|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02323 |
PLN02323 |
probable fructokinase |
1-328 |
0e+00 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 665.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 1 MAVNGASSSGLIVSFGEMLIDFVPTVSGVSLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKT 80
Cdd:PLN02323 2 MTAPSTAESSLVVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 81 NGVQAEGINFDKGARTALAFVTLRADGEREFMFYRNPSADMLLTPAELNLDLIRSAKVFHYGSISLIVEPCRAAHMKAME 160
Cdd:PLN02323 82 NGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 161 VAKEAGALLSYDPNLRLPLWPSAEEAKKQIKSIWDSADVIKVSDVELEFLTGSNKIDDESAMSLWHPNLKLLLVTLGEKG 240
Cdd:PLN02323 162 IAKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVVKLWHPNLKLLLVTEGEEG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 241 CNYYTKKFHGTVGGFHVKTVDTTGAGDSFVGALLTKIVDDQTILEDEARLKEVLRFSCACGAITTTKKGAIPALPTASEA 320
Cdd:PLN02323 242 CRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLEDEERLREALRFANACGAITTTERGAIPALPTKEAV 321
|
....*...
gi 350534508 321 LTLLKGGA 328
Cdd:PLN02323 322 LKLLKKAV 329
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
11-311 |
1.07e-139 |
|
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: 397.01 E-value: 1.07e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 11 LIVSFGEMLIDFVPTVSGVSlaeaPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINF 90
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAP----ETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 91 DKGARTALAFVTLRADGEREFMFYRNPSADMLLTPaELNLDLIRSAKVFHYGSISLIVEPCRAAHMKAMEVAKEAGALLS 170
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDT-ELNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 171 YDPNLRLPLWPSAEEAKKQIKSIWDSADVIKVSDVELEFLTGsNKIDDESAMSLWHPNLKLLLVTLGEKGCNYYTKKFHG 250
Cdd:cd01167 156 FDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFG-EEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350534508 251 TVGGFHVKTVDTTGAGDSFVGALLTKIVDDQTILEDEARLKEVLRFSCACGAITTTKKGAI 311
Cdd:cd01167 235 EVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
12-319 |
3.68e-93 |
|
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: 279.08 E-value: 3.68e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVS----GVSLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEG 87
Cdd:COG0524 2 VLVIGEALVDLVARVDrlpkGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 88 INFDKGARTALAFVTLRADGEREFMFYRnpSADMLLTPAELNLDLIRSAKVFHYGSISLIVEPCRAAHMKAMEVAKEAGA 167
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 168 LLSYDPNLRLPLWpsaEEAKKQIKSIWDSADVIKVSDVELEFLTGSNKIdDESAMSLWHPNLKLLLVTLGEKGCNYYTKK 247
Cdd:COG0524 160 PVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDP-EEAAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350534508 248 FHGTVGGFHVKTVDTTGAGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAIPALPTASE 319
Cdd:COG0524 236 EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLD-------LEEALRFANAAAALVVTRPGAQPALPTREE 300
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
12-311 |
1.20e-83 |
|
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: 254.42 E-value: 1.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVSGVsLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFD 91
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGR-LEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 92 KGARTALAFVTLRADGEREFMFYRNPSADMLLTPAELNLDLIRSAKVFHYGSISL-IVEPCRAAHMKAMEVAKEAGALLS 170
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLaLSESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 171 YDPNLRLPLWpSAEEAKKQIKSIWDSADVIKVSDVELEFLTGSNKIDD-ESAMSLWHPNLKLLLVTLGEKGCNYYTKKFH 249
Cdd:cd01166 161 FDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDaAERALALALGVKAVVVKLGAEGALVYTGGGR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350534508 250 GTVGGFHVKTVDTTGAGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAI 311
Cdd:cd01166 240 VFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWD-------LEEALRFANAAAALVVTRPGDI 294
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
37-319 |
3.64e-81 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 248.70 E-value: 3.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 37 FLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTLRADGEREFMFYRN 116
Cdd:PRK09434 23 YLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 117 PSADMLLTPAElnLDLIRSAKVFHYGSISLIVEPCRAAHMKAMEVAKEAGALLSYDPNLRLPLWPSAEEAKKQIKSIWDS 196
Cdd:PRK09434 103 PSADLFLQPQD--LPPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 197 ADVIKVSDVELEFLTGSNKIDDE-SAMSLWHPnLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAGDSFVGALLT 275
Cdd:PRK09434 181 ADVVKLSEEELCFLSGTSQLEDAiYALADRYP-IALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLA 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 350534508 276 KIVdDQTILEDEARLKEVLRFSCACGAITTTKKGAIPALPTASE 319
Cdd:PRK09434 260 GLS-QAGLWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQE 302
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
11-323 |
5.29e-71 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 228.64 E-value: 5.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 11 LIVSFGEMLIDFVPTVSgVS---------------LAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLA 75
Cdd:PLN02543 127 LVCCFGAVQKEFVPTVR-VHdnqmhpdmysqwkmlQWDPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 76 GILKTNGVQAEGINFDKGARTALAF--VTLRADGEREFMFYRNPSADMLLTpAELNLDLIRSAKVFHYGSISLIVEPCRA 153
Cdd:PLN02543 206 LMMNKERVQTRAVKFDENAKTACSRmkIKFRDGGKMVAETVKEAAEDSLLA-SELNLAVLKEARMFHFNSEVLTSPSMQS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 154 AHMKAMEVAKEAGALLSYDPNLRLPLWPSAEEAKKQIKSIWDSADVIKVSDVELEFLTGS-------------------- 213
Cdd:PLN02543 285 TLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEADIIEVSRQELEFLLDEdyyerkrnyppqyyaesfeq 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 214 --NKID-----DESAMSLWHPNLKLLLVTLGEKGCNYYTKKFHGTVGG-----FHVKTVDTTGAGDSFVGALLTKIVDDQ 281
Cdd:PLN02543 365 tkNWRDyyhytPEEIAPLWHDGLKLLLVTDGTLRIHYYTPKFDGVVVGtedvlITPFTCDRTGSGDAVVAAIMRKLTTCP 444
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 350534508 282 TILEDEARLKEVLRFSCACGAITTTKKGAIPALPTASEALTL 323
Cdd:PLN02543 445 EMFEDQDVLERQLRFAVAAGIISQWTIGAVRGFPTESATQNL 486
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
11-311 |
9.16e-71 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 221.83 E-value: 9.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 11 LIVSFGEMLIDFVPTVSGVS--LAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGI 88
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPgeLVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 89 NFDKGARTALAFVTLRADGEREFMFYRNPSADMLLTPAELNLDLIRSAKVFHYGSIslIVEPCRAAHMKAMEVAKEAGAL 168
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGS--LPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 169 lsYDPNLRLPLWPsaeeAKKQIKSIWDSADVIKVSDVELEFLTGSNKIDDESAM----SLWHPNLKLLLVTLGEKGCNYY 244
Cdd:pfam00294 159 --FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTGAKLDDIEEALaalhKLLAKGIKTVIVTLGADGALVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 350534508 245 TK-KFHGTVGGFHVKTVDTTGAGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAI 311
Cdd:pfam00294 233 EGdGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKS-------LEEALRFANAAAALVVQKSGAQ 293
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
12-324 |
4.53e-62 |
|
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: 199.75 E-value: 4.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVSGVSLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFD 91
Cdd:TIGR04382 4 VITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 92 KGARTALAFVTLRADGEREFMFYRNPSADMLLTPAELNLDLIRSAKVFHYGSISLIVEPCRAAHMKAMEVAKEAGALLSY 171
Cdd:TIGR04382 84 PGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 172 DPNLRLPLWPSAEEAKKQIKSIWDSADVIKVSDVELEFLTGSNKiDDESAMSLWHPNLKLLLVTLGEKGCNYYTKKFHG- 250
Cdd:TIGR04382 164 DIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGD-DEAAARALLDAGVEILVVKRGPEGSLVYTGDGEGv 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 350534508 251 TVGGFHVKTVDTTGAGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAIPALPTASEALTLL 324
Cdd:TIGR04382 243 EVPGFPVEVLNVLGAGDAFASGFLYGLLAGWD-------LEKALRYGNACGAIVVSRHSCSPAMPTLEELEAFL 309
|
|
| PLN02967 |
PLN02967 |
kinase |
37-303 |
1.62e-60 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 202.97 E-value: 1.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 37 FLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTLRADGEREFMFYRn 116
Cdd:PLN02967 238 FVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVK- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 117 PSADMLLTPAELNLDLIRSAKVFHYGSISLIVEPCRAAHMKAMEVAKEAGALLSYDPNLRLPLWPSAEEAKKQIKSIWDS 196
Cdd:PLN02967 317 PCAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 197 ADVIKVSDVELEFLTG---SNKIDD-------------ESAMSLWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVK-- 258
Cdd:PLN02967 397 ADIIEVTKQELEFLCGiepTEEFDTkdndkskfvhyspEVVAPLWHENLKVLFVTNGTSKIHYYTKEHNGAVHGMEDApi 476
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 350534508 259 ---TVDTTGAGDSFVGALLTKIVDDQTILEDEARLKEVLRFSCACGAI 303
Cdd:PLN02967 477 tpfTSDMSASGDGIVAGLMRMLTVQPHLITDKGYLEKTIKYAIDCGVI 524
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
33-316 |
1.22e-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: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 33 EAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTLRADGEREFM 112
Cdd:cd01174 27 LGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 113 FYrnPSADMLLTPAELN--LDLIRSAKVfhygsISLIVEPCRAAHMKAMEVAKEAGALLSYDPnlrLPlwpsaeeAKKQI 190
Cdd:cd01174 107 VV--PGANGELTPADVDaaLELIAAADV-----LLLQLEIPLETVLAALRAARRAGVTVILNP---AP-------ARPLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 191 KSIWDSADVIKVSDVELEFLTGSNKIDDES----AMSLWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAG 266
Cdd:cd01174 170 AELLALVDILVPNETEAALLTGIEVTDEEDaekaARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 350534508 267 DSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAIPALPT 316
Cdd:cd01174 250 DTFIGALAAALARGLS-------LEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
33-319 |
5.74e-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: 5.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 33 EAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTLRADGEREFM 112
Cdd:TIGR02152 22 HGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 113 FYrnPSADMLLTPAELN--LDLIRSAKVfhygsISLIVEPCRAAHMKAMEVAKEAGALLSYDPnlrlplwpsAEEAKKQI 190
Cdd:TIGR02152 102 VV--AGANAELTPEDIDaaEALIAESDI-----VLLQLEIPLETVLEAAKIAKKHGVKVILNP---------APAIKDLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 191 KSIWDSADVIKVSDVELEFLTGsNKIDDESAMS-----LWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGA 265
Cdd:TIGR02152 166 DELLSLVDIITPNETEAEILTG-IEVTDEEDAEkaaekLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVDTTAA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 350534508 266 GDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAIPALPTASE 319
Cdd:TIGR02152 245 GDTFNGAFAVALAEGKS-------LEDAIRFANAAAAISVTRKGAQSSIPYLEE 291
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
12-311 |
1.18e-29 |
|
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: 114.33 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVSGV----SLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEG 87
Cdd:cd01942 2 VAVVGHLNYDIILKVESFpgpfESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 88 INFDKGARTALAFVTlrADGEREFMFYRNPSADMLLTPAElNLDLIRSAKVFHYGSISLIVEpcraahmKAMEVAKEaGA 167
Cdd:cd01942 82 VRVVDEDSTGVAFIL--TDGDDNQIAYFYPGAMDELEPND-EADPDGLADIVHLSSGPGLIE-------LARELAAG-GI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 168 LLSYDPNLRLPLWpSAEEAKKQIKsiwdSADVIKVSDVELEFL---TGSNKIDDESamslwhpNLKLLLVTLGEKGCNYY 244
Cdd:cd01942 151 TVSFDPGQELPRL-SGEELEEILE----RADILFVNDYEAELLkerTGLSEAELAS-------GVRVVVVTLGPKGAIVF 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 350534508 245 TKKFHGTVGGFH-VKTVDTTGAGDSFVGALLTKIVDDQTIledearlKEVLRFSCACGAITTTKKGAI 311
Cdd:cd01942 219 EDGEEVEVPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYDL-------EESLRLGNLAASLKVERRGAQ 279
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
40-324 |
8.09e-29 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 112.66 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 40 APGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTLRADGERefMFYRNPSA 119
Cdd:PRK11142 37 AFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGEN--SIGIHAGA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 120 DMLLTPAELN--LDLIRSAKVFhygsisLI-VEPCRAAHMKAMEVAKEAGALLSYDPnlrLPLWPSAEEAKKQIksiwds 196
Cdd:PRK11142 115 NAALTPALVEahRELIANADAL------LMqLETPLETVLAAAKIAKQHGTKVILNP---APARELPDELLALV------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 197 aDVIKVSDVELEFLTGSNKIDDESAMS----LWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAGDSFVGA 272
Cdd:PRK11142 180 -DIITPNETEAEKLTGIRVEDDDDAAKaaqvLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGA 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 350534508 273 LLTKIVDDQTIleDEArlkevLRFSCACGAITTTKKGAIPALPTASEALTLL 324
Cdd:PRK11142 259 LVTALLEGKPL--PEA-----IRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
37-319 |
1.93e-26 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 106.75 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 37 FLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTL-RADGEREFMFYr 115
Cdd:PTZ00292 47 FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVdTKTGNNEIVII- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 116 nPSADMLLTPaelnlDLIRSAK--VFHYGSIsLIV--EPCRAAHMKAMEVAKEAGALLSYDPNlrlPLwPSAEEAkKQIK 191
Cdd:PTZ00292 126 -PGANNALTP-----QMVDAQTdnIQNICKY-LICqnEIPLETTLDALKEAKERGCYTVFNPA---PA-PKLAEV-EIIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 192 SIWDSADVIKVSDVELEFLTGSNKIDDESAMSLWHPNLKL----LLVTLGEKGCNYYTKKFHGT-VGGFHVKTVDTTGAG 266
Cdd:PTZ00292 194 PFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLgvenVIITLGANGCLIVEKENEPVhVPGKRVKAVDTTGAG 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 350534508 267 DSFVGALLTKIVDDqtiledeARLKEVLRFSCACGAITTTKKGAIPALPTASE 319
Cdd:PTZ00292 274 DCFVGSMAYFMSRG-------KDLKESCKRANRIAAISVTRHGTQSSYPHPSE 319
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
12-302 |
3.79e-25 |
|
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: 102.69 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVS------------GVSLAEAPGF---------LKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEF 70
Cdd:cd01168 4 VLGLGNALVDILAQVDdafleklglkkgDMILADMEEQeellaklpvKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 71 GHMLAGILKTNGVQAEgINFDKGARTALAFVTLRADGEREfmFYRNPSADMLLTPAELNLDLIRSAKVF---HYgsisLI 147
Cdd:cd01168 84 GDFLLKDLRAAGVDTR-YQVQPDGPTGTCAVLVTPDAERT--MCTYLGAANELSPDDLDWSLLAKAKYLyleGY----LL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 148 VEPCRAAhMKAMEVAKEAGALLS---YDPNLrlplwpsAEEAKKQIKSIWDSADVIKVSDVELEFLTGSNKIDD-ESAMS 223
Cdd:cd01168 157 TVPPEAI-LLAAEHAKENGVKIAlnlSAPFI-------VQRFKEALLELLPYVDILFGNEEEAEALAEAETTDDlEAALK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 224 LWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGF-HVKTVDTTGAGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGA 302
Cdd:cd01168 229 LLALRCRIVVITQGAKGAVVVEGGEVYPVPAIpVEKIVDTNGAGDAFAGGFLYGLVQGEP-------LEECIRLGSYAAA 301
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
42-316 |
3.95e-25 |
|
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: 102.37 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 42 GGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTLRA-DGEREFMFYRNPSAD 120
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITgDRATISITAIDTQAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 121 MLLTPAELnLDLIRsakvfhygsISLIVEPCRAAHMKAMEVAKEAG--ALLSYDPnlrlplwpsaeEAKKQIKSIWDSAD 198
Cdd:cd01945 116 PDSLPDAI-LGGAD---------AVLVDGRQPEAALHLAQEARARGipIPLDLDG-----------GGLRVLEELLPLAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 199 VIKVSDVELEFLTGSnkIDDESAMSLWHPNLKLLLVTLGEKGCNYY---TKKFHGTVggFHVKTVDTTGAGDSFVGALLT 275
Cdd:cd01945 175 HAICSENFLRPNTGS--ADDEALELLASLGIPFVAVTLGEAGCLWLerdGELFHVPA--FPVEVVDTTGAGDVFHGAFAH 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 350534508 276 KIVDDQTiledearLKEVLRFSCACGAITTTKKGAIPALPT 316
Cdd:cd01945 251 ALAEGMP-------LREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
40-310 |
1.63e-21 |
|
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: 92.03 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 40 APGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGArTALAFVTLRaDGEREFMFYR-NPS 118
Cdd:cd01940 20 YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGE-NAVADVELV-DGDRIFGLSNkGGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 119 ADMLltPAELNLDLIRSAKVFH---YGSISLIVEPCRAAHMkamevakeAGALLSYDPNLRlplwpsaeeakkqiksiWD 195
Cdd:cd01940 98 AREH--PFEADLEYLSQFDLVHtgiYSHEGHLEKALQALVG--------AGALISFDFSDR-----------------WD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 196 SADVIKVSD-VELEFLTGSNKIDDE---SAMSLWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAGDSFVG 271
Cdd:cd01940 151 DDYLQLVCPyVDFAFFSASDLSDEEvkaKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIA 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 350534508 272 ALLTkivddqTILEDEARLKEVLRFSCACGAITTTKKGA 310
Cdd:cd01940 231 GFLL------SLLAGGTAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
28-327 |
2.18e-20 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 91.88 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 28 GVSLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTLRADG 107
Cdd:COG3892 24 GGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSGVVTDPERLTALVLLGIRDDE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 108 EREFMFYRNPSADMLLTPAELNLDLIRSAKvfhygsiSLIV-------EPCRAAHMKAMEVAKEAGALLSYDPNLRLPLW 180
Cdd:COG3892 104 TFPLIFYRENCADMALTEDDIDEAFIASAR-------ALLItgthlshPRTRAAVLKALRYARAHGGKVVLDIDYRPVLW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 181 -------------PSAEEAkKQIKSIWDSADVIKVSDVELEFLTGSNKiDDESAMSLWHPNLKLLLVTLGEKGCNyytkK 247
Cdd:COG3892 177 gltghgdgetrfvASDAVT-AHLQEVLPLFDLIVGTEEEFHIAGGSTD-TLAALRAVRRVSTATLVCKRGALGCV----V 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 248 FHG----------TVGGFHVKTVDTTGAGDSFVGALLTKIVDDqtiLEDEARlkevLRFSCACGAITTTKKGAIPALPTA 317
Cdd:COG3892 251 FEGaipddlddgiTGPGFPVEVFNVLGAGDAFMSGFLRGWLRG---ESWETA----CAYANACGALVVSRHGCAPAMPTW 323
|
330
....*....|
gi 350534508 318 SEALTLLKGG 327
Cdd:COG3892 324 EELDYFLARG 333
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
43-328 |
9.73e-18 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 83.73 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 43 GAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGI--NFDKGARTALAFVTL----------------R 104
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLieGTDAGDSSSASYETLlcwvlvdplqrhgfcsR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 105 ADGEREFMFyrnpsADMLLTPAELNLDLIRSAKVFHYGSISLIVEPcrAAHMKAMEVAKEAGALLSYDPNLR-LPLWPSA 183
Cdd:PLN02341 200 ADFGPEPAF-----SWISKLSAEAKMAIRQSKALFCNGYVFDELSP--SAIASAVDYAIDVGTAVFFDPGPRgKSLLVGT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 184 EEAKKQIKSIWDSADVIKVSDVELEFLTG-SNKIDdeSAMSLWHPNL--KLLLVTLGEKGCNYYTKKFHGTVGGFHVKTV 260
Cdd:PLN02341 273 PDERRALEHLLRMSDVLLLTSEEAEALTGiRNPIL--AGQELLRPGIrtKWVVVKMGSKGSILVTRSSVSCAPAFKVNVV 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 350534508 261 DTTGAGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAIPALPTASEALTLLKGGA 328
Cdd:PLN02341 351 DTVGCGDSFAAAIALGYIHNLP-------LVNTLTLANAVGAATAMGCGAGRNVATLEKVLELLRASN 411
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
41-310 |
3.81e-17 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 79.78 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGaRTALAFVTLRaDGEREFMFY-RNPSA 119
Cdd:PRK09813 22 SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG-VTAQTQVELH-DNDRVFGDYtEGVMA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 120 DMLLTPAELNL----DLIRSAKVFHygsislivepcraAHmKAMEVAKEAGALLSYDPNLRL--PLWPSAEEakkqiksi 193
Cdd:PRK09813 100 DFALSEEDYAWlaqyDIVHAAIWGH-------------AE-DAFPQLHAAGKLTAFDFSDKWdsPLWQTLVP-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 194 wdsadvikvsdvELEFLTGSNKIDDE----SAMSLWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAGDSF 269
Cdd:PRK09813 158 ------------HLDYAFASAPQEDEflrlKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 350534508 270 VGALLTKIVDDQTIledearlKEVLRFSCACGAITTTKKGA 310
Cdd:PRK09813 226 IAGFLCGWLAGMTL-------PQAMAQGTACAAKTIQYHGA 259
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
12-304 |
4.59e-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: 80.05 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVSGVSLAEA--PGFLK-APGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGI 88
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTsnPGHVKqSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 89 NFdKGARTALAFVTLRADGEREFMFyrnpsADM----LLTPAELNL--DLIRSAK--VFHyGSISLIVepcraahMKAM- 159
Cdd:cd01941 82 VF-EGRSTASYTAILDKDGDLVVAL-----ADMdiyeLLTPDFLRKirEALKEAKpiVVD-ANLPEEA-------LEYLl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 160 EVAKEAGALLSYDPnlrlplwPSAEEAKKqIKSIWDSADVIKVSDVELEFLTG---SNKIDDESAMSLWH-PNLKLLLVT 235
Cdd:cd01941 148 ALAAKHGVPVAFEP-------TSAPKLKK-LFYLLHAIDLLTPNRAELEALAGaliENNEDENKAAKILLlPGIKNVIVT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350534508 236 LGEKGCnYYTKKFHGtVGGFHV------KTVDTTGAGDSFVGALLTKIVDDQtiledeaRLKEVLRFSCACGAIT 304
Cdd:cd01941 220 LGAKGV-LLSSREGG-VETKLFpapqpeTVVNVTGAGDAFVAGLVAGLLEGM-------SLDDSLRFAQAAAALT 285
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
41-273 |
1.05e-15 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 76.39 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGApANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTA--LAFVT-----LRADGEREFMF 113
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTtkTRVIAggqqlLRLDFEDRFPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 114 YRNPSADMLltpaELNLDLIRSAKV-----FHYGSISlivePCRAAHMkaMEVAKEAGALLSYDPNLRLPlwpsaeeakk 188
Cdd:COG2870 134 SAELEARLL----AALEAALPEVDAvilsdYGKGVLT----PELIQAL--IALARAAGKPVLVDPKGRDF---------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 189 qikSIWDSADVIKVSDVELEFLTGSNKIDDES-----AMSLWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTV-DT 262
Cdd:COG2870 194 ---SRYRGATLLTPNLKEAEAAVGIPIADEEElvaaaAELLERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVfDV 270
|
250
....*....|.
gi 350534508 263 TGAGDSFVGAL 273
Cdd:COG2870 271 TGAGDTVIATL 281
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
37-311 |
7.09e-15 |
|
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: 73.22 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 37 FLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGARTALAFVTlrADGEREFMFYRN 116
Cdd:cd01947 31 SRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFID--PNGERTITVPGE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 117 PSADMLLTPAELNLDLirsakVFHYGSISLIvepcraahmKAMEVAKEAGALLsYDPNLRLPLwpsaeeakKQIKSIWDS 196
Cdd:cd01947 109 RLEDDLKWPILDEGDG-----VFITAAAVDK---------EAIRKCRETKLVI-LQVTPRVRV--------DELNQALIP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 197 ADVIKVSDVELEFLTGSNKIddesAMslwhPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAGDSFVGALLTK 276
Cdd:cd01947 166 LDILIGSRLDPGELVVAEKI----AG----PFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYG 237
|
250 260 270
....*....|....*....|....*....|....*
gi 350534508 277 IVDDQTIledearlKEVLRFSCACGAITTTKKGAI 311
Cdd:cd01947 238 LLKGWSI-------EEALELGAQCGAICVSHFGPY 265
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
150-274 |
6.73e-13 |
|
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: 66.35 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 150 PCRAAHMKAMEVAKEAGALLSYDPNlrlplWPSAEEAKKQIKSIWDSADVIKVSDVELEFLTGSN---KIDDESAMSLWH 226
Cdd:cd00287 68 PAPEAVLDALEEARRRGVPVVLDPG-----PRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRdleVKEAAEAAALLL 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 350534508 227 PN-LKLLLVTLGEKGCNYYTKKFH-GTVGGFHVKTVDTTGAGDSFVGALL 274
Cdd:cd00287 143 SKgPKVVIVTLGEKGAIVATRGGTeVHVPAFPVKVVDTTGAGDAFLAALA 192
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
12-309 |
3.75e-12 |
|
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: 65.91 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVSGV--SLAEAPGFLKAP--GGApANVAIAVTRLGGKSAFVGKLGDDEFGHMLagilkTNGVQAEG 87
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLpaSGGDIEAKSKSYviGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQI-----RQAMRDEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 88 I--------NFDKGARTALafvtLRADGEREFMFYrnPSADMLLTPAELNLDLIRSAKVFHYGSISLIVEPCRAAHMKAM 159
Cdd:cd01944 76 IeillpprgGDDGGCLVAL----VEPDGERSFISI--SGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 160 EVAKEAGALLSYDPNLRLPLWPSAEeakkqIKSIWDSADVIKVSDVELEFLTGSNKIDDESAMSLWHPNLK-LLLVTLGE 238
Cdd:cd01944 150 LEALPAGTTLVFDPGPRISDIPDTI-----LQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAaPVVVRLGS 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350534508 239 KGCNYYTKKFH-GTVGGFHVKTVDTTGAGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKG 309
Cdd:cd01944 225 NGAWIRLPDGNtHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMS-------LADAVLLANAAAAIVVTRSG 289
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
41-321 |
4.49e-12 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 65.66 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGApANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINfDKGART-------ALAFVTLRADGEREFMF 113
Cdd:cd01172 39 LGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTttktrviARNQQLLRVDREDDSPL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 114 YRNPSADMLLTPAELnldlIRSAKV-----FHYGSISlivepcrAAHMKAM-EVAKEAGALLSYDPnlrlplwpsaeeaK 187
Cdd:cd01172 117 SAEEEQRLIERIAER----LPEADVvilsdYGKGVLT-------PRVIEALiAAARELGIPVLVDP-------------K 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 188 KQIKSIWDSADVIKVSDVELEFLTGSNKIDDES----AMSLWHP-NLKLLLVTLGEKGCNYY---TKKFHgtVGGFHVKT 259
Cdd:cd01172 173 GRDYSKYRGATLLTPNEKEAREALGDEINDDDEleaaGEKLLELlNLEALLVTLGEEGMTLFerdGEVQH--IPALAKEV 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350534508 260 VDTTGAGDSFVgALLTkivddqTILEDEARLKEVLRFSCACGAITTTKKGAIPAlpTASEAL 321
Cdd:cd01172 251 YDVTGAGDTVI-ATLA------LALAAGADLEEAAFLANAAAGVVVGKVGTAPV--TPKELL 303
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
41-325 |
5.93e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 65.16 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGAPANVAIAVTRLGGKSAFVGKLGDDEfGHMLAGILKTNGVQAEGINFDKGARTALAFVTlrADGEREFMFYrNPSAD 120
Cdd:COG1105 34 PGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETRINIKIVD--PSDGTETEIN-EPGPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 121 mlLTPAELN--LDLI-RSAKVFHY----GSISLIVEPCRAAHMkaMEVAKEAGALL---SYDPNLRLPLwpsaeEAKkqi 190
Cdd:COG1105 110 --ISEEELEalLERLeELLKEGDWvvlsGSLPPGVPPDFYAEL--IRLARARGAKVvldTSGEALKAAL-----EAG--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 191 ksiwdsADVIKVSDVELEFLTGSNKIDDES----AMSLWHPNLKLLLVTLGEKGCNYYTKK--FHGTVGgfHVKTVDTTG 264
Cdd:COG1105 178 ------PDLIKPNLEELEELLGRPLETLEDiiaaARELLERGAENVVVSLGADGALLVTEDgvYRAKPP--KVEVVSTVG 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350534508 265 AGDSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAipALPTASEALTLLK 325
Cdd:COG1105 250 AGDSMVAGFLAGLARGLD-------LEEALRLAVAAGAAAALSPGT--GLPDREDVEELLA 301
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
41-309 |
7.69e-12 |
|
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: 64.86 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGAPANVAIAVTRLGGKSAFVGKLGDDeFGHMLAGILKTNGVQAEGINFDKGARTAlafVTLRADGEREFMFyRNPSAD 120
Cdd:cd01164 35 AGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRIN---VKIKEEDGTETEI-NEPGPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 121 mlLTPAELN--LDLIRSAK-----VFHYGSISLIVEPCraAHMKAMEVAKEAGALLSYD---PNLRLPLwpsaeEAKkqi 190
Cdd:cd01164 110 --ISEEELEalLEKLKALLkkgdiVVLSGSLPPGVPAD--FYAELVRLAREKGARVILDtsgEALLAAL-----AAK--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 191 ksiwdsADVIKVSDVELEFLTGSNKIDDES----AMSLWHPNLKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAG 266
Cdd:cd01164 178 ------PFLIKPNREELEELFGRPLGDEEDviaaARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 350534508 267 DSFVGALLTKIVDDQTiledearLKEVLRFSCACGAITTTKKG 309
Cdd:cd01164 252 DSMVAGFVAGLAQGLS-------LEEALRLAVAAGSATAFSPG 287
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
41-325 |
4.64e-11 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 62.59 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGAPANVAIAVTRLGGKSAFVGKLGDDEfGHMLAGILKTNGVQAEGINFDKGARTALAFVTlraDGEREFMFyRNPSAd 120
Cdd:TIGR03168 34 AGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKE---SSGEETEL-NEPGP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 121 mLLTPAELN------LDLIRSAK-VFHYGSISLIVEPcrAAHMKAMEVAKEAGALLSYD---PNLRLPLwpsaeEAKkqi 190
Cdd:TIGR03168 108 -EISEEELEqlleklRELLASGDiVVISGSLPPGVPP--DFYAQLIAIARKKGAKVILDtsgEALREAL-----AAK--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 191 ksiwdsADVIKVSDVELEFLTGSNKIDDESAMSLWHPNLKL----LLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAG 266
Cdd:TIGR03168 177 ------PFLIKPNHEELEELFGRELKTLEEIIEAARELLDRgaenVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 350534508 267 DSFVGALLTKivddqtiLEDEARLKEVLRFSCACGAITTTKKGAipALPTASEALTLLK 325
Cdd:TIGR03168 251 DSMVAGFLAG-------LARGLSLEEALRFAVAAGSAAAFSPGT--GLPDPEDVEELLD 300
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
12-308 |
6.37e-11 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 61.65 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDFVPTVSGVSlaeapgflKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLagILKTNGVQaegINFD 91
Cdd:cd01937 2 IVIIGHVTIDEIVTNGSGV--------VKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWS--DLFDNGIE---VISL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 92 KGARTALAFVTLRADGEREFMFYRnPSADmlltPAELNLDLIRSAKVFHYGSISLIVEPcraahmkameVAKEAGALLSY 171
Cdd:cd01937 69 LSTETTTFELNYTNEGRTRTLLAK-CAAI----PDTESPLSTITAEIVILGPVPEEISP----------SLFRKFAFISL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 172 DPN--LRlplwpSAEEAKKQIKSIWDSADVIKVSDVELEFLTGSNKIDDESAMSLwhpnLKLLLVTLGEKGCNYYTKKFH 249
Cdd:cd01937 134 DAQgfLR-----RANQEKLIKCVILKLHDVLKLSRVEAEVISTPTELARLIKETG----VKEIIVTDGEEGGYIFDGNGK 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 350534508 250 GTVGGFHVKTVDTTGAGDSFVGALLTKIVddqtileDEARLKEVLRFscacGAITTTKK 308
Cdd:cd01937 205 YTIPASKKDVVDPTGAGDVFLAAFLYSRL-------SGKDIKEAAEF----AAAAAAKF 252
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
12-303 |
1.18e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 52.30 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 12 IVSFGEMLIDfvptVSGVSLA------EAPGFLK-APGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQ 84
Cdd:PRK09850 7 VVIIGSANID----VAGYSHEslnyadSNPGKIKfTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 85 AEGINFDKGARTAlAFVTLrADGEREFMFYRNpsaDMLLT---PAEL---NLDLIRSAKVfhygsislIVEPCRAAHMKA 158
Cdd:PRK09850 83 VDKCLIVPGENTS-SYLSL-LDNTGEMLVAIN---DMNISnaiTAEYlaqHREFIQRAKV--------IVADCNISEEAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 159 MEVAKEAGallsydpnlRLPLWPSAEEAKK--QIKSIWDSADVIKVSDVELEFLTG---SNKIDDESAMSLWHPN-LKLL 232
Cdd:PRK09850 150 AWILDNAA---------NVPVFVDPVSAWKcvKVRDRLNQIHTLKPNRLEAETLSGialSGREDVAKVAAWFHQHgLNRL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350534508 233 LVTLGEKGCnYYTKKFHGTVGGFHVKT--VDTTGAGDSFVGALLTKIVDDQTILEDearlkevLRFSCACGAI 303
Cdd:PRK09850 221 VLSMGGDGV-YYSDISGESGWSAPIKTnvINVTGAGDAMMAGLASCWVDGMPFAES-------VRFAQGCSSM 285
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
198-326 |
1.02e-06 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 49.51 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 198 DVIKVSDVELEFLTGSNKIDDESAMSLWHPNLKL----LLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAGDSFVGAL 273
Cdd:TIGR03828 178 FLIKPNDEELEELFGRELKTLEEIIEAARELLDLgaenVLISLGADGALLVTKEGALFAQPPKGEVVSTVGAGDSMVAGF 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 350534508 274 LTKIVDDQTiledearLKEVLRFSCACGAITTTKKGAipALPTASEALTLLKG 326
Cdd:TIGR03828 258 LAGLESGLS-------LEEALRLAVAAGSAAAFSEGT--GLPDPEDIEELLPQ 301
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
41-277 |
1.16e-06 |
|
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: 49.83 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGApANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQAegiNF----DKGARTALAFVT-----LRADGEREF 111
Cdd:PRK11316 50 PGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKC---DFvsvpTHPTITKLRVLSrnqqlIRLDFEEGF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 112 mfyRNPSADMLLTPAELNLDLIRSAKVFHYGSISLivepcraAHMKAM-EVAKEAGALLSYDPnlrlplwpsaeeaKKQI 190
Cdd:PRK11316 126 ---EGVDPQPLLERIEQALPSIGALVLSDYAKGAL-------ASVQAMiQLARKAGVPVLIDP-------------KGTD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 191 KSIWDSADVIKVSDVELEFLTGSNKIDDE---SAMSLWHP-NLKLLLVTLGEKGCNYYTKkfhgTVGGFHVKTV-----D 261
Cdd:PRK11316 183 FERYRGATLLTPNLSEFEAVVGKCKDEAElveKGMKLIADyDLSALLVTRSEQGMTLLQP----GKAPLHLPTQarevyD 258
|
250
....*....|....*.
gi 350534508 262 TTGAGDSFVGALLTKI 277
Cdd:PRK11316 259 VTGAGDTVISVLAAAL 274
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
42-274 |
9.82e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 46.71 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 42 GGAPANVAIAVTR-LGGKSAFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGArTALAFVTLRADGEREFmfyrNP--S 118
Cdd:PLN02379 86 GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGP-TAQCVCLVDALGNRTM----RPclS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 119 ADMLLTPAELNLDLIRSAK--VFHYG--SISLIVEpcraahmkAMEVAKEAGALLSYD-------PNLRLPLWPSAEEAK 187
Cdd:PLN02379 161 SAVKLQADELTKEDFKGSKwlVLRYGfyNLEVIEA--------AIRLAKQEGLSVSLDlasfemvRNFRSPLLQLLESGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 188 KQIksiwdsadVIKVSDVELEFLTGSNKIDDESAMSLWHPNLKLLLVTLGEKGCnyytKKFHGT-------VGGfhVKTV 260
Cdd:PLN02379 233 IDL--------CFANEDEARELLRGEQESDPEAALEFLAKYCNWAVVTLGSKGC----IARHGKevvrvpaIGE--TNAV 298
|
250
....*....|....
gi 350534508 261 DTTGAGDSFVGALL 274
Cdd:PLN02379 299 DATGAGDLFASGFL 312
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
41-309 |
5.36e-05 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 44.39 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 41 PGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHmLAGILKTNGVQAEGINFDKGARTALaFVTLRADGErEFMFYRnPSAD 120
Cdd:PRK10294 37 PGGGGINVARAIAHLGGSATAIFPAGGATGEH-LVSLLADENVPVATVEAKDWTRQNL-HVHVEASGE-QYRFVM-PGAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 121 mlLTPAELnldlirsakvfhygsislivepcRAAHMKAMEVakEAGALL----SYDPNLRLP-LWPSAEEAKKQ-IKSIW 194
Cdd:PRK10294 113 --LNEDEF-----------------------RQLEEQVLEI--ESGAILvisgSLPPGVKLEkLTQLISAAQKQgIRCII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 195 DSA-------------DVIKVSDVELEFLTGSN--KIDD--ESAMSLWHPN-LKLLLVTLGEKGCNYYTKKFHGTVGGFH 256
Cdd:PRK10294 166 DSSgdalsaalaigniELVKPNQKELSALVNRDltQPDDvrKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPP 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 350534508 257 VKTVDTTGAGDSFVGALLTKIVDDqtiledeARLKEVLRFSCACGAITTTKKG 309
Cdd:PRK10294 246 VKSQSTVGAGDSMVGAMTLKLAEN-------ASLEEMVRFGVAAGSAATLNQG 291
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
232-278 |
7.47e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 44.03 E-value: 7.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 350534508 232 LLVTLGEKGCNYYTKKFHGTVGGFHVKTVDTTGAGDSFVGALLTKIV 278
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLV 252
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
40-290 |
1.31e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 43.26 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 40 APGGAPANVAIAVTRLGGKS--------AFVGKLGDDEFGHMLAGILKTNGVQAEGINFDKGArTALAFVTLRADGEREF 111
Cdd:PLN02813 124 SAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGT-TGTVIVLTTPDAQRTM 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 112 MFYRNPSADMLLTPAELNldLIRSAKVF---HY-----GSISLIVEPCRAAHMKAMEVAKEAGallsyDPNLrlplwpsa 183
Cdd:PLN02813 203 LSYQGTSSTVNYDSCLAS--AISKSRVLvveGYlwelpQTIEAIAQACEEAHRAGALVAVTAS-----DVSC-------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 184 eeAKKQIKSIWD----SADVIKVSDVELEFLTG-SNKIDDESAMSLWHPNLKLLLVTLGEKGcnyytkKFHGTVGGFHV- 257
Cdd:PLN02813 268 --IERHRDDFWDvmgnYADILFANSDEARALCGlGSEESPESATRYLSHFCPLVSVTDGARG------SYIGVKGEAVYi 339
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 350534508 258 -----KTVDTTGAGDSFVG----ALLTKIVDDQTILEDEARL 290
Cdd:PLN02813 340 ppspcVPVDTCGAGDAYAAgilyGLLRGVSDLRGMGELAARV 381
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
184-299 |
4.57e-03 |
|
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: 38.22 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350534508 184 EEAKKQIKSIwdsaDVIKVSDVELEFLTG-SNKIDDESAMSLWHPnlKLLLVTLGEKGCNYYTKKFHGTVGGFHVKTV-D 261
Cdd:cd01946 155 EKLKKVLAKV----DVVIINDGEARQLTGaANLVKAARLILAMGP--KALIIKRGEYGALLFTDDGYFAAPAYPLESVfD 228
|
90 100 110
....*....|....*....|....*....|....*...
gi 350534508 262 TTGAGDSFVGALLTKIVDDQTIleDEARLKEVLRFSCA 299
Cdd:cd01946 229 PTGAGDTFAGGFIGYLASQKDT--SEANMRRAIIYGSA 264
|
|
| |
