENNEDENKAAKILLlPGIKNVIVTLGAKG- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242193 256 RYYTQefKGRVGGVKVKP-------VDTTGAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITV 319
Cdd:cd01941 225 VLLSS--REGGVETKLFPapqpetvVNVTGAGDAFVAGLVAGLLEGMS-------LDDSLRFAQAAAALTL 286
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
210-342 |
2.56e-15 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 75.17 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 210 DVIKISEDEITFLTGGDDPYDDDVV--LQKLFHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTTGAGDAFVSGL 287
Cdd:COG1105 179 DLIKPNLEELEELLGRPLETLEDIIaaARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGF 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15242193 288 LNSLASDLTllkdekkLREALLFANACGAITVTERGAipAMPSMDAVQDLLSSTR 342
Cdd:COG1105 259 LAGLARGLD-------LEEALRLAVAAGAAAALSPGT--GLPDREDVEELLAQVE 304
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
170-292 |
8.84e-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: 69.05 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 170 AMKIAKAAGSLLSYDPNlrlplWPSEEAARKEIMSIWNLADVIKISEDEITFLTGGDDP--YDDDVVLQKLFHPNLKLLV 247
Cdd:cd00287 76 ALEEARRRGVPVVLDPG-----PRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLevKEAAEAAALLLSKGPKVVI 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15242193 248 VSEGPNGCRYYTQEF-KGRVGGVKVKPVDTTGAGDAFVSGLLNSLA 292
Cdd:cd00287 151 VTLGEKGAIVATRGGtEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
32-323 |
5.97e-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: 59.47 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 32 IDFV-----PTVGGVSLAEAPAfkKAPGGAPANVAVGVSRLGGSSAFIGKVGDDeFGRMLADILRLNNVDNSGMRFDHNA 106
Cdd:cd01164 11 IDLTieldqLQPGEVNRVSSTR--KDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 107 RTALAFVTLRGDgEREFLFfrhpsADMLLLESELD---KNLIQKAKIFHY----GSISLIEEPCRSTQLVAmkIAKAAGS 179
Cdd:cd01164 88 RINVKIKEEDGT-ETEINE-----PGPEISEEELEallEKLKALLKKGDIvvlsGSLPPGVPADFYAELVR--LAREKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 180 LLSYDPnlrlplwpSEEAARKeimSIWNLADVIKISEDEITFLTGGDDPYDDDVV--LQKLFHPNLKLLVVSEGPNGCRY 257
Cdd:cd01164 160 RVILDT--------SGEALLA---ALAAKPFLIKPNREELEELFGRPLGDEEDVIaaARKLIERGAENVLVSLGADGALL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242193 258 YTQEFKGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTLLkdekklrEALLFANACGAITVTERG 323
Cdd:cd01164 229 VTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLE-------EALRLAVAAGSATAFSPG 287
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
45-297 |
1.39e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 58.65 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 45 EAPAFKKAPGGAPANVAVGVSR-LGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFDhNARTALAFVTLRGDGEREF 123
Cdd:PLN02379 77 DLSPIKTMAGGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAK-KGPTAQCVCLVDALGNRTM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 124 lffrHP--SADMLLLESELDKNLIQKAK--IFHYG--SISLIEEpcrstqlvAMKIAKAAGSLLSYD-------PNLRLP 190
Cdd:PLN02379 156 ----RPclSSAVKLQADELTKEDFKGSKwlVLRYGfyNLEVIEA--------AIRLAKQEGLSVSLDlasfemvRNFRSP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 191 LWPSEEAARkeimsiwnlADVIKISEDEITFLTGGDDPYDDDVVLQKLfHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVK 270
Cdd:PLN02379 224 LLQLLESGK---------IDLCFANEDEARELLRGEQESDPEAALEFL-AKYCNWAVVTLGSKGCIARHGKEVVRVPAIG 293
|
250 260
....*....|....*....|....*...
gi 15242193 271 -VKPVDTTGAGDAFVSGLLNSLASDLTL 297
Cdd:PLN02379 294 eTNAVDATGAGDLFASGFLYGLIKGLSL 321
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
49-324 |
1.56e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 58.67 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 49 FKKAPGGAPANVAVGVSRLGGSS--------AFIGKVGDDEFGRMLADILRLNNVdnsgmRF----DHNARTALAFVTLR 116
Cdd:PLN02813 121 YKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANV-----HFlsqpVKDGTTGTVIVLTT 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 117 GDGEREFLFFRHPSaDMLLLESELdKNLIQKAKIF---HY-----GSISLIEEPCRstqlvamkIAKAAGSLLSY---DP 185
Cdd:PLN02813 196 PDAQRTMLSYQGTS-STVNYDSCL-ASAISKSRVLvveGYlwelpQTIEAIAQACE--------EAHRAGALVAVtasDV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 186 NL----RLPLWpseeaarkEIMSiwNLADVIKISEDEITFLTGGDDPYDDDVVLQKLFHpNLKLLVVSEGPNGCryYTQe 261
Cdd:PLN02813 266 SCierhRDDFW--------DVMG--NYADILFANSDEARALCGLGSEESPESATRYLSH-FCPLVSVTDGARGS--YIG- 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242193 262 FKGRVGGV---KVKPVDTTGAGDAFVSGLLNSlasdltLLKDEKKLREALLFANACGAITVTERGA 324
Cdd:PLN02813 332 VKGEAVYIppsPCVPVDTCGAGDAYAAGILYG------LLRGVSDLRGMGELAARVAATVVGQQGT 391
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
24-313 |
4.66e-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: 53.17 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTVGGVslaeapafKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMlaDILRLNNVDnsgMRFD 103
Cdd:cd01937 2 IVIIGHVTIDEIVTNGSG--------VVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKW--SDLFDNGIE---VISL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 104 HNARTALAFVTLRGDGEREFLFFRhPSADmllLESELDKNLIQkAKIFHYGSISLieepcrstQLVAMKIAKAAgsLLSY 183
Cdd:cd01937 69 LSTETTTFELNYTNEGRTRTLLAK-CAAI---PDTESPLSTIT-AEIVILGPVPE--------EISPSLFRKFA--FISL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 184 DPNLRLPLWPSEEAARKEIMsiwNLADVIKISEDEITFLTGGDDPYDDDVVLQklfhpnLKLLVVSEGPNGCRYYTQEFK 263
Cdd:cd01937 134 DAQGFLRRANQEKLIKCVIL---KLHDVLKLSRVEAEVISTPTELARLIKETG------VKEIIVTDGEEGGYIFDGNGK 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15242193 264 GRVGGVKVKPVDTTGAGDAFVSGLLNSLASdltllkdEKKLREALLFANA 313
Cdd:cd01937 205 YTIPASKKDVVDPTGAGDVFLAAFLYSRLS-------GKDIKEAAEFAAA 247
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
246-335 |
2.06e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 49.03 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 246 LVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTllkdekkLREALLFANACGAITVTERGai 325
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLA-------VPDAALLGNYFGSLAVEQVG-- 276
|
90
....*....|
gi 15242193 326 paMPSMDAVQ 335
Cdd:PLN02630 277 --IPKFDLRQ 284
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
53-96 |
1.41e-05 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 46.75 E-value: 1.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15242193 53 PGGApANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVD 96
Cdd:PRK11316 50 PGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVK 92
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
196-323 |
1.03e-04 |
|
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: 43.22 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 196 EAARKEIMSIWNLADVIKISEDEITFLTGgddpydddvvlqklfHPNL------------KLLVVSEGPNGCRYYTQEfk 263
Cdd:cd01946 151 SIKPEKLKKVLAKVDVVIINDGEARQLTG---------------AANLvkaarlilamgpKALIIKRGEYGALLFTDD-- 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242193 264 grvgGVKVKP-------VDTTGAGDAFVSGLLNSLASDLTLlkDEKKLREALLFANACGAITVTERG 323
Cdd:cd01946 214 ----GYFAAPayplesvFDPTGAGDTFAGGFIGYLASQKDT--SEANMRRAIIYGSAMASFCVEDFG 274
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
24-313 |
6.47e-04 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 40.85 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 24 VVCFGEMLIDFVPTVggvslaeapafKKAP---------------GGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLAD 88
Cdd:cd01939 2 VLCVGLTVLDFITTV-----------DKYPfedsdqrttngrwqrGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 89 ILRLNNVDNSGMRFDHNARTALAFVTLRGDGEREFLFFRHPSADMLLleSELDKNLIQKAKIFHYGSISLiEEPCRSTQL 168
Cdd:cd01939 71 DFQSRGIDISHCYRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTY--DDFSKIDLTQYGWIHFEGRNP-DETLRMMQH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242193 169 VAMKIAKAAGSLLSYDPNLRLPlwpseeaaRKEIMSIWNLADVIKISEDeitflTGGDDPYDDDVVLQKLFHPNLK---L 245
Cdd:cd01939 148 IEEHNNRRPEIRITISVEVEKP--------REELLELAAYCDVVFVSKD-----WAQSRGYKSPEECLRGEGPRAKkaaL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242193 246 LVVSEG--------PNGCRYYTQEFKGrvggvkVKPVDTTGAGDAFVSGLLNSlasdltLLKDEKKLREALLFANA 313
Cdd:cd01939 215 LVCTWGdqgagalgPDGEYVHSPAHKP------IRVVDTLGAGDTFNAAVIYA------LNKGPDDLSEALDFGNR 278
|
|
| |
