|
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: 551.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 1 MKKIWVLGDAVVDLLPDGEGRLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHR 80
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 81 TSTVVVDLDDQGERSFTFMVRPSADLFLESADLPTFSAGEWLHVCSIALSAEPSRSATFEAMAAIREAGGYVSFDPNIRP 160
Cdd:PRK09434 82 TSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 161 DLWPDENALRRCLELALQSADVVKLSVEELAFLTGNVEVNVGLHVLMARCPARLVLVTQGKEGVIAWHDGAVEHYPATPV 240
Cdd:PRK09434 162 DLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSV 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1069055653 241 ECVDTTGAGDAFVAGLLYGLAAGQDLT------PVIALAQRCGALATTAKGAMTALPWQHDL 296
Cdd:PRK09434 242 DPVDTTGAGDAFVAGLLAGLSQAGLWTdeaelaEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-287 |
2.84e-109 |
|
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: 318.43 E-value: 2.84e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDLLPDGEGRLLQ---CPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAH 79
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETftkAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 80 RTSTVVVDLDDQGERSFTFMVRPSADLFLESADLPT-FSAGEWLHVCSIALSAEPSRSATFEAMAAIREAGGYVSFDPNI 158
Cdd:cd01167 81 PTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDlLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLISFDPNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 159 RPDLWPDENALRRCLELALQSADVVKLSVEELAFLTGNVEVNVGLHvLMARCPARLVLVTQGKEGVIAWHDGAVEHYPAT 238
Cdd:cd01167 161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAA-LLLLFGLKLVLVTRGADGALLYTKGGVGEVPGI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1069055653 239 PVECVDTTGAGDAFVAGLLYGLAAGQD-------LTPVIALAQRCGALATTAKGAM 287
Cdd:cd01167 240 PVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-296 |
2.94e-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: 270.60 E-value: 2.94e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDLLPDGE-----------GRLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVK 71
Cdd:COG0524 1 DVLVIGEALVDLVARVDrlpkggetvlaGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 72 FLRLDPAHRTSTVVVDLDDQGERSFTFMvrPSADLFLESADLP--TFSAGEWLHVCSIALSAEPSRSATFEAMAAIREAG 149
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFY--RGANAELTPEDLDeaLLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 150 GYVSFDPNIRPDLWpdeNALRRCLELALQSADVVKLSVEELAFLTGNVEVNVGLHVLMARcPARLVLVTQGKEGVIAWHD 229
Cdd:COG0524 159 VPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLAR-GVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069055653 230 GAVEHYPATPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGAMTALPWQHDL 296
Cdd:COG0524 235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
7-291 |
6.06e-77 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 237.60 E-value: 6.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 7 LGDAVVDLLPDGEG-------RLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAH 79
Cdd:PLN02323 16 FGEMLIDFVPTVSGvslaeapAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 80 RTSTVVVDLDDQGERSFTFMVRPSADLFLESADLPT--FSAGEWLHVCSIALSAEPSRSATFEAMAAIREAGGYVSFDPN 157
Cdd:PLN02323 96 RTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLdlIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSYDPN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 158 IRPDLWPDENALRRCLELALQSADVVKLSVEELAFLTGNVEVNVGLHVLMARCPARLVLVTQGKEGVIAWHDGAVEHYPA 237
Cdd:PLN02323 176 LRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEG 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069055653 238 TPVECVDTTGAGDAFVAGLLYGLAAGQD-------LTPVIALAQRCGALATTAKGAMTALP 291
Cdd:PLN02323 256 FKVKAVDTTGAGDAFVGGLLSQLAKDLSlledeerLREALRFANACGAITTTERGAIPALP 316
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-287 |
3.68e-76 |
|
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: 234.39 E-value: 3.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDLLPDGEGRLLQC------PGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLD 76
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQAdsfrkfFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 77 PAHRTSTVVVDLDDQGERSFTFMVRPSADLFLESADLPT--FSAGEWLHVCSIALSAEPS-RSATFEAMAAIREAGGYVS 153
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEaaLAGADHLHLSGITLALSESaREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 154 FDPNIRPDLWPDENAlRRCLELALQSADVVKLSVEELAFLTGNVEVNVGLH-VLMARCPARLVLVTQGKEGVIAWHDGAV 232
Cdd:cd01166 161 FDLNYRPKLWSAEEA-REALEELLPYVDIVLPSEEEAEALLGDEDPTDAAErALALALGVKAVVVKLGAEGALVYTGGGR 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1069055653 233 EHYPATPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGAM 287
Cdd:cd01166 240 VFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-288 |
1.16e-72 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 225.30 E-value: 1.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDLLPDGEG---------RLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFL 73
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGlpgelvrvsTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 74 RLDPAHRTSTVVVDLDDQGERSFTFMVRPSADLFLE--SADLPTFSAGEWLHVCSIALSaePSRSATFEAMAAIREAGGY 151
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEelEENEDLLENADLLYISGSLPL--GLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 152 vsFDPNIRPDLWPDENALRRCLELalqsADVVKLSVEELAFLTG--NVEVNVGLHVLMARCP--ARLVLVTQGKEGVIAW 227
Cdd:pfam00294 159 --FDPNLLDPLGAAREALLELLPL----ADLLKPNEEELEALTGakLDDIEEALAALHKLLAkgIKTVIVTLGADGALVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1069055653 228 HDGAVEHYPATP-VECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGAMT 288
Cdd:pfam00294 233 EGDGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
27-291 |
1.04e-59 |
|
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: 192.43 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 27 GGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADL 106
Cdd:TIGR04382 34 GGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPGRRTSLVFLEIKPPDEFPLLFYRENAADL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 107 FLESADLPT--FSAGEWLHVCSIALSAEPSRSATFEAMAAIREAGGYVSFDPNIRPDLWPDENALRRCLELALQSADVVK 184
Cdd:TIGR04382 114 ALTPDDVDEdyIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVLDIDYRPYLWKSPEEAGIYLRLVLPLVDVII 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 185 LSVEELAFLTGNVEVNVGLHVLMARCPArLVLVTQGKEGVIAWH-DGAVEHYPATPVECVDTTGAGDAFVAGLLYGLAAG 263
Cdd:TIGR04382 194 GTREEFDIAGGEGDDEAAARALLDAGVE-ILVVKRGPEGSLVYTgDGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAG 272
|
250 260
....*....|....*....|....*...
gi 1069055653 264 QDLTPVIALAQRCGALATTAKGAMTALP 291
Cdd:TIGR04382 273 WDLEKALRYGNACGAIVVSRHSCSPAMP 300
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
3-292 |
3.83e-46 |
|
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: 156.94 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDL------LPD-GE----GRLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVK 71
Cdd:cd01174 1 KVVVVGSINVDLvtrvdrLPKpGEtvlgSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 72 FLRLDPAHRTSTVVVDLDDQGERSFtfMVRPSADLFLESADLPtfSAGEWLHVCSIALS-AEPSRSATFEAMAAIREAGG 150
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRI--VVVPGANGELTPADVD--AALELIAAADVLLLqLEIPLETVLAALRAARRAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 151 YVSFDP----NIRPDLWPdenalrrclelalqSADVVKLSVEELAFLTGNVEVNVGLHVLMARC----PARLVLVTQGKE 222
Cdd:cd01174 157 TVILNPaparPLPAELLA--------------LVDILVPNETEAALLTGIEVTDEEDAEKAARLllakGVKNVIVTLGAK 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 223 GVIAWHDGAVEHYPATPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGAMTALPW 292
Cdd:cd01174 223 GALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
26-286 |
1.20e-38 |
|
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: 137.06 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVdLDDQGERSFTFMVRPSAD 105
Cdd:cd01942 35 FGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFI-LTDGDDNQIAYFYPGAMD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 106 LFLESADLPTFSAGEWLHVcsialsaePSRSATFEAMAAIREAGGYVSFDPNirPDLWPDENA-LRRCLELAlqsaDVV- 183
Cdd:cd01942 114 ELEPNDEADPDGLADIVHL--------SSGPGLIELARELAAGGITVSFDPG--QELPRLSGEeLEEILERA----DILf 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 184 ------KLSVEelafLTGNVEVNVGLHVlmarcpaRLVLVTQGKEGVIAWHDGAVEHYPATP-VECVDTTGAGDAFVAGL 256
Cdd:cd01942 180 vndyeaELLKE----RTGLSEAELASGV-------RVVVVTLGPKGAIVFEDGEEVEVPAVPaVKVVDTTGAGDAFRAGF 248
|
250 260 270
....*....|....*....|....*....|
gi 1069055653 257 LYGLAAGQDLTPVIALAQRCGALATTAKGA 286
Cdd:cd01942 249 LYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
21-286 |
2.05e-34 |
|
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: 126.96 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 21 RLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHrTSTVVVDLDDQGERSFTFMV 100
Cdd:cd01168 49 PVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGP-TGTCAVLVTPDAERTMCTYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 101 RPSADLFLESADLPTFSAGEWLHVcSIALSAEPSRSAtFEAMAAIREAGGYVSF---DPNI----RPDLWPdenalrrcl 173
Cdd:cd01168 128 GAANELSPDDLDWSLLAKAKYLYL-EGYLLTVPPEAI-LLAAEHAKENGVKIALnlsAPFIvqrfKEALLE--------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 174 elALQSADVVKLSVEELAFLTGNVE---VNVGLHVLMARCpaRLVLVTQGKEGVIAWHDGAVEHYPA-TPVECVDTTGAG 249
Cdd:cd01168 197 --LLPYVDILFGNEEEAEALAEAETtddLEAALKLLALRC--RIVVITQGAKGAVVVEGGEVYPVPAiPVEKIVDTNGAG 272
|
250 260 270
....*....|....*....|....*....|....*..
gi 1069055653 250 DAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGA 286
Cdd:cd01168 273 DAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
26-296 |
2.54e-34 |
|
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: 126.18 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQGERSFtfMVRPSAD 105
Cdd:TIGR02152 30 PGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRI--VVVAGAN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 106 LFLESADLPtfSAGEWLHVCSIALSA-EPSRSATFEAMAAIREAGGYVSFDPN-IRPDLwPDEnalrrclelALQSADVV 183
Cdd:TIGR02152 108 AELTPEDID--AAEALIAESDIVLLQlEIPLETVLEAAKIAKKHGVKVILNPApAIKDL-DDE---------LLSLVDII 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 184 KLSVEELAFLTGNVEVNV-----GLHVLMARCPaRLVLVTQGKEGVIaWHDGA-VEHYPATPVECVDTTGAGDAFVAGLL 257
Cdd:TIGR02152 176 TPNETEAEILTGIEVTDEedaekAAEKLLEKGV-KNVIITLGSKGAL-LVSKDeSKLIPAFKVKAVDTTAAGDTFNGAFA 253
|
250 260 270
....*....|....*....|....*....|....*....
gi 1069055653 258 YGLAAGQDLTPVIALAQRCGALATTAKGAMTALPWQHDL 296
Cdd:TIGR02152 254 VALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
2-286 |
1.80e-32 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 120.61 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 2 KKIWVLGDAVVDLLPDgEGRllQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAhRT 81
Cdd:PRK09813 1 KKLATIGDNCVDIYPQ-LGK--AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG-VT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 82 STVVVDLDDqGERSFTFMVRPS-ADLFLESADLpTFSAGEWLHVCSIALSAEpsrsatfEAMAAIREAGGYVSFDPNIRP 160
Cdd:PRK09813 77 AQTQVELHD-NDRVFGDYTEGVmADFALSEEDY-AWLAQYDIVHAAIWGHAE-------DAFPQLHAAGKLTAFDFSDKW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 161 D--LWpdeNALRRCLELALQSADVVKLSVEElaFLTGNVEvnvglhvlmarCPARLVLVTQGKEGVIAWhDGA-VEHYPA 237
Cdd:PRK09813 148 DspLW---QTLVPHLDYAFASAPQEDEFLRL--KMKAIVA-----------RGAGVVIVTLGENGSIAW-DGAqFWRQAP 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1069055653 238 TPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGA 286
Cdd:PRK09813 211 EPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
7-278 |
1.24e-31 |
|
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: 118.23 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 7 LGDAVVDLLP-DGEGRllqcPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLdpAHRTSTVV 85
Cdd:cd01940 5 IGDNVVDKYLhLGKMY----PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV--KEGENAVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 86 VDLDDQGERSFTFMVR-PSADLFLESADLPTFSAGEWLH--VCSIALSAEpsrsatfEAMAAIREAGGYVSFDPNIRpdl 162
Cdd:cd01940 79 DVELVDGDRIFGLSNKgGVAREHPFEADLEYLSQFDLVHtgIYSHEGHLE-------KALQALVGAGALISFDFSDR--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 163 WPDENALRRC--LELALQSADvvKLSVEELAFLTGNVeVNVGlhvlmarcpARLVLVTQGKEGVIAWHDGAVEHYPATPV 240
Cdd:cd01940 149 WDDDYLQLVCpyVDFAFFSAS--DLSDEEVKAKLKEA-VSRG---------AKLVIVTRGEDGAIAYDGAVFYSVAPRPV 216
|
250 260 270
....*....|....*....|....*....|....*...
gi 1069055653 241 ECVDTTGAGDAFVAGLLYGLAAGQDltpVIALAQRCGA 278
Cdd:cd01940 217 EVVDTLGAGDSFIAGFLLSLLAGGT---AIAEAMRQGA 251
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
27-291 |
6.66e-30 |
|
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: 114.31 E-value: 6.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 27 GGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDlDDQGERSFTFMVRpsADL 106
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSIT-DITGDRATISITA--IDT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 107 FLESADLPTFSagewLHVCSIALSAEPSRSATFEAMAAIREAGgyvsfdpnIRPDLWPDENALRRCLELaLQSADVVKLS 186
Cdd:cd01945 113 QAAPDSLPDAI----LGGADAVLVDGRQPEAALHLAQEARARG--------IPIPLDLDGGGLRVLEEL-LPLADHAICS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 187 VEELAFLTGNVEVNVGlhVLMARCPARLVLVTQGKEGVIAWH-DGAVEHYPATPVECVDTTGAGDAFVAGLLYGLAAGQD 265
Cdd:cd01945 180 ENFLRPNTGSADDEAL--ELLASLGIPFVAVTLGEAGCLWLErDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMP 257
|
250 260
....*....|....*....|....*.
gi 1069055653 266 LTPVIALAQRCGALATTAKGAMTALP 291
Cdd:cd01945 258 LREALRFASAAAALKCRGLGGRAGLP 283
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
26-260 |
5.02e-26 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 106.92 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTST--VVVDLDDqGERSFTFMVRPS 103
Cdd:PLN02543 171 PGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACsrMKIKFRD-GGKMVAETVKEA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 104 AD--LFLESADLPTFSAGEWLHVCSIALSAEPSRSATFEAMAAIREAGGYVSFDPNIRPDLWPDENALRRCLELALQSAD 181
Cdd:PLN02543 250 AEdsLLASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEAD 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 182 VVKLSVEELAFL-----------------------TGN---------VEVNVGLHVLMarcpaRLVLVTqgkEGVIAWH- 228
Cdd:PLN02543 330 IIEVSRQELEFLldedyyerkrnyppqyyaesfeqTKNwrdyyhytpEEIAPLWHDGL-----KLLLVT---DGTLRIHy 401
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1069055653 229 -----DGAV---EHYPATPVECvDTTGAGDAFVAGLLYGL 260
Cdd:PLN02543 402 ytpkfDGVVvgtEDVLITPFTC-DRTGSGDAVVAAIMRKL 440
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
26-286 |
1.22e-24 |
|
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: 99.80 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDdqGERSFTFMVRPSAD 105
Cdd:cd01947 35 PGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFIDPN--GERTITVPGERLED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 106 LFlesaDLPTFSAGEWLHVCSIALSAEPSRSATfEAMAAIREAGGYVSFDPnirpdlwpdenalrrcLELALQSADVVKL 185
Cdd:cd01947 113 DL----KWPILDEGDGVFITAAAVDKEAIRKCR-ETKLVILQVTPRVRVDE----------------LNQALIPLDILIG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 186 SVEELAfltgnvEVNVGLHVLMARcpARLVLVTQGKEGVIAWHDGAVEHYPATPVECVDTTGAGDAFVAGLLYGLAAGQD 265
Cdd:cd01947 172 SRLDPG------ELVVAEKIAGPF--PRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWS 243
|
250 260
....*....|....*....|.
gi 1069055653 266 LTPVIALAQRCGALATTAKGA 286
Cdd:cd01947 244 IEEALELGAQCGAICVSHFGP 264
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
27-280 |
6.91e-24 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 101.12 E-value: 6.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 27 GGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADL 106
Cdd:COG3892 38 GGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 107 FLESADlptFSAGEWLHVCSIA-----LSAEPSRSATFEAMAAIREAGGYVSFDPNIRPDLW-------------PDENA 168
Cdd:COG3892 118 ALTEDD---IDEAFIASARALLitgthLSHPRTRAAVLKALRYARAHGGKVVLDIDYRPVLWgltghgdgetrfvASDAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 169 LRRcLELALQSADVVKLSVEELAFLTGNVEVNVGLHVLMARCPARLVLVTQGK-----EGVI--AWHDGAVehYPATPVE 241
Cdd:COG3892 195 TAH-LQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLVCKRGALgcvvfEGAIpdDLDDGIT--GPGFPVE 271
|
250 260 270
....*....|....*....|....*....|....*....
gi 1069055653 242 CVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALA 280
Cdd:COG3892 272 VFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALV 310
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
27-291 |
8.19e-24 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 98.66 E-value: 8.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 27 GGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLrldpaHRTSTVVVDLD----DQGERSFTFMVRP 102
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFV-----SRTENSSTGLAmifvDTKTGNNEIVIIP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 103 SADLFLESADLPTfSAGEWLHVCSIAL-SAEPSRSATFEAMAAIREAGGYVSFdpNIRPDLWPDENALRRCLelaLQSAD 181
Cdd:PTZ00292 127 GANNALTPQMVDA-QTDNIQNICKYLIcQNEIPLETTLDALKEAKERGCYTVF--NPAPAPKLAEVEIIKPF---LKYVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 182 VVKLSVEELAFLTG----NVEVNVGLHVLMARCPARLVLVTQGKEGVIAWHDGAVE-HYPATPVECVDTTGAGDAFVAGL 256
Cdd:PTZ00292 201 LFCVNEVEAALITGmevtDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPvHVPGKRVKAVDTTGAGDCFVGSM 280
|
250 260 270
....*....|....*....|....*....|....*
gi 1069055653 257 LYGLAAGQDLTPVIALAQRCGALATTAKGAMTALP 291
Cdd:PTZ00292 281 AYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYP 315
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
26-280 |
1.65e-23 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 97.57 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGApANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTST---VVVD------LDDqgERSF 96
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTktrVIAGgqqllrLDF--EDRF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 97 TFMVRPSADL--FLESAdLPTFSAGewlhVCS----IALSAEPSRsatfEAMAAIREAGGYVSFDPNiRPDLWPDENAL- 169
Cdd:COG2870 132 PLSAELEARLlaALEAA-LPEVDAV----ILSdygkGVLTPELIQ----ALIALARAAGKPVLVDPK-GRDFSRYRGATl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 170 ----RRCLELALQSADVVKLSVEELAfltgnvevnvglHVLMARCPARLVLVTQGKEGV-IAWHDGAVEHYPATPVECVD 244
Cdd:COG2870 202 ltpnLKEAEAAVGIPIADEEELVAAA------------AELLERLGLEALLVTRGEEGMtLFDADGPPHHLPAQAREVFD 269
|
250 260 270
....*....|....*....|....*....|....*.
gi 1069055653 245 TTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALA 280
Cdd:COG2870 270 VTGAGDTVIATLALALAAGASLEEAAELANLAAGIV 305
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
26-286 |
1.29e-21 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 92.12 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPANVAVGIARLGGQS---AFIGrvGDDpfGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQGErsfTfmvrp 102
Cdd:COG1105 34 PGGKGINVARVLKALGVDVtalGFLG--GFT--GEFIEELLDEEGIPTDFVPIEGETRINIKIVDPSDGTE---T----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 103 sadLFLESAdlPTFSAGEWL----HVCSIALSAE---------PSRSATF--EAMAAIREAGGYVSFDPnirpdlwpDEN 167
Cdd:COG1105 102 ---EINEPG--PEISEEELEalleRLEELLKEGDwvvlsgslpPGVPPDFyaELIRLARARGAKVVLDT--------SGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 168 ALRRCLElalQSADVVKLSVEELAFLTG-----NVEVNVGLHVLMARcPARLVLVTQGKEGVIAWHDGAVEHYPATPVEC 242
Cdd:COG1105 169 ALKAALE---AGPDLIKPNLEELEELLGrpletLEDIIAAARELLER-GAENVVVSLGADGALLVTEDGVYRAKPPKVEV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1069055653 243 VDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGA 286
Cdd:COG1105 245 VSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGT 288
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
28-286 |
7.01e-20 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 89.12 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 28 GAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFL--------RLDPAHRTSTVVVDLDDQGERSFT-- 97
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLiegtdagdSSSASYETLLCWVLVDPLQRHGFCsr 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 98 --FMVRPsadLFLESADLPTfSAGEWLHVCSIALSA-----EPSRSATFEAMAAIREAGGYVSFDPNIR-PDLWPDENAL 169
Cdd:PLN02341 200 adFGPEP---AFSWISKLSA-EAKMAIRQSKALFCNgyvfdELSPSAIASAVDYAIDVGTAVFFDPGPRgKSLLVGTPDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 170 RRCLELALQSADVVKLSVEELAFLTG-NVEVNVGLHVLMARCPARLVLVTQGKEGVIAWHDGAVEHYPATPVECVDTTGA 248
Cdd:PLN02341 276 RRALEHLLRMSDVLLLTSEEAEALTGiRNPILAGQELLRPGIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGC 355
|
250 260 270
....*....|....*....|....*....|....*...
gi 1069055653 249 GDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGA 286
Cdd:PLN02341 356 GDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCGA 393
|
|
| PLN02967 |
PLN02967 |
kinase |
21-266 |
1.09e-19 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 88.95 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 21 RLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQGERSFTfMV 100
Cdd:PLN02967 237 KFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTT-CV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 101 RPSADLFLESADLPT--FSAGEWLHVCSIALSAEPSRSATFEAMAAIREAGGYVSFDPNIRPDLWPDENALRRCLELALQ 178
Cdd:PLN02967 316 KPCAEDSLSKSEINIdvLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWN 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 179 SADVVKLSVEELAFLTGnVE---------------VNVGLHVLMARCPARL--VLVTQGKEGVIAW---HDGAV---EHY 235
Cdd:PLN02967 396 LADIIEVTKQELEFLCG-IEpteefdtkdndkskfVHYSPEVVAPLWHENLkvLFVTNGTSKIHYYtkeHNGAVhgmEDA 474
|
250 260 270
....*....|....*....|....*....|.
gi 1069055653 236 PATPVECvDTTGAGDAFVAGLLYGLAAGQDL 266
Cdd:PLN02967 475 PITPFTS-DMSASGDGIVAGLMRMLTVQPHL 504
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
25-286 |
3.20e-19 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 85.70 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 25 CPGGAPANVAVGIARLGGQSAFIGRVGDDPfGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQgERSFTF---MVR 101
Cdd:TIGR03168 33 DAGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKESSGE-ETELNEpgpEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 102 PS-ADLFLE--SADLPtfsAGEWLhvcSIALSAEPSRSATF--EAMAAIREAGGYVSFDPnirpdlwpDENALRRCLELA 176
Cdd:TIGR03168 111 EEeLEQLLEklRELLA---SGDIV---VISGSLPPGVPPDFyaQLIAIARKKGAKVILDT--------SGEALREALAAK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 177 LqsaDVVKLSVEELAFLTG-NVEVNVGLhVLMARCP----ARLVLVTQGKEGVIAWHDGAVEHYPATPVECVDTTGAGDA 251
Cdd:TIGR03168 177 P---FLIKPNHEELEELFGrELKTLEEI-IEAARELldrgAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDS 252
|
250 260 270
....*....|....*....|....*....|....*
gi 1069055653 252 FVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGA 286
Cdd:TIGR03168 253 MVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGT 287
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-285 |
1.33e-18 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 83.63 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDL------LP----DGEGRLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKf 72
Cdd:cd01944 1 KVLVIGAAVVDIvldvdkLPasggDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 73 LRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADLFLESADLPTFSAGEWLHVCSIALSAE-PSRSATFEAMAAIrEAGGY 151
Cdd:cd01944 80 LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASEnASKVILLEWLEAL-PAGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 152 VSFDPNIRPDLWPDEnalrrCLELALQSADVVKLSVEELAFLTGNVEVNVGLHVLMARCPAR-LVLVTQGKEGviAW--- 227
Cdd:cd01944 159 LVFDPGPRISDIPDT-----ILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAaPVVVRLGSNG--AWirl 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1069055653 228 HDGAVEHYPATPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKG 285
Cdd:cd01944 232 PDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
1-296 |
1.50e-18 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 83.77 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 1 MKKIWVLGDAVVD------LLPD-GE---GRLLQC-PGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVD 69
Cdd:PRK11142 2 MGKLVVLGSINADhvlnleSFPRpGEtltGRHYQVaFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 70 VKFLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADLFLES--ADLPTFSAGEWLhvcsiaLSAEPSRSATFEAMAAI-R 146
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALveAHRELIANADAL------LMQLETPLETVLAAAKIaK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 147 EAGGYVSFDPNIRPDLwPDEnalrrclelALQSADVVKLSVEELAFLTGnVEVN------VGLHVLMARCPArLVLVTQG 220
Cdd:PRK11142 156 QHGTKVILNPAPAREL-PDE---------LLALVDIITPNETEAEKLTG-IRVEddddaaKAAQVLHQKGIE-TVLITLG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069055653 221 KEGVIAWHDGAVEHYPATPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGAMTALPWQHDL 296
Cdd:PRK11142 224 SRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEI 299
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
3-284 |
3.10e-18 |
|
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: 82.06 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDLLPDGEGRLLQcPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMakTLADERVDVKFLrldPAHRTS 82
Cdd:cd01937 1 KIVIIGHVTIDEIVTNGSGVVK-PGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWS--DLFDNGIEVISL---LSTETT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 83 TVVVDLDDQGeRSFTFMVRPSADLFLESADlpTFSAGEWLHVCSIALSAEPSrsatfeamaaIREAGGYVSFDPnirpdl 162
Cdd:cd01937 75 TFELNYTNEG-RTRTLLAKCAAIPDTESPL--STITAEIVILGPVPEEISPS----------LFRKFAFISLDA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 163 wpdENALRRC------LELALQSADVVKLSVEELAFLTGNVEVNVGLHVLmarcPARLVLVTQGKEGVIAWHDGAVEHYP 236
Cdd:cd01937 136 ---QGFLRRAnqekliKCVILKLHDVLKLSRVEAEVISTPTELARLIKET----GVKEIIVTDGEEGGYIFDGNGKYTIP 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1069055653 237 ATPVECVDTTGAGDAFVAGLLYGLAAGQDLtpviaLAQRCGALATTAK 284
Cdd:cd01937 209 ASKKDVVDPTGAGDVFLAAFLYSRLSGKDI-----KEAAEFAAAAAAK 251
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
26-280 |
1.59e-17 |
|
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: 81.07 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGApANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRlDPAHRTST---VVVD--------------L 88
Cdd:cd01172 39 LGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTTTktrVIARnqqllrvdreddspL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 89 DDQGERSFTFMVR---PSADLFLesadLPTFSAGewlhVCSIALSAEPSrsatfeamAAIREAGGYVSFDPNIRpdlwpD 165
Cdd:cd01172 117 SAEEEQRLIERIAerlPEADVVI----LSDYGKG----VLTPRVIEALI--------AAARELGIPVLVDPKGR-----D 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 166 ENALRRclelalqsADVVKLSVEELAFLTGNVEVNVGLHV-----LMARCPARLVLVTQGKEGVIAW-HDGAVEHYPATP 239
Cdd:cd01172 176 YSKYRG--------ATLLTPNEKEAREALGDEINDDDELEaagekLLELLNLEALLVTLGEEGMTLFeRDGEVQHIPALA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1069055653 240 VECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALA 280
Cdd:cd01172 248 KEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVV 288
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
26-285 |
4.96e-17 |
|
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: 79.11 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPANVAVGIARLGGQSAFIGRVGDDpFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQgersfTFM-VRPSA 104
Cdd:cd01164 35 AGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGT-----ETEiNEPGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 105 DL-------FLESADlPTFSAGEWLhvcSIALSAEPSRSATF--EAMAAIREAGGYVSFDPnirpdlwpDENALRRCLEL 175
Cdd:cd01164 109 EIseeeleaLLEKLK-ALLKKGDIV---VLSGSLPPGVPADFyaELVRLAREKGARVILDT--------SGEALLAALAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 176 AlqsADVVKLSVEELA-----FLTGNVEVNVGLHVLMARcPARLVLVTQGKEGVIAWHDGAVEHYPATPVECVDTTGAGD 250
Cdd:cd01164 177 K---PFLIKPNREELEelfgrPLGDEEDVIAAARKLIER-GAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGD 252
|
250 260 270
....*....|....*....|....*....|....*
gi 1069055653 251 AFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKG 285
Cdd:cd01164 253 SMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
24-296 |
5.98e-17 |
|
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: 79.17 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 24 QCPGGAPANVAVGIARLGGQSAFIGRVGDDPfGRFMAKTLADERVDVKFLRLDPAHRTSTVVVD-------LDDQGersf 96
Cdd:TIGR03828 32 IDAGGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVRVPGETRINVKIKEpsgtetkLNGPG---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 97 tFMVRPSA-DLFLE--SADLPtfsAGEWLhVCSIALSAEPSRSATFEAMAAIREAGGYVSFDPnirpdlwpDENALRRCL 173
Cdd:TIGR03828 107 -PEISEEElEALLEklRAQLA---EGDWL-VLSGSLPPGVPPDFYAELIALAREKGAKVILDT--------SGEALRDGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 174 ELAlqsADVVKLSVEELAFLTGNVEVNVGLHVLMAR----CPARLVLVTQGKEGVIAWHDGAVEHYPATPVECVDTTGAG 249
Cdd:TIGR03828 174 KAK---PFLIKPNDEELEELFGRELKTLEEIIEAARelldLGAENVLISLGADGALLVTKEGALFAQPPKGEVVSTVGAG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1069055653 250 DAFVAGLLYGLAAGQDLTPVIALAQRCGALATTAKGamTALPWQHDL 296
Cdd:TIGR03828 251 DSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDI 295
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
26-266 |
3.31e-15 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 74.75 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPAN---VAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRlDPAHRTSTVVVDLDDqGERSF------ 96
Cdd:PLN02548 51 AGGATQNsirVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVNVHYYE-DESTPTGTCAVLVVG-GERSLvanlsa 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 97 ------TFMVRPSADLFLESADLpTFSAGEWLHVC--SIALSAEPSR----------SATFEA---MAAIREAGGYVSFd 155
Cdd:PLN02548 129 ancykvEHLKKPENWALVEKAKF-YYIAGFFLTVSpeSIMLVAEHAAannktfmmnlSAPFICeffKDQLMEALPYVDF- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 156 pnirpdLWPDENALRRCLELALQSADvvklSVEELAFLTGNVEVNVGLHvlmarcpARLVLVTQGKEGVIAWHDGAVEHY 235
Cdd:PLN02548 207 ------LFGNETEARTFAKVQGWETE----DVEEIALKISALPKASGTH-------KRTVVITQGADPTVVAEDGKVKEF 269
|
250 260 270
....*....|....*....|....*....|....
gi 1069055653 236 PATPVE---CVDTTGAGDAFVAGLLYGLAAGQDL 266
Cdd:PLN02548 270 PVIPLPkekLVDTNGAGDAFVGGFLSQLVQGKDI 303
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
20-286 |
1.49e-14 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 73.30 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 20 GRLLQ----CP-----GGAPANVAVGIARLGGQS--------AFIGRVGDDPFGRFMAKTLadERVDVKFLRLD-PAHRT 81
Cdd:PLN02813 110 GKVLRaldgCSykasaGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKL--RRANVHFLSQPvKDGTT 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 82 STVVVDLDDQGERSFTFMVRPSADLFLESADLPTFSAGEWLHVCSIALSAEPSRSATFEAMAAIREAGGYVSF---DPNI 158
Cdd:PLN02813 188 GTVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASAISKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVtasDVSC 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 159 ----RPDLWpdenalrrclELALQSADVVKLSVEELAFLTGNVEVNVGLHV---LMARCParLVLVTQGKEGVIAWHDGA 231
Cdd:PLN02813 268 ierhRDDFW----------DVMGNYADILFANSDEARALCGLGSEESPESAtryLSHFCP--LVSVTDGARGSYIGVKGE 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1069055653 232 VEHYPATPVECVDTTGAGDAFVAGLLYGLAAG-QDLTPVIALAQRCGALATTAKGA 286
Cdd:PLN02813 336 AVYIPPSPCVPVDTCGAGDAYAAGILYGLLRGvSDLRGMGELAARVAATVVGQQGT 391
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-280 |
5.48e-14 |
|
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: 70.81 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 3 KIWVLGDAVVDL-------LPDGE---GRLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKF 72
Cdd:cd01941 1 EIVVIGAANIDLrgkvsgsLVPGTsnpGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 73 LrLDPAHRTSTVVVDLDDQGE-----------RSFTFMVRPSADLFLESADLPTF------SAGEWLhvcsIALSAEPSR 135
Cdd:cd01941 81 I-VFEGRSTASYTAILDKDGDlvvaladmdiyELLTPDFLRKIREALKEAKPIVVdanlpeEALEYL----LALAAKHGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 136 SATFEA-----MAAIREAGGYVSFdpnirpdLWPDENALRRCLELALQSADVVKLSVEELAFLtgnvevnvGLHVLMARC 210
Cdd:cd01941 156 PVAFEPtsapkLKKLFYLLHAIDL-------LTPNRAELEALAGALIENNEDENKAAKILLLP--------GIKNVIVTL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069055653 211 PARLVLVTQGKEGVIAWHdgavehYPA-TPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALA 280
Cdd:cd01941 221 GAKGVLLSSREGGVETKL------FPApQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
133-261 |
1.45e-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: 65.19 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 133 PSRSATFEAMAAIREAGGYVSFDPNIRPDLWPDENALRrclelALQSADVVKLSVEELAFLTG----NVEVNVGLHVLMA 208
Cdd:cd00287 68 PAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEK-----LLPGVDILTPNEEEAEALTGrrdlEVKEAAEAAALLL 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1069055653 209 RCPARLVLVTQGKEGVIAWH-DGAVEHYPATPVECVDTTGAGDAFVAGLLYGLA 261
Cdd:cd00287 143 SKGPKVVIVTLGEKGAIVATrGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
26-267 |
9.39e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 64.66 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 26 PGGAPANVAvgiaRLG--------GQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPA----------HRTSTVVVD 87
Cdd:PTZ00247 61 PGGSALNTA----RVAqwmlqapkGFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAptgtcavlvcGKERSLVAN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 88 LDDQGERSFTFMVRP-------SADLFLESADLPTFSAGEWLHVCSIAlsaepsrsatfeamaaiREAGGYVSFD---PN 157
Cdd:PTZ00247 137 LGAANHLSAEHMQSHavqeaikTAQLYYLEGFFLTVSPNNVLQVAKHA-----------------RESGKLFCLNlsaPF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 158 IRPDLWpDEnalrrcLELALQSADVVKLSVEELAFLTGNVEVNVG-LHVLMARCPA---------RLVLVTQGKEGVIAW 227
Cdd:PTZ00247 200 ISQFFF-ER------LLQVLPYVDILFGNEEEAKTFAKAMKWDTEdLKEIAARIAMlpkysgtrpRLVVFTQGPEPTLIA 272
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1069055653 228 HDGAVEHYPATPV---ECVDTTGAGDAFVAGLLYGLAAGQDLT 267
Cdd:PTZ00247 273 TKDGVTSVPVPPLdqeKIVDTNGAGDAFVGGFLAQYANGKDID 315
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
16-266 |
1.23e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 61.35 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 16 PDGEGRLLQCPGGAPANVAVGIAR-LGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHrTSTVVVDLDDQGER 94
Cdd:PLN02379 75 PDDLSPIKTMAGGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGP-TAQCVCLVDALGNR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 95 S----FTFMVRPSADLFLESadlpTFSAGEWLHVcsialsaepsRSATFEA---MAAIREA---GGYVSFD-------PN 157
Cdd:PLN02379 154 TmrpcLSSAVKLQADELTKE----DFKGSKWLVL----------RYGFYNLeviEAAIRLAkqeGLSVSLDlasfemvRN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 158 IRPDLwpdenalrrcLELaLQSADV--VKLSVEELAFLTG---NVEVNVGLHVLMARCpaRLVLVTQGKEGVIAWHDGAV 232
Cdd:PLN02379 220 FRSPL----------LQL-LESGKIdlCFANEDEARELLRgeqESDPEAALEFLAKYC--NWAVVTLGSKGCIARHGKEV 286
|
250 260 270
....*....|....*....|....*....|....*
gi 1069055653 233 EHYPAT-PVECVDTTGAGDAFVAGLLYGLAAGQDL 266
Cdd:PLN02379 287 VRVPAIgETNAVDATGAGDLFASGFLYGLIKGLSL 321
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
26-83 |
1.88e-08 |
|
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: 54.83 E-value: 1.88e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1069055653 26 PGGApANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLdPAHRTST 83
Cdd:PRK11316 50 PGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSV-PTHPTIT 105
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
215-280 |
7.86e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 46.72 E-value: 7.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069055653 215 VLVTQGKEGV-IAWHDGAVeHYPATPVECVDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALA 280
Cdd:PLN02630 206 VIVTNGKKGCrIYWKDGEM-RVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLA 271
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
215-280 |
9.38e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 46.23 E-value: 9.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069055653 215 VLVTQGKEGVIAWHDGAVEHypATPVEC--VDTTGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALA 280
Cdd:PRK09513 220 VVISLGAEGALWVNASGEWI--AKPPACdvVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALA 285
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
20-280 |
3.74e-05 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 44.59 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 20 GRLLQCPGGAPANVAVGIARLGGQSAFIGRVGDDPFGRFMAKTLADERVDVKFLRLDPAHRTSTVVVDLDDQGE-----R 94
Cdd:PRK09850 33 GKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEmlvaiN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 95 SFTFMVRPSADLFLESADlptFSAGEWLHVCSIALSAepsrsatfEAMAAIREAGGYVSfdpnirpdLWPDENALRRCLE 174
Cdd:PRK09850 113 DMNISNAITAEYLAQHRE---FIQRAKVIVADCNISE--------EALAWILDNAANVP--------VFVDPVSAWKCVK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 175 LALQSADV-----VKLSVEELA--FLTGNVEVNVGLHVLMARCPARLVLvTQGKEGVIaWHDGAVEHYPATPVE--CVDT 245
Cdd:PRK09850 174 VRDRLNQIhtlkpNRLEAETLSgiALSGREDVAKVAAWFHQHGLNRLVL-SMGGDGVY-YSDISGESGWSAPIKtnVINV 251
|
250 260 270
....*....|....*....|....*....|....*
gi 1069055653 246 TGAGDAFVAGLLYGLAAGQDLTPVIALAQRCGALA 280
Cdd:PRK09850 252 TGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMA 286
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
166-265 |
5.69e-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: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 166 ENALRRCLELAlQSADVVKLSvEELAFLTG--NVEVNVGLHVLMARCPArLVLVTQGKEGVIAWH-DGAVEHYPA-TPVE 241
Cdd:cd01939 167 EKPREELLELA-AYCDVVFVS-KDWAQSRGykSPEECLRGEGPRAKKAA-LLVCTWGDQGAGALGpDGEYVHSPAhKPIR 243
|
90 100
....*....|....*....|....
gi 1069055653 242 CVDTTGAGDAFVAGLLYGLAAGQD 265
Cdd:cd01939 244 VVDTLGAGDTFNAAVIYALNKGPD 267
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
177-276 |
6.72e-05 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 43.61 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069055653 177 LQSADVVKLSVEELAFLTGNVEVNVGLHVLMARCPaRLVLVTQGKEGVIAWHDGAVEHYPATPVECV-DTTGAGDAFvAG 255
Cdd:cd01946 161 LAKVDVVIINDGEARQLTGAANLVKAARLILAMGP-KALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDTF-AG 238
|
90 100
....*....|....*....|.
gi 1069055653 256 LLYGLAAGQDLTPVIALAQRC 276
Cdd:cd01946 239 GFIGYLASQKDTSEANMRRAI 259
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
220-280 |
1.43e-03 |
|
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: 39.63 E-value: 1.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069055653 220 GKEG--VIAWHDGAVEHYPA--TPVECV-DTTGAGDAFVAGLLYGLAAGQDLtpVIALAqrCGALA 280
Cdd:cd01943 233 GKLGcyVGSADSGPELWLPAyhTKSTKVvDPTGGGNSFLGGFAAGLALTKSI--DEACI--YGSVA 294
|
|
| |
