|
Name |
Accession |
Description |
Interval |
E-value |
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-256 |
9.05e-102 |
|
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: 298.40 E-value: 9.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNVTNanlkDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYR 82
Cdd:cd01167 1 KVVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 83 TNEANTALAFVSLTEAGERDFSFYRKPSADMLFEPSfVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVV 162
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTE-LNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 163 FDPNVRLPLWDNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTGNVTVVIYTKGADGAAVYLKNGINH 242
Cdd:cd01167 156 FDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGE 235
|
250
....*....|....
gi 582617436 243 YHsGYKVKPVDTTG 256
Cdd:cd01167 236 VP-GIPVEVVDTTG 248
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-256 |
2.12e-72 |
|
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: 223.61 E-value: 2.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNV----TNANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVS 78
Cdd:COG0524 1 DVLVIGEALVDLVARVdrlpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 79 KVYRTNEANTALAFVSLTEAGERDFSFYRkpSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNAN 158
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 159 GTVVFDPNVRLPLWDNAedlRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTGNVTVVIYTKGADGAAVYLKN 238
Cdd:COG0524 159 VPVSLDPNYRPALWEPA---RELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250
....*....|....*...
gi 582617436 239 GInHYHSGYKVKPVDTTG 256
Cdd:COG0524 236 EV-VHVPAFPVEVVDTTG 252
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
6-256 |
7.96e-68 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 212.94 E-value: 7.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 6 SIGEALIDFIPNVTNANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNE 85
Cdd:PLN02323 15 CFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 86 ANTALAFVSLTEAGERDFSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVVFDP 165
Cdd:PLN02323 95 ARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSYDP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 166 NVRLPLWDNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDEN-EAIQSLFTGNVTVVIYTKGADGAAVYLKNginhYH 244
Cdd:PLN02323 175 NLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDdDTVVKLWHPNLKLLLVTEGEEGCRYYTKD----FK 250
|
250
....*....|....*
gi 582617436 245 ---SGYKVKPVDTTG 256
Cdd:PLN02323 251 grvEGFKVKAVDTTG 265
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-256 |
2.76e-64 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 202.96 E-value: 2.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNVTN--ANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKV 80
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGlpGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 81 YRTNEANTALAFVSLTEAGERDFSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSvdLVDSPMRDAHYQLITKTLNANGT 160
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISG--SLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 161 vvFDPNVRLPLWdnaeDLRQTIHTFLPLAHIVKVSDEELEFITG--IHDENEAIQSLFTGN---VTVVIYTKGADGAAVY 235
Cdd:pfam00294 159 --FDPNLLDPLG----AAREALLELLPLADLLKPNEEELEALTGakLDDIEEALAALHKLLakgIKTVIVTLGADGALVV 232
|
250 260
....*....|....*....|.
gi 582617436 236 LKNGINHYHSGYKVKPVDTTG 256
Cdd:pfam00294 233 EGDGEVHVPAVPKVKVVDTTG 253
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
7-257 |
4.40e-44 |
|
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: 151.21 E-value: 4.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 7 IGEALIDFIPNVTNANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEA 86
Cdd:TIGR04382 7 IGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 87 NTALAFVSLTEAGERDFSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVVFDPN 166
Cdd:TIGR04382 87 RTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVLDID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 167 VRLPLWDNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTGNVTVVIYTKGADGAAVYLKNGINHYHSG 246
Cdd:TIGR04382 167 YRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGEGVEVPG 246
|
250
....*....|.
gi 582617436 247 YKVKPVDTTGG 257
Cdd:TIGR04382 247 FPVEVLNVLGA 257
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-256 |
9.05e-102 |
|
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: 298.40 E-value: 9.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNVTNanlkDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYR 82
Cdd:cd01167 1 KVVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 83 TNEANTALAFVSLTEAGERDFSFYRKPSADMLFEPSfVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVV 162
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTE-LNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 163 FDPNVRLPLWDNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTGNVTVVIYTKGADGAAVYLKNGINH 242
Cdd:cd01167 156 FDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGE 235
|
250
....*....|....
gi 582617436 243 YHsGYKVKPVDTTG 256
Cdd:cd01167 236 VP-GIPVEVVDTTG 248
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-256 |
2.12e-72 |
|
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: 223.61 E-value: 2.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNV----TNANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVS 78
Cdd:COG0524 1 DVLVIGEALVDLVARVdrlpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 79 KVYRTNEANTALAFVSLTEAGERDFSFYRkpSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNAN 158
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 159 GTVVFDPNVRLPLWDNAedlRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTGNVTVVIYTKGADGAAVYLKN 238
Cdd:COG0524 159 VPVSLDPNYRPALWEPA---RELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250
....*....|....*...
gi 582617436 239 GInHYHSGYKVKPVDTTG 256
Cdd:COG0524 236 EV-VHVPAFPVEVVDTTG 252
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
6-256 |
7.96e-68 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 212.94 E-value: 7.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 6 SIGEALIDFIPNVTNANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNE 85
Cdd:PLN02323 15 CFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 86 ANTALAFVSLTEAGERDFSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVVFDP 165
Cdd:PLN02323 95 ARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSYDP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 166 NVRLPLWDNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDEN-EAIQSLFTGNVTVVIYTKGADGAAVYLKNginhYH 244
Cdd:PLN02323 175 NLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDdDTVVKLWHPNLKLLLVTEGEEGCRYYTKD----FK 250
|
250
....*....|....*
gi 582617436 245 ---SGYKVKPVDTTG 256
Cdd:PLN02323 251 grvEGFKVKAVDTTG 265
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-256 |
2.76e-64 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 202.96 E-value: 2.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNVTN--ANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKV 80
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGlpGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 81 YRTNEANTALAFVSLTEAGERDFSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSvdLVDSPMRDAHYQLITKTLNANGT 160
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISG--SLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 161 vvFDPNVRLPLWdnaeDLRQTIHTFLPLAHIVKVSDEELEFITG--IHDENEAIQSLFTGN---VTVVIYTKGADGAAVY 235
Cdd:pfam00294 159 --FDPNLLDPLG----AAREALLELLPLADLLKPNEEELEALTGakLDDIEEALAALHKLLakgIKTVIVTLGADGALVV 232
|
250 260
....*....|....*....|.
gi 582617436 236 LKNGINHYHSGYKVKPVDTTG 256
Cdd:pfam00294 233 EGDGEVHVPAVPKVKVVDTTG 253
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-257 |
6.55e-59 |
|
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: 188.94 E-value: 6.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNVTNAnLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYR 82
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGR-LEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 83 TNEANTALAFVSLTEAGERDFSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSVDL-VDSPMRDAHYQLITKTLNANGTV 161
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLaLSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 162 VFDPNVRLPLWdNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAI---QSLFTGNVTVVIyTKGADGAAVYLKN 238
Cdd:cd01166 160 SFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAeraLALALGVKAVVV-KLGAEGALVYTGG 237
|
250
....*....|....*....
gi 582617436 239 GInHYHSGYKVKPVDTTGG 257
Cdd:cd01166 238 GR-VFVPAYPVEVVDTTGA 255
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-256 |
2.47e-55 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 180.13 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 1 MRRLFSIGEALIDFIPNVTNANLKdvqtftkQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKV 80
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPEGENRYLK-------CPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 81 YRTNEANTALAFVSLTEAGERDFSFYRKPSADMLFEPSfvnDI-DVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANG 159
Cdd:PRK09434 75 RLDPAHRTSTVVVDLDDQGERSFTFMVRPSADLFLQPQ---DLpPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 160 TVVFDPNVRLPLWDNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTG-NVTVVIYTKGADGAAVYLKN 238
Cdd:PRK09434 152 FVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADRyPIALLLVTLGAEGVLVHTRG 231
|
250
....*....|....*...
gi 582617436 239 GINHYhSGYKVKPVDTTG 256
Cdd:PRK09434 232 QVQHF-PAPSVDPVDTTG 248
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
7-257 |
4.40e-44 |
|
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: 151.21 E-value: 4.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 7 IGEALIDFIPNVTNANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEA 86
Cdd:TIGR04382 7 IGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 87 NTALAFVSLTEAGERDFSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVVFDPN 166
Cdd:TIGR04382 87 RTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVLDID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 167 VRLPLWDNAEDLRQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTGNVTVVIYTKGADGAAVYLKNGINHYHSG 246
Cdd:TIGR04382 167 YRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGEGVEVPG 246
|
250
....*....|.
gi 582617436 247 YKVKPVDTTGG 257
Cdd:TIGR04382 247 FPVEVLNVLGA 257
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
3-256 |
4.11e-26 |
|
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: 103.16 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNVTNANLKDVQTFTKQI----GGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVS 78
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLrrefGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 79 KVYRTNEANTALAFVSLTEAGERDFSFYrkPSADMLFEPSFVNDIDVNeNDVVHFCSVDLVdspMRDAhyqlitKTLNAN 158
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYFY--PGAMDELEPNDEADPDGL-ADIVHLSSGPGL---IELA------RELAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 159 G-TVVFDPNVRLPLWDNAEdlrqtIHTFLPLAHIVKVSDEELEF---ITGIHDENEAIQslftgnVTVVIYTKGADGAAV 234
Cdd:cd01942 149 GiTVSFDPGQELPRLSGEE-----LEEILERADILFVNDYEAELlkeRTGLSEAELASG------VRVVVVTLGPKGAIV 217
|
250 260
....*....|....*....|..
gi 582617436 235 YLKNGINHYHSGYKVKPVDTTG 256
Cdd:cd01942 218 FEDGEEVEVPAVPAVKVVDTTG 239
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
34-256 |
5.15e-22 |
|
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: 92.23 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 34 GGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEANTALAFVSLTEAGERDFSFYrkPSADM 113
Cdd:cd01174 36 GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVV--PGANG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 114 LFEPSfvnDIDVNENDvvhFCSVDLV----DSPMrDAHYQLITKTLNANGTVVFDPnvrLPlwdnaedLRQTIHTFLPLA 189
Cdd:cd01174 114 ELTPA---DVDAALEL---IAAADVLllqlEIPL-ETVLAALRAARRAGVTVILNP---AP-------ARPLPAELLALV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582617436 190 HIVKVSDEELEFITGIHDENE-----AIQSLFTGNVTVVIYTKGADGAAVYLKNGINHYhSGYKVKPVDTTG 256
Cdd:cd01174 177 DILVPNETEAALLTGIEVTDEedaekAARLLLAKGVKNVIVTLGAKGALLASGGEVEHV-PAFKVKAVDTTG 247
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
29-202 |
1.57e-16 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 78.80 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 29 FTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEANTALAF--VSLTEAGERDFSFY 106
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRmkIKFRDGGKMVAETV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 107 RKPSADMLFEPSFvnDIDV-NENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVVFDPNVRLPLWDNAEDLRQTIHTF 185
Cdd:PLN02543 247 KEAAEDSLLASEL--NLAVlKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKA 324
|
170
....*....|....*..
gi 582617436 186 LPLAHIVKVSDEELEFI 202
Cdd:PLN02543 325 WNEADIIEVSRQELEFL 341
|
|
| PLN02967 |
PLN02967 |
kinase |
27-239 |
2.75e-16 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 78.16 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 27 QTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEANTALAFVSLTEAGERDFSFY 106
Cdd:PLN02967 236 EKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 107 rKPSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNANGTVVFDPNVRLPLWDNAEDLRQTIHTFL 186
Cdd:PLN02967 316 -KPCAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAW 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582617436 187 PLAHIVKVSDEELEFITGI-----------------HDENEAIQSLFTGNVTVVIYTKGADGAAVYLK--NG 239
Cdd:PLN02967 395 NLADIIEVTKQELEFLCGIepteefdtkdndkskfvHYSPEVVAPLWHENLKVLFVTNGTSKIHYYTKehNG 466
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
29-260 |
3.10e-16 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 77.08 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 29 FTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEANTALAFVsLTEAGERDFSFYRK 108
Cdd:PTZ00292 47 FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMI-FVDTKTGNNEIVII 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 109 PSADMLFEPSFVNDidvNENDVVHFCSVDLV--DSPMrDAHYQLITKTLNANGTVVFDPNvrlPLwdNAEDLRQTIHTFL 186
Cdd:PTZ00292 126 PGANNALTPQMVDA---QTDNIQNICKYLICqnEIPL-ETTLDALKEAKERGCYTVFNPA---PA--PKLAEVEIIKPFL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 187 PLAHIVKVSDEELEFITGIH--DENEAIQS---LFTGNVTVVIYTKGADGAAvYLKNGINHYH-SGYKVKPVDTTGGRGC 260
Cdd:PTZ00292 197 KYVSLFCVNEVEAALITGMEvtDTESAFKAskeLQQLGVENVIITLGANGCL-IVEKENEPVHvPGKRVKAVDTTGAGDC 275
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-260 |
1.38e-15 |
|
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: 74.77 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNV----TNANLKDVQTFTKQIGGApCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVS 78
Cdd:cd01944 1 KVLVIGAAVVDIVLDVdklpASGGDIEAKSKSYVIGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 79 KVYRTNEaNTALAFVSLTEAGERdfSFYRKPSADMLFEPSFVNDIDVNENDVVHFCSVDLVDSPMRDAHYQLITKTLNAN 158
Cdd:cd01944 80 LPPRGGD-DGGCLVALVEPDGER--SFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 159 GTVVFDPNVRLPLWDNAEdlrqtIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTG--NVTVVIYTKGADGAAVYL 236
Cdd:cd01944 157 TTLVFDPGPRISDIPDTI-----LQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYakTAAPVVVRLGSNGAWIRL 231
|
250 260
....*....|....*....|....
gi 582617436 237 KNGINHYHSGYKVKPVDTTGGRGC 260
Cdd:cd01944 232 PDGNTHIIPGFKVKAVDTIGAGDT 255
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
34-256 |
2.42e-15 |
|
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: 73.54 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 34 GGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVyRTNEANTALAFVsLTEAGERDFSFYRKpsADM 113
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADV-ELVDGDRIFGLSNK--GGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 114 LFEPSFVNDID-VNENDVVHFCSVDLVDspmrdaHYQLITKTLNANGTVV-FDPNVRlplWDnaEDLRQTIHTFLPLAhi 191
Cdd:cd01940 98 AREHPFEADLEyLSQFDLVHTGIYSHEG------HLEKALQALVGAGALIsFDFSDR---WD--DDYLQLVCPYVDFA-- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 192 vkvsdeeleFITGIHDENEAIQSL----FTGNVTVVIYTKGADGAAVYlkNGINHYHSG-YKVKPVDTTG 256
Cdd:cd01940 165 ---------FFSASDLSDEEVKAKlkeaVSRGAKLVIVTRGEDGAIAY--DGAVFYSVApRPVEVVDTLG 223
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
31-256 |
6.01e-13 |
|
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: 66.93 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 31 KQIGGAPC-NVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEANTALAFVSLTEAGERDFSFYRKP 109
Cdd:cd01945 32 AVIGGGNAaNAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISITAID 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 110 SADMlfEPSFVNDIdvnendvVHFCSVDLVDSPMRDAHYQLITKTLNANGTVVFDpnvrlplWDnAEDLRQTiHTFLPLA 189
Cdd:cd01945 112 TQAA--PDSLPDAI-------LGGADAVLVDGRQPEAALHLAQEARARGIPIPLD-------LD-GGGLRVL-EELLPLA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 582617436 190 HIVKVSDEELEFITGIHDEnEAIQSLFTGNVTVVIYTKGADGAAVYLKNGINHYHSGYKVKPVDTTG 256
Cdd:cd01945 174 DHAICSENFLRPNTGSADD-EALELLASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVEVVDTTG 239
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
3-256 |
6.89e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 63.99 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 3 RLFSIGEALIDFIPNVTNAnlkdvqtFTkqiGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVyR 82
Cdd:PRK09813 2 KLATIGDNCVDIYPQLGKA-------FS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV-H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 83 TNEANTALAFVSLtEAGERDFSFYrkpsadmlfEPSFVNDIDVNENDVVHFCSVDLVDSPMRdAHYQLITKTLNANGTVV 162
Cdd:PRK09813 71 TKHGVTAQTQVEL-HDNDRVFGDY---------TEGVMADFALSEEDYAWLAQYDIVHAAIW-GHAEDAFPQLHAAGKLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 163 -FDPNVRL--PLWDnaedlrqtihTFLP-LAHIVKVSDEELEFItgihdeNEAIQSLFTGNVTVVIYTKGADGAAVYlkN 238
Cdd:PRK09813 140 aFDFSDKWdsPLWQ----------TLVPhLDYAFASAPQEDEFL------RLKMKAIVARGAGVVIVTLGENGSIAW--D 201
|
250
....*....|....*....
gi 582617436 239 GINHYHSG-YKVKPVDTTG 256
Cdd:PRK09813 202 GAQFWRQApEPVTVVDTMG 220
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
35-256 |
1.91e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 63.70 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 35 GAPCNVACTVQKLGQQAYMITQLGNDAFGDSII-----ETISSIGV---DVSKVYRTNEANTALAFVSLTEAGERDFSfy 106
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLdvlaeEGISVVGLiegTDAGDSSSASYETLLCWVLVDPLQRHGFC-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 107 rkPSADMLFEPSF--VNDIDVNENDVVHFCSVDLVDSPMRDAHY-QLITKTLN---ANGTVV-FDPNVR-LPLWDNAEDL 178
Cdd:PLN02341 198 --SRADFGPEPAFswISKLSAEAKMAIRQSKALFCNGYVFDELSpSAIASAVDyaiDVGTAVfFDPGPRgKSLLVGTPDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 179 RQTIHTFLPLAHIVKVSDEELEFITGIHDENEAIQSLFTGNVTV--VIYTKGADGAAVYLKNGINhYHSGYKVKPVDTTG 256
Cdd:PLN02341 276 RRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVS-CAPAFKVNVVDTVG 354
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
24-256 |
6.40e-09 |
|
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: 55.12 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 24 KDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEANTALAFVslTEAGERDF 103
Cdd:cd01947 26 SHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFI--DPNGERTI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 104 SFYRKPSADMLFEPSFVndidvnENDVVhFCSVDLVDSPMRdahyqlitKTLNANGTVVFDPNVRLPLWDNAEDLRQtih 183
Cdd:cd01947 104 TVPGERLEDDLKWPILD------EGDGV-FITAAAVDKEAI--------RKCRETKLVILQVTPRVRVDELNQALIP--- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 582617436 184 tflplAHIVKVSDEELefitGIHDENEAIQSLFtgnVTVVIYTKGADGAAVYLKNGINHYhSGYKVKPVDTTG 256
Cdd:cd01947 166 -----LDILIGSRLDP----GELVVAEKIAGPF---PRYLIVTEGELGAILYPGGRYNHV-PAKKAKVPDSTG 225
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
131-256 |
1.83e-07 |
|
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: 50.17 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 131 VHFCSVDLV----DSPMRDAHYQLITKTLNANGTVVFDPNVRLPLWDNAEDLRqtihtFLPLAHIVKVSDEELEFITGIH 206
Cdd:cd00287 53 VTLVGADAVvisgLSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEK-----LLPGVDILTPNEEEAEALTGRR 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 582617436 207 DENE------AIQSLFTGNVTVVIyTKGADGAAVYLKNGinHYHSG--YKVKPVDTTG 256
Cdd:cd00287 128 DLEVkeaaeaAALLLSKGPKVVIV-TLGEKGAIVATRGG--TEVHVpaFPVKVVDTTG 182
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
12-256 |
1.70e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 47.78 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 12 IDFIPNVTNANLKDVQTFTKQIGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKvyrtnEANTALA 91
Cdd:cd01937 2 IVIIGHVTIDEIVTNGSGVVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVISLL-----STETTTF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 92 FVSLTEAGERDFSFyRKPSADmlfePSFVNDIDVNENDVVHFCSVDLVDSPMrdahyqLITKTlnanGTVVFDPN--VRl 169
Cdd:cd01937 77 ELNYTNEGRTRTLL-AKCAAI----PDTESPLSTITAEIVILGPVPEEISPS------LFRKF----AFISLDAQgfLR- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 170 plwdNAEDLRQTIHTFLPLAHIVKVSDEELEfitGIHDENEAIQSLFTGNVTVVIYTKGADGAAVYLKNGINHYHSgYKV 249
Cdd:cd01937 141 ----RANQEKLIKCVILKLHDVLKLSRVEAE---VISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPA-SKK 212
|
....*..
gi 582617436 250 KPVDTTG 256
Cdd:cd01937 213 DVVDPTG 219
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
34-215 |
1.34e-05 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 45.69 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 34 GGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEANTAlAFVSLTEAGERDFSFYRKPSADM 113
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTS-TYLAIANRQDETVLAINDTHILQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 114 LFEPSFVNdidvNENDVVHFCSVDLVDSPMRDAHYQLITKTlnANGTVVFDPNVrlplwdnAEDLRQTIHTFLPLAHIVK 193
Cdd:PRK09954 172 QLTPQLLN----GSRDLIRHAGVVLADCNLTAEALEWVFTL--ADEIPVFVDTV-------SEFKAGKIKHWLAHIHTLK 238
|
170 180
....*....|....*....|....
gi 582617436 194 VSDEELEFITG--IHDENEAIQSL 215
Cdd:PRK09954 239 PTQPELEILWGqaITSDADRNAAV 262
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
33-256 |
3.62e-05 |
|
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: 44.23 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 33 IGGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSKVYRTNEaNTALAFVSLTEAGERDFSFyrkpsAD 112
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGR-STASYTAILDKDGDLVVAL-----AD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 113 MlfepsfvndiDVNENdvvhfcsvdlvdspMRDAHYQLITKTLNANGTVVFDPNVRLP----LWDNAEDLRQTI------ 182
Cdd:cd01941 108 M----------DIYEL--------------LTPDFLRKIREALKEAKPIVVDANLPEEaleyLLALAAKHGVPVafepts 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 183 -----HTFLPLAHI--VKVSDEELEFITGI-----HDENEAIQSLFTGNVTVVIYTKGADGAAVYLKNGiNHYHSGY--- 247
Cdd:cd01941 164 apklkKLFYLLHAIdlLTPNRAELEALAGAliennEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREG-GVETKLFpap 242
|
250
....*....|
gi 582617436 248 -KVKPVDTTG 256
Cdd:cd01941 243 qPETVVNVTG 252
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
4-256 |
8.03e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 39.97 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 4 LFSIGEALIDfIPNVTNANLKDVQTFTKQI----GGAPCNVACTVQKLGQQAYMITQLGNDAFGDSIIETISSIGVDVSK 79
Cdd:PRK09850 7 VVIIGSANID-VAGYSHESLNYADSNPGKIkftpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 80 VYRTNEANTALAFVSLTEAGE-----RDFSFYRKPSADMLFEpsfvndidvnENDVVHFCSVDLVDSPMRDAHYQLITKt 154
Cdd:PRK09850 86 CLIVPGENTSSYLSLLDNTGEmlvaiNDMNISNAITAEYLAQ----------HREFIQRAKVIVADCNISEEALAWILD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582617436 155 lNANGTVVF-DPnvrLPLWDNAEdlrqtIHTFLPLAHIVKVSDEELEFITGI----HDENEAIQSLF-TGNVTVVIYTKG 228
Cdd:PRK09850 155 -NAANVPVFvDP---VSAWKCVK-----VRDRLNQIHTLKPNRLEAETLSGIalsgREDVAKVAAWFhQHGLNRLVLSMG 225
|
250 260
....*....|....*....|....*...
gi 582617436 229 ADGAAVYLKNGINHYHSGYKVKPVDTTG 256
Cdd:PRK09850 226 GDGVYYSDISGESGWSAPIKTNVINVTG 253
|
|
| |
