|
Name |
Accession |
Description |
Interval |
E-value |
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
54-382 |
5.79e-117 |
|
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: 342.67 E-value: 5.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 54 EGILMGFGNPLLDITCTVEDNViLEKYGLEANAAIIAdekHDALFDELMNMENVIYSAGGACQNSMRIFQWIVQtpfRAV 133
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAF-LEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAALGG---SAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 134 FIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEELPTGSCAVIIN-GPNRSLVANLGAASLFSDDWIDEDdnicALDRAEYF 212
Cdd:cd01168 74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTpDAERTMCTYLGAANELSPDDLDWS----LLAKAKYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 213 YFTGFFLAVCPPAVERVARMCCETNRIMILNFSAVFVLQMQKEALGNILQYVDIIICNKEEAIAFSDTNdwkTKNIFEIG 292
Cdd:cd01168 150 YLEGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEAE---TTDDLEAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 293 SRLQQMpkentRPRLVMITDAVCPVLVFQDndrVLEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIF 372
Cdd:cd01168 227 LKLLAL-----RCRIVVITQGAKGAVVVEG---GEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSY 298
|
330
....*....|
gi 28381281 373 ASQQVLHVVG 382
Cdd:cd01168 299 AAAEVIQQLG 308
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
61-392 |
8.59e-114 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 335.53 E-value: 8.59e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 61 GNPLLDITCTVEDNvILEKYGLEANAAIIADEKHDALFDELMNMENVIYSAGGACQNSMRIFQWIVQTPFRAVFIGSVGK 140
Cdd:PLN02548 2 GNPLLDISAVVDQD-FLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPGATSYMGCIGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 141 DKLGDRIEKRAKSDGLLTLYQLKEELPTGSCAVIINGPNRSLVANLGAASLFSDDWIDEDDNICALDRAEYFYFTGFFLA 220
Cdd:PLN02548 81 DKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVEHLKKPENWALVEKAKFYYIAGFFLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 221 VCPPAVERVARMCCETNRIMILNFSAVFVLQMQKEALGNILQYVDIIICNKEEAIAFSDTNDWKTKNIFEIGSRLQQMPK 300
Cdd:PLN02548 161 VSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISALPK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 301 EN-TRPRLVMITDAVCPVLVFQDNdRVLEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIFASQQVLH 379
Cdd:PLN02548 241 ASgTHKRTVVITQGADPTVVAEDG-KVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQ 319
|
330
....*....|...
gi 28381281 380 VVGVQIDKLPKFS 392
Cdd:PLN02548 320 RSGCTYPEKPDFS 332
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
50-392 |
2.65e-113 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 334.69 E-value: 2.65e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 50 MDLPEGILMGFGNPLLDITCTVEDNvILEKYGLEANAAIIADEKHDALFDELMNMENVIYSAGGACQNSMRIFQWIVQTP 129
Cdd:PTZ00247 1 TSSAPKKLLGFGNPLLDISAHVSDE-FLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 130 FRAV-FIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEELPTGSCAVIINGPNRSLVANLGAASLFSDDWIDEDDNICALDR 208
Cdd:PTZ00247 80 KGFVcYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAEHMQSHAVQEAIKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 209 AEYFYFTGFFLAVCPPAVERVARMCCETNRIMILNFSAVFVLQMQKEALGNILQYVDIIICNKEEAIAFSDTNDWKTKNI 288
Cdd:PTZ00247 160 AQLYYLEGFFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 289 FEIGSRLQQMPKEN-TRPRLVMITDAVCPVLVFQdNDRVLEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCI 367
Cdd:PTZ00247 240 KEIAARIAMLPKYSgTRPRLVVFTQGPEPTLIAT-KDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCV 318
|
330 340
....*....|....*....|....*
gi 28381281 368 RTGIFASQQVLHVVGVQIDKLPKFS 392
Cdd:PTZ00247 319 EAGHYSAQVIIQHNGCTYPEKPPFL 343
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
77-385 |
4.94e-43 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 152.11 E-value: 4.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 77 LEKYGLEANAAIIADEKHdalFDELMNMENVIYSAGGACQNSMRIFQWIVqtpFRAVFIGSVGKDKLGDRIEKRAKSDGL 156
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLG---GDVAFIGAVGDDNFGEFLLQELKKEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 157 LTLYQL-KEELPTGSCAVIINGP-NRSLVANLGAASLFsdDWIDEDDNICALDRAEYFYFTGFFLAVCPPAVERVARMCC 234
Cdd:pfam00294 76 DTDYVViDEDTRTGTALIEVDGDgERTIVFNRGAAADL--TPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 235 ETNRIMILNFSAVFvLQMqKEALGNILQYVDIIICNKEEAIAFSDtndwktKNIFEIGSRLQQMPKENT-RPRLVMITDA 313
Cdd:pfam00294 154 KNGGTFDPNLLDPL-GAA-REALLELLPLADLLKPNEEELEALTG------AKLDDIEEALAALHKLLAkGIKTVIVTLG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28381281 314 VCPVLVFQDNDrvlEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIFASQQVLHVVGVQI 385
Cdd:pfam00294 226 ADGALVVEGDG---EVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
131-370 |
2.88e-35 |
|
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: 131.55 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 131 RAVFIGSVGKDKLGDRIEKRAKSDGLLTLY-QLKEELPTGSCAVIINGP-NRSLVANLGAASLFSDDWIDEDdnicALDR 208
Cdd:COG0524 52 RVALVGAVGDDPFGDFLLAELRAEGVDTSGvRRDPGAPTGLAFILVDPDgERTIVFYRGANAELTPEDLDEA----LLAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 209 AEYFYFTGFFLA--VCPPAVERVARMCCETNRIMILNFSAVFVLQMQ-KEALGNILQYVDIIICNKEEAIAFSDTNDWKt 285
Cdd:COG0524 128 ADILHLGGITLAsePPREALLAALEAARAAGVPVSLDPNYRPALWEPaRELLRELLALVDILFPNEEEAELLTGETDPE- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 286 knifEIGSRLQQMPkentrPRLVMITDAVCPVLVFqDNDRVLEYPVPPVkqgEIFDTNGCGDAFVGGFLAMYVQRMPLDY 365
Cdd:COG0524 207 ----EAAAALLARG-----VKLVVVTLGAEGALLY-TGGEVVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEE 273
|
....*
gi 28381281 366 CIRTG 370
Cdd:COG0524 274 ALRFA 278
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
134-382 |
3.56e-22 |
|
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: 95.34 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 134 FIGSVGKDKLGDRIEKRAKSDGLLTLY-QLKEELPTGSCAVIINGPNRSLVANL---GAASLFSDDWIDEDdnicALDRA 209
Cdd:cd01166 50 LVTAVGDDPFGRFILAELRREGVDTSHvRVDPGRPTGLYFLEIGAGGERRVLYYragSAASRLTPEDLDEA----ALAGA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 210 EYFYFTGFFLAV---CPPAVERVARMCCETNRIMI--LNFSAVFVLQMQ-KEALGNILQYVDIIICNKEEAIAFSDTNDW 283
Cdd:cd01166 126 DHLHLSGITLALsesAREALLEALEAAKARGVTVSfdLNYRPKLWSAEEaREALEELLPYVDIVLPSEEEAEALLGDEDP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 284 KtknifEIGSRLQQMpkeNTRPRLVMITDAVCPVLVFQDNDRVL--EYPVPPVkqgeifDTNGCGDAFVGGFLAMYVQRM 361
Cdd:cd01166 206 T-----DAAERALAL---ALGVKAVVVKLGAEGALVYTGGGRVFvpAYPVEVV------DTTGAGDAFAAGFLAGLLEGW 271
|
250 260
....*....|....*....|.
gi 28381281 362 PLDYCIRTGIFASQQVLHVVG 382
Cdd:cd01166 272 DLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
131-374 |
8.51e-18 |
|
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: 82.98 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 131 RAVFIGSVGKDKLGDRIEKRAKSDGLLTLY-QLKEELPTGScAVII---NGPNRSLV---ANlgaASLFSDDWIDEDDNI 203
Cdd:cd01174 52 RVAMIGAVGDDAFGDELLENLREEGIDVSYvEVVVGAPTGT-AVITvdeSGENRIVVvpgAN---GELTPADVDAALELI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 204 CALDraeyfyftgffLAVC-----PPAVERVARMCCETNRIMILNFSAVfvlqmqKEALGNILQYVDIIICNKEEAIAFS 278
Cdd:cd01174 128 AAAD-----------VLLLqleipLETVLAALRAARRAGVTVILNPAPA------RPLPAELLALVDILVPNETEAALLT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 279 DTNDWKTKNIFEIGSRLQQMPKENtrprlVMITdavcpvL-----VFQDNDRVLEYPVPPVKqgeIFDTNGCGDAFVGGF 353
Cdd:cd01174 191 GIEVTDEEDAEKAARLLLAKGVKN-----VIVT------LgakgaLLASGGEVEHVPAFKVK---AVDTTGAGDTFIGAL 256
|
250 260
....*....|....*....|.
gi 28381281 354 LAMYVQRMPLDYCIRTGIFAS 374
Cdd:cd01174 257 AAALARGLSLEEAIRFANAAA 277
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
107-375 |
8.14e-15 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 74.27 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 107 VIYSAGGACQNsmrIFQWIVQTPFRAVFIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEELPTGSCaVIINGPNRSLV--- 183
Cdd:cd01941 30 VKQSPGGVGRN---IAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASY-TAILDKDGDLVval 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 184 ANLGAASLFSDDWIDEddNICALDRAEYFYFTGfflAVCPPAVERVARMCCETNRIMIlnFSAVFVLQMQKeaLGNILQY 263
Cdd:cd01941 106 ADMDIYELLTPDFLRK--IREALKEAKPIVVDA---NLPEEALEYLLALAAKHGVPVA--FEPTSAPKLKK--LFYLLHA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 264 VDIIICNKEEAIAF-----SDTNDWKTKNIFEIGSRLQQMPkentrprlvmITDAVCPVLVFQDNDRVLEYPVPPVKQGE 338
Cdd:cd01941 177 IDLLTPNRAELEALagaliENNEDENKAAKILLLPGIKNVI----------VTLGAKGVLLSSREGGVETKLFPAPQPET 246
|
250 260 270
....*....|....*....|....*....|....*..
gi 28381281 339 IFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIFASQ 375
Cdd:cd01941 247 VVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAA 283
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
131-370 |
2.96e-13 |
|
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: 69.65 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 131 RAVFIGSVGKDKLGDRIEKRAKSDGL-LTLYQLKEELPTGSCAVIINGPNRSLVA-NLGAASLFSDDWIDEDDNicaldR 208
Cdd:cd01942 52 SPGLVAAVGEDFHGRLYLEELREEGVdTSHVRVVDEDSTGVAFILTDGDDNQIAYfYPGAMDELEPNDEADPDG-----L 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 209 AEYFYFTGFflavcpPAVERVARMCcetnRIMILNFSavF-----VLQMQKEALGNILQYVDIIICNKEEAIAFSDtndw 283
Cdd:cd01942 127 ADIVHLSSG------PGLIELAREL----AAGGITVS--FdpgqeLPRLSGEELEEILERADILFVNDYEAELLKE---- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 284 KTknifeiGSRLqqmPKENTRPRLVMITDAVCPVLVFQDNDrvlEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPL 363
Cdd:cd01942 191 RT------GLSE---AELASGVRVVVVTLGPKGAIVFEDGE---EVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDL 258
|
....*..
gi 28381281 364 DYCIRTG 370
Cdd:cd01942 259 EESLRLG 265
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
131-360 |
5.56e-13 |
|
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: 68.82 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 131 RAVFIGSVGKDKLGDRIEKRAKSDGLLTLY-QLKEELPTGSCAVIINGP-NRSLVANLGAASlfsDDWIDEDDNICALDR 208
Cdd:cd01167 44 KAAFIGKVGDDEFGDFLLETLKEAGVDTRGiQFDPAAPTTLAFVTLDADgERSFEFYRGPAA---DLLLDTELNPDLLSE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 209 AEYFYFTGFFLAVcPPAVE------RVARMccetNRIMI---LNFSAVFVLQMQ--KEALGNILQYVDIIICNKEEAIAF 277
Cdd:cd01167 121 ADILHFGSIALAS-EPSRSallellEAAKK----AGVLIsfdPNLRPPLWRDEEeaRERIAELLELADIVKLSDEELELL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 278 SDTndwktKNIFEIGSRLQQMPkentrPRLVMITDAVCPVLVFqDNDRVLEYPVPPVKQGeifDTNGCGDAFVGGFLAMY 357
Cdd:cd01167 196 FGE-----EDPEEIAALLLLFG-----LKLVLVTRGADGALLY-TKGGVGEVPGIPVEVV---DTTGAGDAFVAGLLAQL 261
|
...
gi 28381281 358 VQR 360
Cdd:cd01167 262 LSR 264
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
219-355 |
6.52e-11 |
|
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: 61.34 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 219 LAVCPPAVERVARMCCETNRIMILNFSAVFVLQmQKEALGNILQYVDIIICNKEEAIAFSDTNDWKTKNIFEIGSRLQQM 298
Cdd:cd00287 66 LSPAPEAVLDALEEARRRGVPVVLDPGPRAVRL-DGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSK 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 28381281 299 pkentRPRLVMITDAVCPVLVFQDNDRVLEYPVPPVKQGeifDTNGCGDAFVGGFLA 355
Cdd:cd00287 145 -----GPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVV---DTTGAGDAFLAALAA 193
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
134-383 |
5.18e-08 |
|
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: 53.58 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 134 FIGSVGKDKLGDRIEKRAKSdGLLTLYQLKEELPTGSCAVIINGPNRSLVANLGAASLFSDDWideddniCALDRAEYFY 213
Cdd:cd01947 55 FFSNLGRDEIGIQSLEELES-GGDKHTVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKW-------PILDEGDGVF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 214 FTGFflavcppAVERVARMCCETNRIMILNFSavfvLQMQKEALGNILQYVDIIICNKEE-AIAFSDTNDWKTknifeig 292
Cdd:cd01947 127 ITAA-------AVDKEAIRKCRETKLVILQVT----PRVRVDELNQALIPLDILIGSRLDpGELVVAEKIAGP------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 293 srlqqmpkentRPRLVMITDAVCPVLVFQDNdrvlEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIF 372
Cdd:cd01947 189 -----------FPRYLIVTEGELGAILYPGG----RYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQ 253
|
250
....*....|.
gi 28381281 373 ASQQVLHVVGV 383
Cdd:cd01947 254 CGAICVSHFGP 264
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
57-384 |
1.41e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 53.27 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 57 LMGFGNPLLDITCTVEDNViLEKYGLEANAAIIADEKHDALFDELMNMENVIYSAGGACQNSM----RI-FQWIVQTPFR 131
Cdd:PLN02813 72 VLGLGQAMVDFSGMVDDEF-LERLGLEKGTRKVINHEERGKVLRALDGCSYKASAGGSLSNTLvalaRLgSQSAAGPALN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 132 AVFIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEELPTGSCAVIINgPN--RSLVANLGAASLfsddwIDEDDNICALDRA 209
Cdd:PLN02813 151 VAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTT-PDaqRTMLSYQGTSST-----VNYDSCLASAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 210 EYFYFTGFFLAVCPPAVERVARMCCETNR---IMILNFSAVFVLQMQKEALGNIL-QYVDIIICNKEEAIAFsdtndwkt 285
Cdd:PLN02813 225 SRVLVVEGYLWELPQTIEAIAQACEEAHRagaLVAVTASDVSCIERHRDDFWDVMgNYADILFANSDEARAL-------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 286 knifeIGSRLQQMPKENTRprlvmITDAVCPVLVFQDNDR--------VLEYpVPPVKQGEIfDTNGCGDAFVGGFLAMY 357
Cdd:PLN02813 297 -----CGLGSEESPESATR-----YLSHFCPLVSVTDGARgsyigvkgEAVY-IPPSPCVPV-DTCGAGDAYAAGILYGL 364
|
330 340
....*....|....*....|....*...
gi 28381281 358 VQRMPlDycIRT-GIFASQQVLHVVGVQ 384
Cdd:PLN02813 365 LRGVS-D--LRGmGELAARVAATVVGQQ 389
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
131-375 |
1.64e-06 |
|
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: 49.21 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 131 RAVFIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEELPTGSCAVIIN-GPNRSLVANLGAASLFSDDWIDEDDnicaLDRA 209
Cdd:cd01945 52 QARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDiTGDRATISITAIDTQAAPDSLPDAI----LGGA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 210 EYFYFTGfflaVCPPAVERVARMCCETNRIMILNFSAVFVLQMQKealgnILQYVDIIICNKEEAIAFSdtndwktknif 289
Cdd:cd01945 128 DAVLVDG----RQPEAALHLAQEARARGIPIPLDLDGGGLRVLEE-----LLPLADHAICSENFLRPNT----------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 290 eiGSRLQQMPKENTRP--RLVMITDAVCPVLVFQDNDRVLEYPVPPVkqgEIFDTNGCGDAFVGGFLAMYVQRMPLDYCI 367
Cdd:cd01945 188 --GSADDEALELLASLgiPFVAVTLGEAGCLWLERDGELFHVPAFPV---EVVDTTGAGDVFHGAFAHALAEGMPLREAL 262
|
....*...
gi 28381281 368 RtgiFASQ 375
Cdd:cd01945 263 R---FASA 267
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
131-377 |
1.84e-06 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 131 RAVFIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEE-LPTGsCAVII----NGPNrSLVANLGAASLFSDDWIDEDdnica 205
Cdd:PTZ00292 68 KVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTEnSSTG-LAMIFvdtkTGNN-EIVIIPGANNALTPQMVDAQ----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 206 ldRAEYFYFTGFFLA---VCPPAVERVARMCCETNRIMILNfSAVFVLQMQKEALGNILQYVDIIICNKEEA--IAFSDT 280
Cdd:PTZ00292 141 --TDNIQNICKYLICqneIPLETTLDALKEAKERGCYTVFN-PAPAPKLAEVEIIKPFLKYVSLFCVNEVEAalITGMEV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 281 NDwkTKNIFEIGSRLQQMPKENtrprlVMIT--DAVCpVLVFQDNDRVLEypvpPVKQGEIFDTNGCGDAFVGGFLAMYV 358
Cdd:PTZ00292 218 TD--TESAFKASKELQQLGVEN-----VIITlgANGC-LIVEKENEPVHV----PGKRVKAVDTTGAGDCFVGSMAYFMS 285
|
250 260
....*....|....*....|
gi 28381281 359 QRMPL-DYCIRTGIFASQQV 377
Cdd:PTZ00292 286 RGKDLkESCKRANRIAAISV 305
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
218-354 |
6.63e-06 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 47.46 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 218 FLAVCPPAVERVARMCCETNRIMILNfSAVFVLQMQKEALGNILQYVDIIICNKEEAIAFS-DTNDWKT-KNIFEIGsrl 295
Cdd:cd01946 119 FLGNIAPELQREVLEQVKDPKLVVMD-TMNFWISIKPEKLKKVLAKVDVVIINDGEARQLTgAANLVKAaRLILAMG--- 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 28381281 296 qqmpkentrPRLVMITDAVCPVLVFQDnDRVLEYPVPPVKqgEIFDTNGCGDAFVGGFL 354
Cdd:cd01946 195 ---------PKALIIKRGEYGALLFTD-DGYFAAPAYPLE--SVFDPTGAGDTFAGGFI 241
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
319-371 |
8.86e-05 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 43.97 E-value: 8.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 28381281 319 VFQDNDRVLEYPVPPVKQGeifDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGI 371
Cdd:COG1105 227 LLVTEDGVYRAKPPKVEVV---STVGAGDSMVAGFLAGLARGLDLEEALRLAV 276
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
322-382 |
3.57e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.03 E-value: 3.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28381281 322 DNDRVLEYPVPPVkqgEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIFASQQVLHVVG 382
Cdd:PRK09813 201 DGAQFWRQAPEPV---TVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
322-380 |
2.16e-03 |
|
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: 39.64 E-value: 2.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28381281 322 DNDRVLEYPVPPVkqgEIFDTNGCGDAFVGGFLAMYVQ-RMPLDYCIRTG-IFASQQVLHV 380
Cdd:cd01940 204 DGAVFYSVAPRPV---EVVDTLGAGDSFIAGFLLSLLAgGTAIAEAMRQGaQFAAKTCGHE 261
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
305-355 |
2.18e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 39.53 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 28381281 305 PRLVMITDAVCPVLVFqDNDRVLEYPVPPVKqgeIFDTNGCGDAFVGGFLA 355
Cdd:PRK09434 213 IALLLVTLGAEGVLVH-TRGQVQHFPAPSVD---PVDTTGAGDAFVAGLLA 259
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
248-371 |
6.81e-03 |
|
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: 37.90 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28381281 248 FVLQMQKEALGNILQY-VDIIICNKEEAIAFSDTNDWKTKNIFEIGSRLQQMPKENtrprlVMITDAVCPVLVFqDNDRV 326
Cdd:cd01164 161 VILDTSGEALLAALAAkPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAEN-----VLVSLGADGALLV-TKDGV 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 28381281 327 LEYPVPPVKQGeifDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGI 371
Cdd:cd01164 235 YRASPPKVKVV---STVGAGDSMVAGFVAGLAQGLSLEEALRLAV 276
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
331-370 |
8.12e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 38.23 E-value: 8.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 28381281 331 VPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTG 370
Cdd:PLN02379 289 VPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVG 328
|
|
| |
