|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02323 |
PLN02323 |
probable fructokinase |
55-384 |
0e+00 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 680.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 55 SSDGSTQESPYVVCFGEMLIDFVPTTSGLSLADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKD 134
Cdd:PLN02323 2 MTAPSTAESSLVVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 135 NNVNNDGMRFDPGARTALAFVTLTNEGEREFMFYRNPSADMLLEESELDFDLIKKAKIFHYGSISLITEPCKSAHISAAK 214
Cdd:PLN02323 82 NGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 215 AAKEAGVILSYDPNLRLPLWPSADNAREEILSIWETADIIKISEEEIVFLTKGEDPYDDNVVrKLFHPKLKLLLVTEGPE 294
Cdd:PLN02323 162 IAKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVV-KLWHPNLKLLLVTEGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 295 GCRYYTKDFSGRVHGLKVDVVDTTGAGDAFVAGILSQLANDLSLLQDEERLREALMFANACGALTVKVRGAIPALPTKEA 374
Cdd:PLN02323 241 GCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLEDEERLREALRFANACGAITTTERGAIPALPTKEA 320
|
330
....*....|
gi 22330456 375 VHEALLKAVV 384
Cdd:PLN02323 321 VLKLLKKAVA 330
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
66-366 |
1.09e-137 |
|
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: 394.31 E-value: 1.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTTSGlslaDAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFD 145
Cdd:cd01167 2 VVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 146 PGARTALAFVTLTNEGEREFMFYRNPSADMLLEEsELDFDLIKKAKIFHYGSISLITEPCKSAHISAAKAAKEAGVILSY 225
Cdd:cd01167 78 PAAPTTLAFVTLDADGERSFEFYRGPAADLLLDT-ELNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLISF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 226 DPNLRLPLWPSADNAREEILSIWETADIIKISEEEIVFLTKGEDPydDNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSG 305
Cdd:cd01167 157 DPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDP--EEIAALLLLFGLKLVLVTRGADGALLYTKGGVG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330456 306 RVHGLKVDVVDTTGAGDAFVAGILSQLANDLSLLQDEERLREALMFANACGALTVKVRGAI 366
Cdd:cd01167 235 EVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
66-375 |
3.49e-104 |
|
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: 309.51 E-value: 3.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTTSGL----SLADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDG 141
Cdd:COG0524 2 VLVIGEALVDLVARVDRLpkggETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 142 MRFDPGARTALAFVTLTNEGEREFMFYRnpSADMLLEESELDFDLIKKAKIFHYGSISLITEPCKSAHISAAKAAKEAGV 221
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 222 ILSYDPNLRLPLWpsaDNAREEILSIWETADIIKISEEEIVFLTKGEDPydDNVVRKLFHPKLKLLLVTEGPEGCRYYTK 301
Cdd:COG0524 160 PVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDP--EEAAAALLARGVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330456 302 DFSGRVHGLKVDVVDTTGAGDAFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRGAIPALPTKEAV 375
Cdd:COG0524 235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLD-------LEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
66-366 |
2.81e-92 |
|
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: 278.69 E-value: 2.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTTSGlSLADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFD 145
Cdd:cd01166 2 VVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 146 PGARTALAFVTLTNEGEREFMFYRNPSADMLLEESELDFDLIKKAKIFHYGSISL-ITEPCKSAHISAAKAAKEAGVILS 224
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLaLSESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 225 YDPNLRLPLWpSADNAREEILSIWETADIIKISEEEIVFLTKGEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFS 304
Cdd:cd01166 161 FDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALGVKAVVVKLGAEGALVYTGGGR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22330456 305 GRVHGLKVDVVDTTGAGDAFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRGAI 366
Cdd:cd01166 240 VFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWD-------LEEALRFANAAAALVVTRPGDI 294
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
70-372 |
4.48e-89 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 271.04 E-value: 4.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 70 GEMLIDFVPTTSGLSLadapafkKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGAR 149
Cdd:PRK09434 9 GDAVVDLIPEGENRYL-------KCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 150 TALAFVTLTNEGEREFMFYRNPSADMLLEESEL-DFdliKKAKIFHYGSISLITEPCKSAHISAAKAAKEAGVILSYDPN 228
Cdd:PRK09434 82 TSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLpPF---RQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 229 LRLPLWPSADNAREEILSIWETADIIKISEEEIVFLTkGEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVH 308
Cdd:PRK09434 159 LREDLWQDEAELRECLRQALALADVVKLSEEELCFLS-GTSQLEDAIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330456 309 GLKVDVVDTTGAGDAFVAGILSQLAnDLSLLQDEERLREALMFANACGALTVKVRGAIPALPTK 372
Cdd:PRK09434 238 APSVDPVDTTGAGDAFVAGLLAGLS-QAGLWTDEAELAEIIAQAQACGALATTAKGAMTALPNR 300
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
65-366 |
6.80e-84 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 257.27 E-value: 6.80e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 65 YVVCFGEMLIDFVPTTSGLS--LADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGM 142
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPgeLVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 143 RFDPGARTALAFVTLTNEGEREFMFYRNPSADMLLEESELDFDLIKKAKIFHYGSIslITEPCKSAHISAAKAAKEAGVI 222
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGS--LPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 223 lsYDPNLRLPLWPsadnAREEILSIWETADIIKISEEEIVFLTkGEDPYDDNVVRKLFHPKL----KLLLVTEGPEGCRY 298
Cdd:pfam00294 159 --FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALT-GAKLDDIEEALAALHKLLakgiKTVIVTLGADGALV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330456 299 YTKDFSGRVHGL-KVDVVDTTGAGDAFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRGAI 366
Cdd:pfam00294 232 VEGDGEVHVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKS-------LEEALRFANAAAALVVQKSGAQ 293
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
66-379 |
3.69e-66 |
|
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: 212.07 E-value: 3.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTTSGLSLADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFD 145
Cdd:TIGR04382 4 VITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 146 PGARTALAFVTLTNEGEREFMFYRNPSADMLLEESELDFDLIKKAKIFHYGSISLITEPCKSAHISAAKAAKEAGVILSY 225
Cdd:TIGR04382 84 PGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 226 DPNLRLPLWPSADNAREEILSIWETADIIKISEEEivFLTKGEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSG 305
Cdd:TIGR04382 164 DIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREE--FDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGEG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330456 306 -RVHGLKVDVVDTTGAGDAFVAGILSqlandlSLLQDEErLREALMFANACGALTVKVRGAIPALPTKEAVHEAL 379
Cdd:TIGR04382 242 vEVPGFPVEVLNVLGAGDAFASGFLY------GLLAGWD-LEKALRYGNACGAIVVSRHSCSPAMPTLEELEAFL 309
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
19-374 |
1.58e-61 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 205.91 E-value: 1.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 19 STPHSLTSKRPISIKATTSSPSRLSNSRSNLKGRALSSDGstQESPY-----VVCFGEMLIDFVPT-------------T 80
Cdd:PLN02543 78 SPPKAKTTRRRTKKTDQELDPEGAEEDQEAAEDGEDYDDG--IDFPYddpplVCCFGAVQKEFVPTvrvhdnqmhpdmyS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 81 SGLSLA-DAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTALAF--VTL 157
Cdd:PLN02543 156 QWKMLQwDPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRmkIKF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 158 TNEGEREFMFYRNPSADMLLeESELDFDLIKKAKIFHYGSISLITEPCKSAHISAAKAAKEAGVILSYDPNLRLPLWPSA 237
Cdd:PLN02543 236 RDGGKMVAETVKEAAEDSLL-ASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSR 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 238 DNAREEILSIWETADIIKISEEEIVFLTKGE--------------DPYDDNVVRK------------LFHPKLKLLLVTE 291
Cdd:PLN02543 315 DETRELIKKAWNEADIIEVSRQELEFLLDEDyyerkrnyppqyyaESFEQTKNWRdyyhytpeeiapLWHDGLKLLLVTD 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 292 GPEGCRYYTKDFSGRVHGLKvDVV------DTTGAGDAFVAGILSQLANDLSLLQDEERLREALMFANACGALTVKVRGA 365
Cdd:PLN02543 395 GTLRIHYYTPKFDGVVVGTE-DVLitpftcDRTGSGDAVVAAIMRKLTTCPEMFEDQDVLERQLRFAVAAGIISQWTIGA 473
|
....*....
gi 22330456 366 IPALPTKEA 374
Cdd:PLN02543 474 VRGFPTESA 482
|
|
| PLN02967 |
PLN02967 |
kinase |
64-377 |
3.02e-55 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 191.03 E-value: 3.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 64 PYVVCFGEMLIDFVPT-TSGLSLAD------------AP-AFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLA 129
Cdd:PLN02967 197 PLVCCFGAAQHAFVPSgRPANRLLDyeihermkdafwAPeKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAML 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 130 NILKDNNVNNDGMRFDPGARTALAFVTLTNEGEREFMFYRnPSADMLLEESELDFDLIKKAKIFHYGSISLITEPCKSAH 209
Cdd:PLN02967 277 YYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVK-PCAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 210 ISAAKAAKEAGVILSYDPNLRLPLWPSADNAREEILSIWETADIIKISEEEIVFL----------TKGEDP-----YDDN 274
Cdd:PLN02967 356 LRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNLADIIEVTKQELEFLcgiepteefdTKDNDKskfvhYSPE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 275 VVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVV-----DTTGAGDAFVAGILSQLANDLSLLQDEERLREAL 349
Cdd:PLN02967 436 VVAPLWHENLKVLFVTNGTSKIHYYTKEHNGAVHGMEDAPItpftsDMSASGDGIVAGLMRMLTVQPHLITDKGYLEKTI 515
|
330 340
....*....|....*....|....*...
gi 22330456 350 MFANACGALTVKVRGAIPALPTKEAVHE 377
Cdd:PLN02967 516 KYAIDCGVIDQWLLARTRGFPPKEDMED 543
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
88-371 |
3.06e-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: 170.42 E-value: 3.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 88 APAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTALAFVTLTNEGEREFMF 167
Cdd:cd01174 28 GSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 168 YrnPSADMLL--EESELDFDLIKKAKIfhygsISLITEPCKSAHISAAKAAKEAGVILSYDPnlrLPlwpsadnAREEIL 245
Cdd:cd01174 108 V--PGANGELtpADVDAALELIAAADV-----LLLQLEIPLETVLAALRAARRAGVTVILNP---AP-------ARPLPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 246 SIWETADIIKISEEEIVFLT--KGEDPYDDNVVRKLFHPK-LKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGD 322
Cdd:cd01174 171 ELLALVDILVPNETEAALLTgiEVTDEEDAEKAARLLLAKgVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGD 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 22330456 323 AFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRGAIPALPT 371
Cdd:cd01174 251 TFIGALAAALARGLS-------LEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
88-375 |
5.63e-47 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 162.00 E-value: 5.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 88 APAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTALAFVTLTNEGEREFMF 167
Cdd:TIGR02152 23 GHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 168 YrnPSADMLLEESELD--FDLIKKAKIfhygsISLITEPCKSAHISAAKAAKEAGVILSYDPNlrlplwPSADNAREEIL 245
Cdd:TIGR02152 103 V--AGANAELTPEDIDaaEALIAESDI-----VLLQLEIPLETVLEAAKIAKKHGVKVILNPA------PAIKDLDDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 246 SiweTADIIKISEEEIVFLT--KGEDPYDDNVVRKLFHPK-LKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGD 322
Cdd:TIGR02152 170 S---LVDIITPNETEAEILTgiEVTDEEDAEKAAEKLLEKgVKNVIITLGSKGALLVSKDESKLIPAFKVKAVDTTAAGD 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 22330456 323 AFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRGAIPALPTKEAV 375
Cdd:TIGR02152 247 TFNGAFAVALAEGKS-------LEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
66-367 |
3.28e-43 |
|
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: 152.77 E-value: 3.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTTS------------GLSLADAPAF---------KKAPGGAPANVAVGIARLGGSSAFIGKVGEDEF 124
Cdd:cd01168 4 VLGLGNALVDILAQVDdafleklglkkgDMILADMEEQeellaklpvKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 125 GYMLANILKDNNVNNDGMRfDPGARTALAFVTLTNEGEREfmFYRNPSADMLLEESELDFDLIKKAKIF---HYgsisLI 201
Cdd:cd01168 84 GDFLLKDLRAAGVDTRYQV-QPDGPTGTCAVLVTPDAERT--MCTYLGAANELSPDDLDWSLLAKAKYLyleGY----LL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 202 TEPCKSAhISAAKAAKEAGVILS---YDPNLrlplwpsADNAREEILSIWETADIIKISEEEIVFLTKGEDPYDDNVVRK 278
Cdd:cd01168 157 TVPPEAI-LLAAEHAKENGVKIAlnlSAPFI-------VQRFKEALLELLPYVDILFGNEEEAEALAEAETTDDLEAALK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 279 LFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVD-VVDTTGAGDAFVAGILSQLANDLSllqdeerLREALMFANACGA 357
Cdd:cd01168 229 LLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQGEP-------LEECIRLGSYAAA 301
|
330
....*....|
gi 22330456 358 LTVKVRGAIP 367
Cdd:cd01168 302 EVIQQLGPRL 311
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
66-366 |
3.55e-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: 149.00 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTtsGLSLAD------APAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNN 139
Cdd:cd01942 2 VAVVGHLNYDIILK--VESFPGpfesvlVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 140 DGMRFDPGARTALAFVTLTNEGERefMFYRNPSADMLLEESELDfDLIKKAKIFHYGSIslitepckSAHISAAKAAKEA 219
Cdd:cd01942 80 SHVRVVDEDSTGVAFILTDGDDNQ--IAYFYPGAMDELEPNDEA-DPDGLADIVHLSSG--------PGLIELARELAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 220 GVILSYDPNLRLPLWPSadnarEEILSIWETADIIKISEEEI-VFLTK-GEDPYDDNVvrklfhpKLKLLLVTEGPEGCR 297
Cdd:cd01942 149 GITVSFDPGQELPRLSG-----EELEEILERADILFVNDYEAeLLKERtGLSEAELAS-------GVRVVVVTLGPKGAI 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 298 YYTKDFSGRVHGLK-VDVVDTTGAGDAFVAGILSQLANDLSLlqdEERLRealmFANACGALTVKVRGAI 366
Cdd:cd01942 217 VFEDGEEVEVPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYDL---EESLR----LGNLAASLKVERRGAQ 279
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
82-374 |
5.53e-34 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 133.09 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 82 GLSLADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTALAFVTLTNEG 161
Cdd:COG3892 24 GGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSGVVTDPERLTALVLLGIRDDE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 162 EREFMFYRNPSADMLLEESELDFDLIKKAKIFHYGSISLITEPCKSAHISAAKAAKEAG--VILSYDPnlRLPLW----- 234
Cdd:COG3892 104 TFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARAHGgkVVLDIDY--RPVLWgltgh 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 235 --------PSADNARE--EILSIWetaDIIKISEEEIVFLTKGEDpyDDNVVRKLFHPKLKLLLVTEGPEGCRYYT---- 300
Cdd:COG3892 182 gdgetrfvASDAVTAHlqEVLPLF---DLIVGTEEEFHIAGGSTD--TLAALRAVRRVSTATLVCKRGALGCVVFEgaip 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22330456 301 ----KDFSGRvhGLKVDVVDTTGAGDAFVAGILsqlandLSLLQDEErLREALMFANACGALTVKVRGAIPALPTKEA 374
Cdd:COG3892 257 ddldDGITGP--GFPVEVFNVLGAGDAFMSGFL------RGWLRGES-WETACAYANACGALVVSRHGCAPAMPTWEE 325
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
92-365 |
2.23e-28 |
|
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: 111.68 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 92 KKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGArTALAFVTLTNeGEREFMFYR-N 170
Cdd:cd01940 18 KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGE-NAVADVELVD-GDRIFGLSNkG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 171 PSADMLLEESelDFDLIKKAKIFH---YGSISLITEPCKSAHIsaakaakeAGVILSYDpnlrlplwpSADNAREEilsI 247
Cdd:cd01940 96 GVAREHPFEA--DLEYLSQFDLVHtgiYSHEGHLEKALQALVG--------AGALISFD---------FSDRWDDD---Y 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 248 WETAdiikISEEEIVFLTKGEDPYDD--NVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGDAFV 325
Cdd:cd01940 154 LQLV----CPYVDFAFFSASDLSDEEvkAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 22330456 326 AGILsqlandLSLLQDEERLREALMFANACGALTVKVRGA 365
Cdd:cd01940 230 AGFL------LSLLAGGTAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
66-371 |
2.77e-26 |
|
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: 106.61 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTTSGLSLAD----APAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDG 141
Cdd:cd01945 2 VLGVGLAVLDLIYLVASFPGGDgkivATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 142 MRFDPGARTALAFVTLtNEGEREFMFYRN----PSADMLLEESELDFDLIkkakifhygsisLITEPCKSAHISAAKAAK 217
Cdd:cd01945 82 IVVAPGARSPISSITD-ITGDRATISITAidtqAAPDSLPDAILGGADAV------------LVDGRQPEAALHLAQEAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 218 EAGV--ILSYDpnlrlplwPSADNAREEILSIwetADIIKISEEeiVFLTKGEDPyDDNVVRKLFHPKLKLLLVTEGPEG 295
Cdd:cd01945 149 ARGIpiPLDLD--------GGGLRVLEELLPL---ADHAICSEN--FLRPNTGSA-DDEALELLASLGIPFVAVTLGEAG 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22330456 296 CRYYTKDfSGRVHG--LKVDVVDTTGAGDAFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRGAIPALPT 371
Cdd:cd01945 215 CLWLERD-GELFHVpaFPVEVVDTTGAGDVFHGAFAHALAEGMP-------LREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
94-382 |
1.79e-25 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 104.57 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 94 APGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTALAFVTLTNEGEREFMFYRNPSA 173
Cdd:PRK11142 37 AFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 174 DMLLEESELDFDLIKKAkifHYGSISLITePCKSAhISAAKAAKEAG--VILSYDPNLRLPlwpsadnarEEILSIwetA 251
Cdd:PRK11142 117 ALTPALVEAHRELIANA---DALLMQLET-PLETV-LAAAKIAKQHGtkVILNPAPARELP---------DELLAL---V 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 252 DIIKISEEEIVFLTKGEDPYDDNVVR--KLFHPK-LKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGD----AF 324
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKaaQVLHQKgIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDtfngAL 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 22330456 325 VAGILSQLAndlsllqdeerLREALMFANACGALTVKVRGAIPALPTKEAVhEALLKA 382
Cdd:PRK11142 260 VTALLEGKP-----------LPEAIRFAHAAAAIAVTRKGAQPSIPWREEI-DAFLQE 305
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
55-373 |
7.38e-24 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 100.58 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 55 SSDGSTQESPYVV---CFGEMLI--DFVPTTSGLSLADApaFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGY-ML 128
Cdd:PTZ00292 8 ASHGGEAEPDVVVvgsSNTDLIGyvDRMPQVGETLHGTS--FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSdTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 129 ANiLKDNNVNNDGMRFDPGARTALAFVTL-TNEGEREFMFYrnPSADMLLEESELDfdlIKKAKIFHYGSISLI-TEPCK 206
Cdd:PTZ00292 86 KN-FKRNGVNTSFVSRTENSSTGLAMIFVdTKTGNNEIVII--PGANNALTPQMVD---AQTDNIQNICKYLICqNEIPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 207 SAHISAAKAAKEAGVILSYDPNlrlPLwPSADNArEEILSIWETADIIKISEEEIVFLTkGEDPYDDNVVRKLFHPKLKL 286
Cdd:PTZ00292 160 ETTLDALKEAKERGCYTVFNPA---PA-PKLAEV-EIIKPFLKYVSLFCVNEVEAALIT-GMEVTDTESAFKASKELQQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 287 ----LLVTEGPEGCRYYTKDfSGRVH--GLKVDVVDTTGAGDAFVAGILSQLANDLSLLQDEERlrealmfANACGALTV 360
Cdd:PTZ00292 234 gvenVIITLGANGCLIVEKE-NEPVHvpGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKR-------ANRIAAISV 305
|
330
....*....|...
gi 22330456 361 KVRGAIPALPTKE 373
Cdd:PTZ00292 306 TRHGTQSSYPHPS 318
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
92-368 |
2.33e-22 |
|
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: 96.09 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 92 KKAPGGApANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRfDPGARTA--LAFVTLTNEgerefMF-- 167
Cdd:cd01172 36 EIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTTtkTRVIARNQQ-----LLrv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 168 -YRNPSADMLLEESELDFDLIKKAKIFH------YGSISLITEPCKSAHisaaKAAKEAGVILSYDPnlrlplwpsadna 240
Cdd:cd01172 109 dREDDSPLSAEEEQRLIERIAERLPEADvvilsdYGKGVLTPRVIEALI----AAARELGIPVLVDP------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 241 REEILSIWETADIIKISEEEIVFLTKGEDPYDDNVV---RKLFHPK-LKLLLVTEGPEGCRYYTKDfSGRVH--GLKVDV 314
Cdd:cd01172 172 KGRDYSKYRGATLLTPNEKEAREALGDEINDDDELEaagEKLLELLnLEALLVTLGEEGMTLFERD-GEVQHipALAKEV 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 22330456 315 VDTTGAGDAFVAGILSQLANDLSLLqdeerlrEALMFANACGALTVKVRGAIPA 368
Cdd:cd01172 251 YDVTGAGDTVIATLALALAAGADLE-------EAAFLANAAAGVVVGKVGTAPV 297
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
91-366 |
1.48e-21 |
|
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: 92.87 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 91 FKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTALAFVtlTNEGEREFMFYRN 170
Cdd:cd01947 31 SRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFI--DPNGERTITVPGE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 171 PSADMlLEESELD-FDLikkakIFHYGSISLITepcksahiSAAKAAKEAGVILSYDPNLRLplwpsadnarEEILSIWE 249
Cdd:cd01947 109 RLEDD-LKWPILDeGDG-----VFITAAAVDKE--------AIRKCRETKLVILQVTPRVRV----------DELNQALI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 250 TADIIKISEEEIVFLTKGEdpyddnvvrKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGDAFVAGIL 329
Cdd:cd01947 165 PLDILIGSRLDPGELVVAE---------KIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFI 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 22330456 330 SQLANDLSllqdeerLREALMFANACGALTVKVRGAI 366
Cdd:cd01947 236 YGLLKGWS-------IEEALELGAQCGAICVSHFGPY 265
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
92-365 |
9.00e-21 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 90.57 E-value: 9.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 92 KKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGaRTALAFVTLTNeGEREFMFY-RN 170
Cdd:PRK09813 19 KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG-VTAQTQVELHD-NDRVFGDYtEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 171 PSADMLLEESELDF----DLIKKAKifhYGsislitepcksaHISAAKAA-KEAGVILSYDPNLRL--PLW----PSADN 239
Cdd:PRK09813 97 VMADFALSEEDYAWlaqyDIVHAAI---WG------------HAEDAFPQlHAAGKLTAFDFSDKWdsPLWqtlvPHLDY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 240 AreeilsiwetadiikiseeeivFLT-KGEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTT 318
Cdd:PRK09813 162 A----------------------FASaPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTM 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 22330456 319 GAGDAFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRGA 365
Cdd:PRK09813 220 GAGDSFIAGFLCGWLAGMT-------LPQAMAQGTACAAKTIQYHGA 259
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
95-360 |
6.10e-20 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 89.49 E-value: 6.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 95 PGGApANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTalafVTLTnegeReFM-------- 166
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPT----TTKT----R-VIaggqqllr 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 167 --FYRNPSADMLLEESELDF--DLIKKAKI-----FHYGsisLITEPCKSAHIsaaKAAKEAGVILSYDPNLRLplwpsa 237
Cdd:COG2870 125 ldFEDRFPLSAELEARLLAAleAALPEVDAvilsdYGKG---VLTPELIQALI---ALARAAGKPVLVDPKGRD------ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 238 dnareeiLSIWETADIIKISEEEIVFLTKGEDPYDDNVVRK----LFHPKLKLLLVTEGPEGCRYYTKDfsGRVHGL--- 310
Cdd:COG2870 193 -------FSRYRGATLLTPNLKEAEAAVGIPIADEEELVAAaaelLERLGLEALLVTRGEEGMTLFDAD--GPPHHLpaq 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 22330456 311 KVDVVDTTGAGDAFVAGILSQLANDLSllqdeerLREALMFANACGALTV 360
Cdd:COG2870 264 AREVFDVTGAGDTVIATLALALAAGAS-------LEEAAELANLAAGIVV 306
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
1-382 |
1.43e-19 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 89.89 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 1 MALQATTTTF----CFSGPTFRSTPHSLTSKRPISIK----ATTSSPSRLSNSRSNLKGRALSSDGSTQESPY-VVCFGE 71
Cdd:PLN02341 1 MQAHRLIGQLgafsPHPGLSSPPSPHGHLVPRRVCSRcrasARASSRARAGARSRARRRLGDTEVGSAAGKEIdVATLGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 72 MLIDFV-------PTTSGLS-------LADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNV 137
Cdd:PLN02341 81 LCVDIVlpvpelpPPSREERkaymeelAASPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 138 NNDGM--------RFDPGARTALAFVTLTNEGEREFM----FYRNPSADMLLEESELDFDLIKKAK-IFHYGSISLITEP 204
Cdd:PLN02341 161 SVVGLiegtdagdSSSASYETLLCWVLVDPLQRHGFCsradFGPEPAFSWISKLSAEAKMAIRQSKaLFCNGYVFDELSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 205 ckSAHISAAKAAKEAGVILSYDPNLRLPLWPSADNAREEILS-IWETADIIKISEEEIVFLTKGEDPYDdnVVRKLFHPK 283
Cdd:PLN02341 241 --SAIASAVDYAIDVGTAVFFDPGPRGKSLLVGTPDERRALEhLLRMSDVLLLTSEEAEALTGIRNPIL--AGQELLRPG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 284 L--KLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGDAFVAGILSQLANDLSLLqdeerlrEALMFANACGALTVK 361
Cdd:PLN02341 317 IrtKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLV-------NTLTLANAVGAATAM 389
|
410 420
....*....|....*....|.
gi 22330456 362 VRGAIPALPTKEAVHEaLLKA 382
Cdd:PLN02341 390 GCGAGRNVATLEKVLE-LLRA 409
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
95-384 |
1.08e-18 |
|
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: 85.70 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 95 PGGAPANVAVGIARLGGSSAFIGKVGEDEFGYmLANILKDNNVNNDGMRFDPGARTALAFVTLTNEgEREFMFY----RN 170
Cdd:TIGR03168 34 AGGKGINVARVLARLGAEVVATGFLGGFTGEF-IEALLAEEGIKNDFVEVKGETRINVKIKESSGE-ETELNEPgpeiSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 171 PSADMLLEESEldfDLIKKAKIFHY-GSISLITEPCKSAHISAAKAAKEAGVI-----------LSYDPNLRLPlwpsad 238
Cdd:TIGR03168 112 EELEQLLEKLR---ELLASGDIVVIsGSLPPGVPPDFYAQLIAIARKKGAKVIldtsgealreaLAAKPFLIKP------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 239 NAREeilsIWETADIIKISEEEIVfltkgedpyddNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTT 318
Cdd:TIGR03168 183 NHEE----LEELFGRELKTLEEII-----------EAARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTV 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330456 319 GAGDAFVAGILSQLANDLSLlqdEERLRealmFANACGALTVKVRGAipALPTKEAVhEALLKAVV 384
Cdd:TIGR03168 248 GAGDSMVAGFLAGLARGLSL---EEALR----FAVAAGSAAAFSPGT--GLPDPEDV-EELLDQVT 303
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
72-364 |
1.57e-18 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 84.78 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 72 MLIDFVPTTSGLSLADAPAFKKapGGApANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRfDPGARTA 151
Cdd:cd01944 14 LDVDKLPASGGDIEAKSKSYVI--GGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPP-RGGDDGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 152 LAFVTLTNEGEREFMFYRNPSADMLLEeselDFDLIKKA--KIFHYGSISLITEPCKSAHISAAKAAKEAGVILSYDPNL 229
Cdd:cd01944 90 CLVALVEPDGERSFISISGAEQDWSTE----WFATLTVApyDYVYLSGYTLASENASKVILLEWLEALPAGTTLVFDPGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 230 RLPLWPsadnaREEILSIWETADIIKISEEEIVFLTKGEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKD-FSGRVH 308
Cdd:cd01944 166 RISDIP-----DTILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDgNTHIIP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 22330456 309 GLKVDVVDTTGAGDAFVAGILSQLANDLSllqdeerLREALMFANACGALTVKVRG 364
Cdd:cd01944 241 GFKVKAVDTIGAGDTHAGGMLAGLAKGMS-------LADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
95-383 |
1.03e-17 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 82.88 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 95 PGGAPANVAVGIARLGGSSAFIGKVGEDEfGYMLANILKDNNVNNDGMRFDPGARTALAFVTLTNEGEREFMFYRNPsad 174
Cdd:COG1105 34 PGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETRINIKIVDPSDGTETEINEPGPE--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 175 mlLEESELD------FDLIKKAKIFh-yGSISLITEPCKSAHIsaAKAAKEAG--VIL-SYDPNLRlplwpsadnareEI 244
Cdd:COG1105 110 --ISEEELEallerlEELLKEGDWVvlsGSLPPGVPPDFYAEL--IRLARARGakVVLdTSGEALK------------AA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 245 LSiwETADIIKISEEEIVFLTKGEDPYDDNVV---RKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAG 321
Cdd:COG1105 174 LE--AGPDLIKPNLEELEELLGRPLETLEDIIaaaRELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAG 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22330456 322 DAFVAGILSQLANDLSLlqdEERLRealmFANACGALTVKVRGAipALPTKEAVhEALLKAV 383
Cdd:COG1105 252 DSMVAGFLAGLARGLDL---EEALR----LAVAAGAAAALSPGT--GLPDREDV-EELLAQV 303
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
212-333 |
2.23e-17 |
|
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: 79.45 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 212 AAKAAKEAGVILSYDPNlrlplWPSADNAREEILSIWETADIIKISEEEIVFLTKGEDP---YDDNVVRKLFHPKLKLLL 288
Cdd:cd00287 76 ALEEARRRGVPVVLDPG-----PRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLevkEAAEAAALLLSKGPKVVI 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 22330456 289 VTEGPEGCRYYTKDF-SGRVHGLKVDVVDTTGAGDAFVAGILSQLA 333
Cdd:cd00287 151 VTLGEKGAIVATRGGtEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
65-360 |
1.45e-15 |
|
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: 76.20 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 65 YVVCFGEMLIDFVPTTSGLSLADA--PA-FKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDG 141
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTsnPGhVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 142 MRFdPGARTALAFVTLTNEGEREFMFyrnpsADM----LLEESELDF--DLIKKAK-IFHYGSISLITepckSAHIsaAK 214
Cdd:cd01941 81 IVF-EGRSTASYTAILDKDGDLVVAL-----ADMdiyeLLTPDFLRKirEALKEAKpIVVDANLPEEA----LEYL--LA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 215 AAKEAGVILSYDPnlrlplwPSADNAReEILSIWETADIIKISEEEIVFLT--KGEDPYDDNVVRKLFH-PKLKLLLVTE 291
Cdd:cd01941 149 LAAKHGVPVAFEP-------TSAPKLK-KLFYLLHAIDLLTPNRAELEALAgaLIENNEDENKAAKILLlPGIKNVIVTL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330456 292 GPEGCRYYTKDFSGRVH----GLKVDVVDTTGAGDAFVAGILSQLANDLsllqdeeRLREALMFANACGALTV 360
Cdd:cd01941 221 GAKGVLLSSREGGVETKlfpaPQPETVVNVTGAGDAFVAGLVAGLLEGM-------SLDDSLRFAQAAAALTL 286
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
95-360 |
1.14e-13 |
|
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: 70.64 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 95 PGGAPANVAVGIARLGGSSAFIGKVGEDeFGYMLANILKDNNVNNDGMRFDPGARTAlafVTLTNEGEREFMFyRNPSAD 174
Cdd:cd01164 35 AGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRIN---VKIKEEDGTETEI-NEPGPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 175 mlLEESELD------FDLIKKAKIFHY-GSISLITEPckSAHISAAKAAKEAGV-------------ILSYDPNLRLPlw 234
Cdd:cd01164 110 --ISEEELEalleklKALLKKGDIVVLsGSLPPGVPA--DFYAELVRLAREKGArvildtsgeallaALAAKPFLIKP-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 235 psadNAREeiLSIWetADIIKISEEEIVfltkgedpyddNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDV 314
Cdd:cd01164 184 ----NREE--LEEL--FGRPLGDEEDVI-----------AAARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22330456 315 VDTTGAGDAFVAGILSQLANDLSLlqdEERLRealmFANACGALTV 360
Cdd:cd01164 245 VSTVGAGDSMVAGFVAGLAQGLSL---EEALR----LAVAAGSATA 283
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
95-384 |
4.00e-12 |
|
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: 66.46 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 95 PGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANiLKDNNVNNDGMRFDPGARTAlafVTLTNEGEREFM-----FYR 169
Cdd:TIGR03828 34 AGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEAL-LREEGIKTDFVRVPGETRIN---VKIKEPSGTETKlngpgPEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 170 NPSA-DMLLEESEldfDLIKKAKIFHY-GSISLITEPCKSAHISAAKAAKEAGVIL-SYDPNLRLplwpsadnareeilS 246
Cdd:TIGR03828 110 SEEElEALLEKLR---AQLAEGDWLVLsGSLPPGVPPDFYAELIALAREKGAKVILdTSGEALRD--------------G 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 247 IWETADIIKISEEEIVFLTKGEDPYDDNVV---RKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGDA 323
Cdd:TIGR03828 173 LKAKPFLIKPNDEELEELFGRELKTLEEIIeaaRELLDLGAENVLISLGADGALLVTKEGALFAQPPKGEVVSTVGAGDS 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330456 324 FVAGILSQLANDLSLlqdEERLRealmFANACGALTVKVRGAipALPTKEAVhEALLKAVV 384
Cdd:TIGR03828 253 MVAGFLAGLESGLSL---EEALR----LAVAAGSAAAFSEGT--GLPDPEDI-EELLPQVT 303
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
87-338 |
1.12e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 65.58 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 87 DAPAFKKAPGGAPANVAVGIAR-LGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGArTALAFVTLTNEGEREF 165
Cdd:PLN02379 77 DLSPIKTMAGGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGP-TAQCVCLVDALGNRTM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 166 mfyrNP--SADMLLEESELDFDLIKKAK--IFHYG--SISLItepcksahISAAKAAKEAGVILSYDpnlrLPLWPSADN 239
Cdd:PLN02379 156 ----RPclSSAVKLQADELTKEDFKGSKwlVLRYGfyNLEVI--------EAAIRLAKQEGLSVSLD----LASFEMVRN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 240 AREEILSIWETADI--IKISEEEIVFLTKGEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLK-VDVVD 316
Cdd:PLN02379 220 FRSPLLQLLESGKIdlCFANEDEARELLRGEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAVD 299
|
250 260
....*....|....*....|..
gi 22330456 317 TTGAGDAFVAGILSQLANDLSL 338
Cdd:PLN02379 300 ATGAGDLFASGFLYGLIKGLSL 321
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
85-370 |
1.76e-11 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 64.66 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 85 LADAPAFKKAPGGAPANVAvgiaRLG--------GSSAFIGKVGEDEFGYMLANILKDNNVNndgMRFDP--GARTALAF 154
Cdd:PTZ00247 51 LESIPNVSYVPGGSALNTA----RVAqwmlqapkGFVCYVGCVGDDRFAEILKEAAEKDGVE---MLFEYttKAPTGTCA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 155 VTLTNEgEREFMfyRNPSADMLLE----ESELDFDLIKKAKIFHYGSISLITEPCKSAHIsaAKAAKEAGVILSYdpNLR 230
Cdd:PTZ00247 124 VLVCGK-ERSLV--ANLGAANHLSaehmQSHAVQEAIKTAQLYYLEGFFLTVSPNNVLQV--AKHARESGKLFCL--NLS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 231 LPLwpsADNAR-EEILSIWETADIIKISEEEIVFLTKGEDPYDDNVVR---------KLFHPKLKLLLVTEGPEGCRYYT 300
Cdd:PTZ00247 197 APF---ISQFFfERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDLKEiaariamlpKYSGTRPRLVVFTQGPEPTLIAT 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330456 301 KDFSGRVHGLKVD---VVDTTGAGDAFVAGILSQLANDlsllQDEERLREAlmfANACGALTVKVRGA-IPALP 370
Cdd:PTZ00247 274 KDGVTSVPVPPLDqekIVDTNGAGDAFVGGFLAQYANG----KDIDRCVEA---GHYSAQVIIQHNGCtYPEKP 340
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
85-332 |
4.83e-10 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 60.11 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 85 LADAPAFKKAPGGAPAN---VAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRfDPGARTALAFVtLTNEG 161
Cdd:PLN02548 41 LASKYNVEYIAGGATQNsirVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVNVHYYE-DESTPTGTCAV-LVVGG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 162 EREFMFYRNpSADML----LEESElDFDLIKKAKIFHYGSISLITEPcKSAHISAAKAAKEAGVilsYDPNLRLP----- 232
Cdd:PLN02548 119 ERSLVANLS-AANCYkvehLKKPE-NWALVEKAKFYYIAGFFLTVSP-ESIMLVAEHAAANNKT---FMMNLSAPficef 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 233 -------LWPSAD----NAREEI----LSIWETADI----IKISE--------EEIVFLTKGEDPyddNVVRKlfHPKLK 285
Cdd:PLN02548 193 fkdqlmeALPYVDflfgNETEARtfakVQGWETEDVeeiaLKISAlpkasgthKRTVVITQGADP---TVVAE--DGKVK 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 22330456 286 LLLVTEGPegcryytkdfsgrvhglKVDVVDTTGAGDAFVAGILSQL 332
Cdd:PLN02548 268 EFPVIPLP-----------------KEKLVDTNGAGDAFVGGFLSQL 297
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
87-329 |
1.25e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 59.44 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 87 DAPAFKKAPGGAPANVAVGIARLGGSS--------AFIGKVGEDEFGYMLANILKDNNVNndgmrF----DPGARTALAF 154
Cdd:PLN02813 117 DGCSYKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANVH-----FlsqpVKDGTTGTVI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 155 VTLTNEGEREFMFYRNPSadmlleeSELDFD-----LIKKAKIF---HY-----GSISLITEPCKSAHISAAKAAKEAGv 221
Cdd:PLN02813 192 VLTTPDAQRTMLSYQGTS-------STVNYDsclasAISKSRVLvveGYlwelpQTIEAIAQACEEAHRAGALVAVTAS- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 222 ilsyDPNLrlplwpsADNAREEILSIWE-TADIIKISEEEIVFLTK-GEDPYDDNVVRKLFHpKLKLLLVTEGPEGCRYY 299
Cdd:PLN02813 264 ----DVSC-------IERHRDDFWDVMGnYADILFANSDEARALCGlGSEESPESATRYLSH-FCPLVSVTDGARGSYIG 331
|
250 260 270
....*....|....*....|....*....|...
gi 22330456 300 TKdfsGRVHGL---KVDVVDTTGAGDAFVAGIL 329
Cdd:PLN02813 332 VK---GEAVYIppsPCVPVDTCGAGDAYAAGIL 361
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
66-332 |
1.35e-09 |
|
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: 58.18 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 66 VVCFGEMLIDFVPTTSGLsladapafKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEfgymlANILKDNNVNNDGMRFD 145
Cdd:cd01937 2 IVIIGHVTIDEIVTNGSG--------VVKPGGPATYASLTLSRLGLTVKLVTKVGRDY-----PDKWSDLFDNGIEVISL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 146 PGARTALAFVTLTNEGEREFMFyrNPSADMLLEESELDFDlikKAKIFHYGSISLitepcksaHISAAKAAKEAGVILsy 225
Cdd:cd01937 69 LSTETTTFELNYTNEGRTRTLL--AKCAAIPDTESPLSTI---TAEIVILGPVPE--------EISPSLFRKFAFISL-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 226 DPNLRLPLWPSADNAREEILSIwetADIIKISEEEI-VFLTKGEdpyddnVVRKLFHPKLKLLLVTEGPEGCRYYTKDFS 304
Cdd:cd01937 134 DAQGFLRRANQEKLIKCVILKL---HDVLKLSRVEAeVISTPTE------LARLIKETGVKEIIVTDGEEGGYIFDGNGK 204
|
250 260
....*....|....*....|....*...
gi 22330456 305 GRVHGLKVDVVDTTGAGDAFVAGILSQL 332
Cdd:cd01937 205 YTIPASKKDVVDPTGAGDVFLAAFLYSR 232
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
61-360 |
9.15e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 56.15 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 61 QESPYVVCFGEMLIDFVP-TTSGLSLADA-PA-FKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNV 137
Cdd:PRK09850 2 REKDYVVIIGSANIDVAGySHESLNYADSnPGkIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 138 NNDGMRFDPGARTALAFVTLTNEGE-----REFMFYRNPSADMLLEESeldfDLIKKAKIfhygsislITEPCKSAHISA 212
Cdd:PRK09850 82 YVDKCLIVPGENTSSYLSLLDNTGEmlvaiNDMNISNAITAEYLAQHR----EFIQRAKV--------IVADCNISEEAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 213 AKAAKEAG-VILSYDPnlrLPLWPSAdNAREEILSIW---------ETADIIKISEEEivfltkgedpyDDNVVRKLFHP 282
Cdd:PRK09850 150 AWILDNAAnVPVFVDP---VSAWKCV-KVRDRLNQIHtlkpnrleaETLSGIALSGRE-----------DVAKVAAWFHQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 283 K-LKLLLVTEGPEGCrYYTKDF--SGRVHGLKVDVVDTTGAGDAFVAGILSQLANDLSLLqdeerlrEALMFANACGALT 359
Cdd:PRK09850 215 HgLNRLVLSMGGDGV-YYSDISgeSGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFA-------ESVRFAQGCSSMA 286
|
.
gi 22330456 360 V 360
Cdd:PRK09850 287 L 287
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
95-140 |
1.55e-07 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 52.91 E-value: 1.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 22330456 95 PGGApANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNND 140
Cdd:PRK11316 50 PGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCD 94
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
253-360 |
2.14e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 52.12 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 253 IIKISEEEIVFLtkgedpyDDNVVRKLfhpklKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGDAFVAGILSQL 332
Cdd:PLN02630 184 FLKASSEEALFI-------DVEEVRQK-----CCVIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGL 251
|
90 100
....*....|....*....|....*...
gi 22330456 333 ANDLSLLQdeerlreALMFANACGALTV 360
Cdd:PLN02630 252 VQGLAVPD-------AALLGNYFGSLAV 272
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
238-361 |
5.36e-06 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 47.46 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330456 238 DNAREEILSIWETADIIKISEEEIVFLTkgEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKD--FSGRVHGLKvDVV 315
Cdd:cd01946 151 SIKPEKLKKVLAKVDVVIINDGEARQLT--GAANLVKAARLILAMGPKALIIKRGEYGALLFTDDgyFAAPAYPLE-SVF 227
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 22330456 316 DTTGAGDAFVAGILSQLANDLSLlqDEERLREALMFANACGALTVK 361
Cdd:cd01946 228 DPTGAGDTFAGGFIGYLASQKDT--SEANMRRAIIYGSAMASFCVE 271
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
292-354 |
2.29e-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: 42.78 E-value: 2.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330456 292 GPEGCRYYTKDFSGrvhglkVDVVDTTGAGDAFVAGILsqlandLSLLQDEERLREALMFANA 354
Cdd:cd01939 228 GPDGEYVHSPAHKP------IRVVDTLGAGDTFNAAVI------YALNKGPDDLSEALDFGNR 278
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
311-360 |
1.84e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 39.68 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 22330456 311 KVDVVDTTGAGDAFVAGILSQLANDLSllqDEERLRealmFANACGALTV 360
Cdd:PRK09513 244 ACDVVSTVGAGDSMVGGLIYGLLMRES---SEHTLR----LATAVSALAV 286
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
311-358 |
6.56e-03 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 38.17 E-value: 6.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 22330456 311 KVDVVDTTGAGDAFVAGILSQLANDLSllqDEERLREalmfANACGAL 358
Cdd:PRK13508 242 KIEVVNPVGSGDSTVAGIASGLLHQED---DADLLKK----ANVLGML 282
|
|
| |
