|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-296 |
0e+00 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 564.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 1 MKKIWVLGDAVVDLLPDGEGRLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHR 80
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 81 TSTVVVDLDDHGERSFTFMVRPSADLFLEPADLPSFSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYVSFDPNIRP 160
Cdd:PRK09434 82 TSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 161 DLWADENELRRCLELALQHADVVKLSVEELTFLTHDAQVKTGLESLMRRCPARLVLVTLGKEGVIAWHDGAVKHYPATSV 240
Cdd:PRK09434 162 DLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSV 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1736704024 241 ECVDTTGAGDAFVAGLLYGLAAG------QELVPVIGLAQRCGALATTAKGAMTALPYHHEL 296
Cdd:PRK09434 242 DPVDTTGAGDAFVAGLLAGLSQAglwtdeAELAEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-287 |
1.03e-107 |
|
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: 314.57 E-value: 1.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDLLPDGEGRLLQ---CPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAH 79
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETftkAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 80 RTSTVVVDLDDHGERSFTFMVRPSADLFLEPADLPS-FSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYVSFDPNI 158
Cdd:cd01167 81 PTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDlLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLISFDPNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 159 RPDLWADENELRRCLELALQHADVVKLSVEELTFLTHDAQVKTGLESLmRRCPARLVLVTLGKEGVIAWHDGAVKHYPAT 238
Cdd:cd01167 161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALL-LLFGLKLVLVTRGADGALLYTKGGVGEVPGI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1736704024 239 SVECVDTTGAGDAFVAGLLYGLAAGQ-------ELVPVIGLAQRCGALATTAKGAM 287
Cdd:cd01167 240 PVEVVDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-296 |
3.42e-90 |
|
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: 270.22 E-value: 3.42e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDLLPDGE-----------GRLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQ 71
Cdd:COG0524 1 DVLVIGEALVDLVARVDrlpkggetvlaGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 72 QMRLDPAHRTSTVVVDLDDHGERSFTFMvrPSADLFLEPADLPS--FSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAG 149
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFY--RGANAELTPEDLDEalLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 150 GYVSFDPNIRPDLWadeNELRRCLELALQHADVVKLSVEELTFLTHDAQVKTGLESLMRRcPARLVLVTLGKEGVIAWHD 229
Cdd:COG0524 159 VPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLAR-GVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736704024 230 GAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGAMTALPYHHEL 296
Cdd:COG0524 235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
7-291 |
2.06e-76 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 236.06 E-value: 2.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 7 LGDAVVDLLPDGEG-------RLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAH 79
Cdd:PLN02323 16 FGEMLIDFVPTVSGvslaeapAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 80 RTSTVVVDLDDHGERSFTFMVRPSADLFLEPA--DLPSFSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYVSFDPN 157
Cdd:PLN02323 96 RTALAFVTLRSDGEREFMFYRNPSADMLLRESelDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSYDPN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 158 IRPDLWADENELRRCLELALQHADVVKLSVEELTFLTHDAQVKtgLESLMRRCPAR--LVLVTLGKEGVIAWHDGAVKHY 235
Cdd:PLN02323 176 LRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPD--DDTVVKLWHPNlkLLLVTEGEEGCRYYTKDFKGRV 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736704024 236 PATSVECVDTTGAGDAFVAGLLYGLAAGQELV-------PVIGLAQRCGALATTAKGAMTALP 291
Cdd:PLN02323 254 EGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLedeerlrEALRFANACGAITTTERGAIPALP 316
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-287 |
1.19e-74 |
|
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: 230.54 E-value: 1.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDLLPDGEGRLLQC------PGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLD 76
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQAdsfrkfFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 77 PAHRTSTVVVDLDDHGERSFTFMVRPSADLFLEPADLP--SFSAGEWLHVCSIALSAEPS-RSAAFQAMTSIREAGGYVS 153
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDeaALAGADHLHLSGITLALSESaREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 154 FDPNIRPDLWADEnELRRCLELALQHADVVKLSVEELTFLTHDAQVKTGLESLMRRCP-ARLVLVTLGKEGVIAWHDGAV 232
Cdd:cd01166 161 FDLNYRPKLWSAE-EAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALgVKAVVVKLGAEGALVYTGGGR 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1736704024 233 KHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGAM 287
Cdd:cd01166 240 VFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-288 |
3.40e-68 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 213.74 E-value: 3.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDLLPDGEG---------RLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQM 73
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGlpgelvrvsTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 74 RLDPAHRTSTVVVDLDDHGERSFTFMVRPSADLFLEP--ADLPSFSAGEWLHVCSIALSaePSRSAAFQAMTSIREAGGY 151
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEEleENEDLLENADLLYISGSLPL--GLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 152 vsFDPNIRPDLWADenelRRCLELALQHADVVKLSVEELTFLTHDAQVktGLESLMRRCP------ARLVLVTLGKEGVI 225
Cdd:pfam00294 159 --FDPNLLDPLGAA----REALLELLPLADLLKPNEEELEALTGAKLD--DIEEALAALHkllakgIKTVIVTLGADGAL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1736704024 226 AWH-DGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGAMT 288
Cdd:pfam00294 231 VVEgDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
27-296 |
8.35e-58 |
|
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: 187.81 E-value: 8.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 27 GGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHGERSFTFMVRPSADL 106
Cdd:TIGR04382 34 GGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPGRRTSLVFLEIKPPDEFPLLFYRENAADL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 107 FLEPADLPS--FSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYVSFDPNIRPDLWADENELRRCLELALQHADVVK 184
Cdd:TIGR04382 114 ALTPDDVDEdyIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVLDIDYRPYLWKSPEEAGIYLRLVLPLVDVII 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 185 LSVEELTFLTHDAQVKTGLESLMRRCPArLVLVTLGKEGVIAWH-DGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAG 263
Cdd:TIGR04382 194 GTREEFDIAGGEGDDEAAARALLDAGVE-ILVVKRGPEGSLVYTgDGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAG 272
|
250 260 270
....*....|....*....|....*....|...
gi 1736704024 264 QELVPVIGLAQRCGALATTAKGAMTALPYHHEL 296
Cdd:TIGR04382 273 WDLEKALRYGNACGAIVVSRHSCSPAMPTLEEL 305
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
3-292 |
8.19e-45 |
|
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: 153.47 E-value: 8.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDL------LPD-GE----GRLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQ 71
Cdd:cd01174 1 KVVVVGSINVDLvtrvdrLPKpGEtvlgSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 72 QMRLDPAHRTSTVVVDLDDHGERSFtfMVRPSADLFLEPADLPSfsAGEWLHVCSIALS-AEPSRSAAFQAMTSIREAGG 150
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRI--VVVPGANGELTPADVDA--ALELIAAADVLLLqLEIPLETVLAALRAARRAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 151 YVSFDPN-IRPDLwadeNELrrclelaLQHADVVKLSVEELTFLTHD-----AQVKTGLESLMRRcPARLVLVTLGKEGV 224
Cdd:cd01174 157 TVILNPApARPLP----AEL-------LALVDILVPNETEAALLTGIevtdeEDAEKAARLLLAK-GVKNVIVTLGAKGA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736704024 225 IAWHDGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGAMTALPY 292
Cdd:cd01174 225 LLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
26-286 |
6.47e-39 |
|
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: 137.83 E-value: 6.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHGERSFTFMvrPSAD 105
Cdd:cd01942 35 FGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFY--PGAM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 106 LFLEPAD-LPSFSAGEWLHVcsialsaePSRSAAFQAMTSIREAGGYVSFDPNirPDLWADENE-LRRCLElalqHADVV 183
Cdd:cd01942 113 DELEPNDeADPDGLADIVHL--------SSGPGLIELARELAAGGITVSFDPG--QELPRLSGEeLEEILE----RADIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 184 KLSVEELTFLTHdaqvKTGLESLMRRCPARLVLVTLGKEGVIAWHDGAVKHYPAT-SVECVDTTGAGDAFVAGLLYGLAA 262
Cdd:cd01942 179 FVNDYEAELLKE----RTGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVpAVKVVDTTGAGDAFRAGFLYGLLR 254
|
250 260
....*....|....*....|....
gi 1736704024 263 GQELVPVIGLAQRCGALATTAKGA 286
Cdd:cd01942 255 GYDLEESLRLGNLAASLKVERRGA 278
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
26-296 |
3.01e-37 |
|
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: 133.88 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHGERSFtfMVRPSAD 105
Cdd:TIGR02152 30 PGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRI--VVVAGAN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 106 LFLEPADLPSfsAGEWLHVCSIAL----SAEPSRSAAFQAMtsiREAGGYVSFDP-----NIRPDLWAD-------ENEL 169
Cdd:TIGR02152 108 AELTPEDIDA--AEALIAESDIVLlqleIPLETVLEAAKIA---KKHGVKVILNPapaikDLDDELLSLvdiitpnETEA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 170 rrclelalqhadvvklsvEELT--FLTHDAQVKTGLESLMRRCPaRLVLVTLGKEGVIaWHDGA-VKHYPATSVECVDTT 246
Cdd:TIGR02152 183 ------------------EILTgiEVTDEEDAEKAAEKLLEKGV-KNVIITLGSKGAL-LVSKDeSKLIPAFKVKAVDTT 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1736704024 247 GAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGAMTALPYHHEL 296
Cdd:TIGR02152 243 AAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
21-286 |
1.25e-31 |
|
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: 119.64 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 21 RLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHrTSTVVVDLDDHGERSFTFMV 100
Cdd:cd01168 49 PVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGP-TGTCAVLVTPDAERTMCTYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 101 RPSADLFLEPADLPSFSAGEWLHVCSIALSAEPsrSAAFQAMTSIREAGGYVSFDpnirpdlWADENELRRC---LELAL 177
Cdd:cd01168 128 GAANELSPDDLDWSLLAKAKYLYLEGYLLTVPP--EAILLAAEHAKENGVKIALN-------LSAPFIVQRFkeaLLELL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 178 QHADVV---KLSVEELTFLTHDAQVKTGLESLMRRCpaRLVLVTLGKEGVIAWHDGAVKHYPA-TSVECVDTTGAGDAFV 253
Cdd:cd01168 199 PYVDILfgnEEEAEALAEAETTDDLEAALKLLALRC--RIVVITQGAKGAVVVEGGEVYPVPAiPVEKIVDTNGAGDAFA 276
|
250 260 270
....*....|....*....|....*....|...
gi 1736704024 254 AGLLYGLAAGQELVPVIGLAQRCGALATTAKGA 286
Cdd:cd01168 277 GGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
2-286 |
3.64e-31 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 117.15 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 2 KKIWVLGDAVVDLLPDgEGRllQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAhRT 81
Cdd:PRK09813 1 KKLATIGDNCVDIYPQ-LGK--AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG-VT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 82 STVVVDLDD----HGERSFTFMvrpsADLFLEPADLpSFSAGEWLHVCSIALSAEpsrsaafQAMTSIREAGGYVSFDPN 157
Cdd:PRK09813 77 AQTQVELHDndrvFGDYTEGVM----ADFALSEEDY-AWLAQYDIVHAAIWGHAE-------DAFPQLHAAGKLTAFDFS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 158 IRPD--LWadenelrrclELALQHADvvklsveeLTFLTHDAQVKTgLESLMRR---CPARLVLVTLGKEGVIAWhDGA- 231
Cdd:PRK09813 145 DKWDspLW----------QTLVPHLD--------YAFASAPQEDEF-LRLKMKAivaRGAGVVIVTLGENGSIAW-DGAq 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1736704024 232 VKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGA 286
Cdd:PRK09813 205 FWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
7-268 |
2.65e-30 |
|
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: 114.76 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 7 LGDAVVDLLP-DGEGRllqcPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLdpAHRTSTVV 85
Cdd:cd01940 5 IGDNVVDKYLhLGKMY----PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV--KEGENAVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 86 VDLDDHGERSFTFMVR-PSADLFLEPADLPSFSAGEWLHVCSiaLSAEPSRSAAFQAMTSireAGGYVSFDPNIRpdlWA 164
Cdd:cd01940 79 DVELVDGDRIFGLSNKgGVAREHPFEADLEYLSQFDLVHTGI--YSHEGHLEKALQALVG---AGALISFDFSDR---WD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 165 DENelrrcLELALQHADVVKLSVEELTflthDAQVKTGLESLMRRcPARLVLVTLGKEGVIAWHDGAVKHYPATSVECVD 244
Cdd:cd01940 151 DDY-----LQLVCPYVDFAFFSASDLS----DEEVKAKLKEAVSR-GAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVD 220
|
250 260
....*....|....*....|....
gi 1736704024 245 TTGAGDAFVAGLLYGLAAGQELVP 268
Cdd:cd01940 221 TLGAGDSFIAGFLLSLLAGGTAIA 244
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
27-292 |
8.42e-28 |
|
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: 108.54 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 27 GGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDlDDHGERSFTFMVRpsADL 106
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSIT-DITGDRATISITA--IDT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 107 FLEPADLPSFSagewLHVCSIALSAEPSRSAAFQAMTSIREAGgyvsfdpnIRPDLWADENELRRCLELaLQHADVVKLS 186
Cdd:cd01945 113 QAAPDSLPDAI----LGGADAVLVDGRQPEAALHLAQEARARG--------IPIPLDLDGGGLRVLEEL-LPLADHAICS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 187 VEELTFLTHDAQVKTGLesLMRRCPARLVLVTLGKEGVIAWH-DGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQE 265
Cdd:cd01945 180 ENFLRPNTGSADDEALE--LLASLGIPFVAVTLGEAGCLWLErDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMP 257
|
250 260
....*....|....*....|....*..
gi 1736704024 266 LVPVIGLAQRCGALATTAKGAMTALPY 292
Cdd:cd01945 258 LREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
26-286 |
1.34e-25 |
|
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: 102.50 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQ-QMRLDPAHRTSTVVvdlDDHGERSFTFMVRPSA 104
Cdd:cd01947 35 PGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTvAWRDKPTRKTLSFI---DPNGERTITVPGERLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 105 DLFlepaDLPSFSAGEWLHVCSIALSAEPSRSAAFQAMTsIREAGGYVSFDPnirpdlwadenelrrcLELALQHADVVK 184
Cdd:cd01947 112 DDL----KWPILDEGDGVFITAAAVDKEAIRKCRETKLV-ILQVTPRVRVDE----------------LNQALIPLDILI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 185 LSVEELTFLTHdaqvktGLESLMRRcpARLVLVTLGKEGVIAWHDGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQ 264
Cdd:cd01947 171 GSRLDPGELVV------AEKIAGPF--PRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGW 242
|
250 260
....*....|....*....|..
gi 1736704024 265 ELVPVIGLAQRCGALATTAKGA 286
Cdd:cd01947 243 SIEEALELGAQCGAICVSHFGP 264
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
26-266 |
2.37e-25 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 104.99 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTST--VVVDLDDhGERSFTFMVRPS 103
Cdd:PLN02543 171 PGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACsrMKIKFRD-GGKMVAETVKEA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 104 AD--LFLEPADLPSFSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYVSFDPNIRPDLWADENELRRCLELALQHAD 181
Cdd:PLN02543 250 AEdsLLASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEAD 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 182 VVKLSVEELTF-LTHDAQVKTgleslmRRCPARLVLVTLG-------------KEGVIAWHDG-----------AVKHYP 236
Cdd:PLN02543 330 IIEVSRQELEFlLDEDYYERK------RNYPPQYYAESFEqtknwrdyyhytpEEIAPLWHDGlklllvtdgtlRIHYYT 403
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1736704024 237 ATSVECV-------------DTTGAGDAFVAGLLYGLAAGQEL 266
Cdd:PLN02543 404 PKFDGVVvgtedvlitpftcDRTGSGDAVVAAIMRKLTTCPEM 446
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
28-286 |
1.69e-24 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 102.60 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 28 GAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEV--------QQMRLDPAHRT--STVVVD-LDDHGersf 96
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVvgliegtdAGDSSSASYETllCWVLVDpLQRHG---- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 97 tFMVRpsADLFLEPA-----DLPSfSAGEWLHVCSIALSA-----EPSRSAAFQAMTSIREAGGYVSFDPNIRPDLWADE 166
Cdd:PLN02341 196 -FCSR--ADFGPEPAfswisKLSA-EAKMAIRQSKALFCNgyvfdELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 167 -NELRRCLELALQHADVVKLSVEELTFLTHDAQVKTGLESLMRR-CPARLVLVTLGKEGVIAWHDGAVKHYPATSVECVD 244
Cdd:PLN02341 272 tPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPgIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVD 351
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1736704024 245 TTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGA 286
Cdd:PLN02341 352 TVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCGA 393
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
27-296 |
1.39e-21 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 92.49 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 27 GGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMrldpaHRTSTVVVDLD----DHGERSFTFMVRP 102
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFV-----SRTENSSTGLAmifvDTKTGNNEIVIIP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 103 SADLFLEPADLpSFSAGEWLHVCSIAL-SAEPSRSAAFQAMTSIREAGGYVSFdpNIRPDLWADENELRRCLelaLQHAD 181
Cdd:PTZ00292 127 GANNALTPQMV-DAQTDNIQNICKYLIcQNEIPLETTLDALKEAKERGCYTVF--NPAPAPKLAEVEIIKPF---LKYVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 182 VVKLSVEELTFLT----HDAQVKTGLESLMRRCPARLVLVTLGKEG-VIAWHDGAVKHYPATSVECVDTTGAGDAFVAGL 256
Cdd:PTZ00292 201 LFCVNEVEAALITgmevTDTESAFKASKELQQLGVENVIITLGANGcLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSM 280
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1736704024 257 LYGLAAGQELVPVIGLAQRCGALATTAKGAMTALPYHHEL 296
Cdd:PTZ00292 281 AYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
1-296 |
1.56e-20 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 89.16 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 1 MKKIWVLGDAVVD------LLPD-GE---GRLLQC-PGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVE 69
Cdd:PRK11142 2 MGKLVVLGSINADhvlnleSFPRpGEtltGRHYQVaFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 70 VQQMRLDPAHRTSTVVVDLDDHGERSFTfmVRPSADLFLEPADLPSFSA----GEWLhvcsiALSAEPSRSAAFQAMTSI 145
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIG--IHAGANAALTPALVEAHRElianADAL-----LMQLETPLETVLAAAKIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 146 REAGGYVSFDPnirpdlwADENELRrcLELaLQHADVVKLSVEELTFLT-------HDAQV------KTGLESlmrrcpa 212
Cdd:PRK11142 155 KQHGTKVILNP-------APARELP--DEL-LALVDIITPNETEAEKLTgirveddDDAAKaaqvlhQKGIET------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 213 rlVLVTLGKEGVIAWHDGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGAMTALPY 292
Cdd:PRK11142 218 --VLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPW 295
|
....
gi 1736704024 293 HHEL 296
Cdd:PRK11142 296 REEI 299
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
27-280 |
2.52e-20 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 90.72 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 27 GGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHGERSFTFMVRPSADL 106
Cdd:COG3892 38 GGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 107 FLEPADlpsFSAGEWLHVCSIA-----LSAEPSRSAAFQAMTSIREAGGYVSFDPNIRPDLW-------------ADENE 168
Cdd:COG3892 118 ALTEDD---IDEAFIASARALLitgthLSHPRTRAAVLKALRYARAHGGKVVLDIDYRPVLWgltghgdgetrfvASDAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 169 LRRcLELALQHADVVKLSVEELTFLTHDAQVKTGLESLMRRCPARLVLVTLGK-----EGVI--AWHDGAVkhYPATSVE 241
Cdd:COG3892 195 TAH-LQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLVCKRGALgcvvfEGAIpdDLDDGIT--GPGFPVE 271
|
250 260 270
....*....|....*....|....*....|....*....
gi 1736704024 242 CVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALA 280
Cdd:COG3892 272 VFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALV 310
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
26-280 |
1.27e-19 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 87.17 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGApANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTST---VVVDLD-----DHGERSFT 97
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTktrVIAGGQqllrlDFEDRFPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 98 FMVRPSADLFLEPADLPSFSAGewlhVCS----IALSAEPSRSAAFQAmtsiREAGGYVSFDPNiRPDLWAdenelrrcl 173
Cdd:COG2870 134 SAELEARLLAALEAALPEVDAV----ILSdygkGVLTPELIQALIALA----RAAGKPVLVDPK-GRDFSR--------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 174 elaLQHADVVKLSVEELTFLTH-----DAQVKTGLESLMRRCPARLVLVTLGKEGV-IAWHDGAVKHYPATSVECVDTTG 247
Cdd:COG2870 196 ---YRGATLLTPNLKEAEAAVGipiadEEELVAAAAELLERLGLEALLVTRGEEGMtLFDADGPPHHLPAQAREVFDVTG 272
|
250 260 270
....*....|....*....|....*....|...
gi 1736704024 248 AGDAFVAGLLYGLAAGQELVPVIGLAQRCGALA 280
Cdd:COG2870 273 AGDTVIATLALALAAGASLEEAAELANLAAGIV 305
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
3-267 |
1.64e-19 |
|
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: 85.53 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDLLPDGEGRLLQcPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVqqmrlDPAHRTS 82
Cdd:cd01937 1 KIVIIGHVTIDEIVTNGSGVVK-PGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVIS-----LLSTETT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 83 TVVVDLDDHGeRSFTFMVRPSADLFLEPADlpSFSAGEWLHVCSIALSAEPSrsaafqamtsIREAGGYVSFDPN--IRP 160
Cdd:cd01937 75 TFELNYTNEG-RTRTLLAKCAAIPDTESPL--STITAEIVILGPVPEEISPS----------LFRKFAFISLDAQgfLRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 161 dlWADENELRRcleLALQHADVVKLSVEELtflthdAQVKTGLES--LMRRCPARLVLVTLGKEGVIAWHDGAVKHYPAT 238
Cdd:cd01937 142 --ANQEKLIKC---VILKLHDVLKLSRVEA------EVISTPTELarLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPAS 210
|
250 260
....*....|....*....|....*....
gi 1736704024 239 SVECVDTTGAGDAFVAGLLYGLAAGQELV 267
Cdd:cd01937 211 KKDVVDPTGAGDVFLAAFLYSRLSGKDIK 239
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
26-286 |
1.70e-19 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 86.34 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPANVAVGVARLGGNS---AFIGrvGDDpfGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHGErsfTfmvrp 102
Cdd:COG1105 34 PGGKGINVARVLKALGVDVtalGFLG--GFT--GEFIEELLDEEGIPTDFVPIEGETRINIKIVDPSDGTE---T----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 103 sadLFLEPAdlPSFSAGEWlhvcsialsaepsrSAAFQAMTSIREAGGYV----SFDPNIRPDLWAD------ENELR-- 170
Cdd:COG1105 102 ---EINEPG--PEISEEEL--------------EALLERLEELLKEGDWVvlsgSLPPGVPPDFYAElirlarARGAKvv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 171 -----RCLELALQ-HADVVKLSVEELTFLTH-----DAQVKTGLESLMRRcPARLVLVTLGKEGVIAWHDGAVKHYPATS 239
Cdd:COG1105 163 ldtsgEALKAALEaGPDLIKPNLEELEELLGrpletLEDIIAAARELLER-GAENVVVSLGADGALLVTEDGVYRAKPPK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1736704024 240 VECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGA 286
Cdd:COG1105 242 VEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGT 288
|
|
| PLN02967 |
PLN02967 |
kinase |
21-281 |
8.42e-19 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 86.25 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 21 RLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHGERSFTfMV 100
Cdd:PLN02967 237 KFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTT-CV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 101 RPSADLFLEPADLPS--FSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYVSFDPNIRPDLWADENELRRCLELALQ 178
Cdd:PLN02967 316 KPCAEDSLSKSEINIdvLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWN 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 179 HADVVKLSVEELTFL-------------------TH-DAQVKTGL--ESLmrrcpaRLVLVTLGKEGVIAW---HDGAVK 233
Cdd:PLN02967 396 LADIIEVTKQELEFLcgiepteefdtkdndkskfVHySPEVVAPLwhENL------KVLFVTNGTSKIHYYtkeHNGAVH 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1736704024 234 ---HYPATSVECvDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALAT 281
Cdd:PLN02967 470 gmeDAPITPFTS-DMSASGDGIVAGLMRMLTVQPHLITDKGYLEKTIKYAI 519
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
26-280 |
1.22e-18 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 84.15 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGApANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRlDPAHRTST---VVVD--------------L 88
Cdd:cd01172 39 LGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTTTktrVIARnqqllrvdreddspL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 89 DDHGERSFTFMVR---PSADLFLepadLPSFSAGewlhVCSIALSAEPSRSAafqamtsiREAGGYVSFDPnirpdlwad 165
Cdd:cd01172 117 SAEEEQRLIERIAerlPEADVVI----LSDYGKG----VLTPRVIEALIAAA--------RELGIPVLVDP--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 166 enelrRCLELAL-QHADVVKLSVEELTFLTH-----DAQVKTGLESLMRRCPARLVLVTLGKEGVIAW-HDGAVKHYPAT 238
Cdd:cd01172 172 -----KGRDYSKyRGATLLTPNEKEAREALGdeindDDELEAAGEKLLELLNLEALLVTLGEEGMTLFeRDGEVQHIPAL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1736704024 239 SVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALA 280
Cdd:cd01172 247 AKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVV 288
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-285 |
3.46e-16 |
|
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: 77.08 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDL------LP----DGEGRLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQ 72
Cdd:cd01944 1 KVLVIGAAVVDIvldvdkLPasggDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 73 MRLdPAHRTSTVVVDLDDHGERSFTFMVRPSADLFLEPADLPSFSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYV 152
Cdd:cd01944 81 PPR-GGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 153 SFDPNIRPDLwADENELRRCLELALqhadVVKLSVEELTFLT---HDAQVKTGLESLMRRcpARLVLVTLGKEGviAW-- 227
Cdd:cd01944 160 VFDPGPRISD-IPDTILQALMAKRP----IWSCNREEAAIFAergDPAAEASALRIYAKT--AAPVVVRLGSNG--AWir 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1736704024 228 -HDGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKG 285
Cdd:cd01944 231 lPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
26-285 |
2.74e-15 |
|
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: 74.49 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPANVAVGVARLGGNSAFIGRVGDDpFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHgersfTFM-VRPSA 104
Cdd:cd01164 35 AGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGT-----ETEiNEPGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 105 DLflEPADLPSF--------SAGEWLHVC-SIALSAEPSrsaAFQAMTSI-REAGGYVSFDpnirpdlwADENELRRCLE 174
Cdd:cd01164 109 EI--SEEELEALleklkallKKGDIVVLSgSLPPGVPAD---FYAELVRLaREKGARVILD--------TSGEALLAALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 175 lalQHADVVKLSVEEL------TFLTHDAQVKTGLEslMRRCPARLVLVTLGKEGVIAWHDGAVKHYPATSVECVDTTGA 248
Cdd:cd01164 176 ---AKPFLIKPNREELeelfgrPLGDEEDVIAAARK--LIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGA 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 1736704024 249 GDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKG 285
Cdd:cd01164 251 GDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
25-296 |
1.67e-14 |
|
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: 72.22 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 25 CPGGAPANVAVGVARLGGNSAFIGRVGDDPfGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDdhgERSFTFMV---- 100
Cdd:TIGR03168 33 DAGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKESS---GEETELNEpgpe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 101 --RPSADLFLE--PADLPSfsaGEWLhvcSIALSAEPSRSAAF--QAMTSIREAGGYVSFDpnirpdlwADENELRRCLE 174
Cdd:TIGR03168 109 isEEELEQLLEklRELLAS---GDIV---VISGSLPPGVPPDFyaQLIAIARKKGAKVILD--------TSGEALREALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 175 lalQHADVVKLSVEELTFLTH-----DAQVKTGLESLMRRcPARLVLVTLGKEGVIAWHDGAVKHYPATSVECVDTTGAG 249
Cdd:TIGR03168 175 ---AKPFLIKPNHEELEELFGrelktLEEIIEAARELLDR-GAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1736704024 250 DAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGamTALPYHHEL 296
Cdd:TIGR03168 251 DSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPDPEDV 295
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
26-266 |
4.76e-13 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 68.20 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPAN---VAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRlDPAHRTSTVVVDLDDhGERSF------ 96
Cdd:PLN02548 51 AGGATQNsirVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVNVHYYE-DESTPTGTCAVLVVG-GERSLvanlsa 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 97 ------TFMVRPSADLFLEPADLpSFSAGEWLHVC--SIALSAEPSR----------SAAF-------QAMtsirEAGGY 151
Cdd:PLN02548 129 ancykvEHLKKPENWALVEKAKF-YYIAGFFLTVSpeSIMLVAEHAAannktfmmnlSAPFiceffkdQLM----EALPY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 152 VSFdpnirpdLWADENElrrclelALQHADVVKLSVEELtflthdAQVKTGLESLMRRC--PARLVLVTLGKEGVIAWHD 229
Cdd:PLN02548 204 VDF-------LFGNETE-------ARTFAKVQGWETEDV------EEIALKISALPKASgtHKRTVVITQGADPTVVAED 263
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1736704024 230 GAVKHYPATSVE---CVDTTGAGDAFVAGLLYGLAAGQEL 266
Cdd:PLN02548 264 GKVKEFPVIPLPkekLVDTNGAGDAFVGGFLSQLVQGKDI 303
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
20-286 |
1.65e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 67.14 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 20 GRLLQ----CP-----GGAPANVAVGVARLGGNS--------AFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHrTS 82
Cdd:PLN02813 110 GKVLRaldgCSykasaGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGT-TG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 83 TVVVDLDDHGERSFTFMVRPSADLFLEPADLPSFSAGEWLHVCSIALSAEPSRSAAFQAMTSIREAGGYVSF---DPNI- 158
Cdd:PLN02813 189 TVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASAISKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVtasDVSCi 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 159 ---RPDLWadenelrrclELALQHADVVKLSVEELTFLTHDAQVKTGLES---LMRRCParLVLVTLGKEGVIAWHDGAV 232
Cdd:PLN02813 269 erhRDDFW----------DVMGNYADILFANSDEARALCGLGSEESPESAtryLSHFCP--LVSVTDGARGSYIGVKGEA 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1736704024 233 KHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIG-LAQRCGALATTAKGA 286
Cdd:PLN02813 337 VYIPPSPCVPVDTCGAGDAYAAGILYGLLRGVSDLRGMGeLAARVAATVVGQQGT 391
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
133-261 |
1.82e-12 |
|
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: 64.81 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 133 PSRSAAFQAMTSIREAGGYVSFDPNIRPDLWADENelrrcLELALQHADVVKLSVEELTFLTH----DAQVKTGLESLMR 208
Cdd:cd00287 68 PAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-----LEKLLPGVDILTPNEEEAEALTGrrdlEVKEAAEAAALLL 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1736704024 209 RCPARLVLVTLGKEGVIAWH-DGAVKHYPATSVECVDTTGAGDAFVAGLLYGLA 261
Cdd:cd00287 143 SKGPKVVIVTLGEKGAIVATrGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
24-286 |
1.43e-11 |
|
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: 63.76 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 24 QCPGGAPANVAVGVARLGGNSAFIGRVGDDPfGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDH-------Gersf 96
Cdd:TIGR03828 32 IDAGGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVRVPGETRINVKIKEPSGTetklngpG---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 97 tFMVRPSA-DLFLE--PADLPsfsAGEWLhVCSIALSAEPSRSAAFQAMTSIREAGGYVSFDpnirpdlwADENELRRCL 173
Cdd:TIGR03828 107 -PEISEEElEALLEklRAQLA---EGDWL-VLSGSLPPGVPPDFYAELIALAREKGAKVILD--------TSGEALRDGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 174 ElalQHADVVKLSVEELTFLTHDAQvkTGLESL------MRRCPARLVLVTLGKEGVI------AWHDGAVKhypatsVE 241
Cdd:TIGR03828 174 K---AKPFLIKPNDEELEELFGREL--KTLEEIieaareLLDLGAENVLISLGADGALlvtkegALFAQPPK------GE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1736704024 242 CVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALATTAKGA 286
Cdd:TIGR03828 243 VVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGT 287
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
16-266 |
1.89e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 63.66 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 16 PDGEGRLLQCPGGAPANVAVGVAR-LGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHrTSTVVVDLDDHGER 94
Cdd:PLN02379 75 PDDLSPIKTMAGGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGP-TAQCVCLVDALGNR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 95 S----FTFMVRPSADLFLEPadlpSFSAGEWLHVCSIALSAEPSRSAAFQAmtsiREAGGYVSFD-------PNIRPdlw 163
Cdd:PLN02379 154 TmrpcLSSAVKLQADELTKE----DFKGSKWLVLRYGFYNLEVIEAAIRLA----KQEGLSVSLDlasfemvRNFRS--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 164 adenELRRCLE-----LALQHADvvklSVEELTFLTHDAQVKTGLESLMRRCpaRLVLVTLGKEGVIAWHDGAVKHYPAT 238
Cdd:PLN02379 223 ----PLLQLLEsgkidLCFANED----EARELLRGEQESDPEAALEFLAKYC--NWAVVTLGSKGCIARHGKEVVRVPAI 292
|
250 260
....*....|....*....|....*....
gi 1736704024 239 -SVECVDTTGAGDAFVAGLLYGLAAGQEL 266
Cdd:PLN02379 293 gETNAVDATGAGDLFASGFLYGLIKGLSL 321
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-280 |
6.47e-11 |
|
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: 61.56 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 3 KIWVLGDAVVDL-------LPDGE---GRLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQilADEQVEVQq 72
Cdd:cd01941 1 EIVVIGAANIDLrgkvsgsLVPGTsnpGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILE--ESEKAGLN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 73 MR--LDPAHRTSTVVVDLDDHGE-------------------RSFTFMVRpSADLFLEPADLPSFSAGEWLHVC---SIA 128
Cdd:cd01941 78 VRgiVFEGRSTASYTAILDKDGDlvvaladmdiyelltpdflRKIREALK-EAKPIVVDANLPEEALEYLLALAakhGVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 129 LSAEPSRSAAFQAMTSIREAGGYVSfdPNirpdlwadENELRRCLELAlqHADVVKLSVEELTFLTHdaqvktGLESLMR 208
Cdd:cd01941 157 VAFEPTSAPKLKKLFYLLHAIDLLT--PN--------RAELEALAGAL--IENNEDENKAAKILLLP------GIKNVIV 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736704024 209 RCPARLVLVTLGKEGVIAWHdgavkhYPA-TSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALA 280
Cdd:cd01941 219 TLGAKGVLLSSREGGVETKL------FPApQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
26-267 |
1.19e-07 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 52.34 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGAPANVAvGVAR-----LGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPA----------HRTSTVVVDLDD 90
Cdd:PTZ00247 61 PGGSALNTA-RVAQwmlqaPKGFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAptgtcavlvcGKERSLVANLGA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 91 HGERSFTFMVRPSADLFLEPADLpSFSAGEWLHVcsialSAEPSRSAAFQAmtsiREAGGYVSFD---PNIRPDLWadeN 167
Cdd:PTZ00247 140 ANHLSAEHMQSHAVQEAIKTAQL-YYLEGFFLTV-----SPNNVLQVAKHA----RESGKLFCLNlsaPFISQFFF---E 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 168 ELRrcleLALQHADVVKLSVEEL-TFLTHDAQVKTGLESLMRRCPA---------RLVLVTLGKEGVIAWHDGAVKHYPA 237
Cdd:PTZ00247 207 RLL----QVLPYVDILFGNEEEAkTFAKAMKWDTEDLKEIAARIAMlpkysgtrpRLVVFTQGPEPTLIATKDGVTSVPV 282
|
250 260 270
....*....|....*....|....*....|...
gi 1736704024 238 TSV---ECVDTTGAGDAFVAGLLYGLAAGQELV 267
Cdd:PTZ00247 283 PPLdqeKIVDTNGAGDAFVGGFLAQYANGKDID 315
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
20-280 |
3.90e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 50.76 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 20 GRLLQCPGGAPANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLDPAHRTSTVVVDLDDHGE-----R 94
Cdd:PRK09850 33 GKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEmlvaiN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 95 SFTFMVRPSADLFLEPADlpsFSAGEWLHVCSIALSAEpsrsaafqAMTSIREAGGYVSfdpnirpdLWADENELRRCLE 174
Cdd:PRK09850 113 DMNISNAITAEYLAQHRE---FIQRAKVIVADCNISEE--------ALAWILDNAANVP--------VFVDPVSAWKCVK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 175 LALQHADVVKLSVEELTFLTHDAQVKTGLESLMRRCP-------ARLVLvTLGKEGV-IAWHDGAVKHYPATSVECVDTT 246
Cdd:PRK09850 174 VRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAwfhqhglNRLVL-SMGGDGVyYSDISGESGWSAPIKTNVINVT 252
|
250 260 270
....*....|....*....|....*....|....
gi 1736704024 247 GAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALA 280
Cdd:PRK09850 253 GAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMA 286
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
26-285 |
1.32e-05 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 46.36 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 26 PGGApANVAVGVARLGGNSAFIGRVGDDPFGRFMYQILADEQVEVQQMRLdPAHRTST-----------VVVDLDDhger 94
Cdd:PRK11316 50 PGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSV-PTHPTITklrvlsrnqqlIRLDFEE---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 95 sfTFMVRPSADLF--LEPAdLPSFSAgewlhvcsIALS-------AEPsrsaafQAMTSI-REAGGYVSFDPN------- 157
Cdd:PRK11316 124 --GFEGVDPQPLLerIEQA-LPSIGA--------LVLSdyakgalASV------QAMIQLaRKAGVPVLIDPKgtdfery 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 158 -----IRPDL---------WADENELrrclelalqhadvvklsveeltflthdaqVKTGLEsLMRRCPARLVLVTLGKEG 223
Cdd:PRK11316 187 rgatlLTPNLsefeavvgkCKDEAEL-----------------------------VEKGMK-LIADYDLSALLVTRSEQG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736704024 224 V-IAWHDGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQElvpvigLAQRCgALATTAKG 285
Cdd:PRK11316 237 MtLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNS------LEEAC-ALANAAAG 292
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
215-280 |
1.46e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 45.84 E-value: 1.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736704024 215 VLVTLGKEGVIAWHDGAVKHYPATSVECVDTTGAGDAFVAGLLYGLAAGQELVPVIGLAQRCGALA 280
Cdd:PRK09513 220 VVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALA 285
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
166-289 |
4.87e-05 |
|
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: 43.93 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 166 ENELRRCLELAlQHADVVKLSveeLTFLTHDAQvKTGLESLMRRCP----ARLVLVTLGKEGVIAWH-DGAVKHYPATSV 240
Cdd:cd01939 167 EKPREELLELA-AYCDVVFVS---KDWAQSRGY-KSPEECLRGEGPrakkAALLVCTWGDQGAGALGpDGEYVHSPAHKP 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1736704024 241 E-CVDTTGAGDAFVAGLLYGLAAGQELVPViglAQRCGALATTAKGAMTA 289
Cdd:cd01939 242 IrVVDTLGAGDTFNAAVIYALNKGPDDLSE---ALDFGNRVASQKCTGVG 288
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
182-263 |
2.63e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 42.10 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 182 VVKLSVEELTFLThdaqvktgLESLMRRCparLVLVTLGKEGV-IAWHDGAVkHYPATSVECVDTTGAGDAFVAGLLYGL 260
Cdd:PLN02630 184 FLKASSEEALFID--------VEEVRQKC---CVIVTNGKKGCrIYWKDGEM-RVPPFPAIQVDPTGAGDSFLGGFVAGL 251
|
...
gi 1736704024 261 AAG 263
Cdd:PLN02630 252 VQG 254
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
220-280 |
6.61e-04 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 40.79 E-value: 6.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736704024 220 GKEG--VIAWHDGAVKHYPA--TSVECV-DTTGAGDAFVAGLLYGLAAGQELVPviglAQRCGALA 280
Cdd:cd01943 233 GKLGcyVGSADSGPELWLPAyhTKSTKVvDPTGGGNSFLGGFAAGLALTKSIDE----ACIYGSVA 294
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
177-276 |
3.01e-03 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 38.60 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736704024 177 LQHADVVKLSVEELTFLTHDAQ-VKTGleSLMRRCPARLVLVTLGKEGVIAWHDGAVKHYPATSVECV-DTTGAGDAFvA 254
Cdd:cd01946 161 LAKVDVVIINDGEARQLTGAANlVKAA--RLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDTF-A 237
|
90 100
....*....|....*....|..
gi 1736704024 255 GLLYGLAAGQELVPVIGLAQRC 276
Cdd:cd01946 238 GGFIGYLASQKDTSEANMRRAI 259
|
|
|