|
Name |
Accession |
Description |
Interval |
E-value |
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
23-319 |
2.05e-142 |
|
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: 403.52 E-value: 2.05e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 183 MADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKA 262
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397419 263 VDTTGAGDSFVGALAFYLAYYPnlSLEEMLKRSNFIAAVSVQATGTQSSYPYKKDLP 319
Cdd:TIGR02152 239 VDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
23-314 |
1.59e-128 |
|
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: 368.42 E-value: 1.59e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01174 6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:cd01174 86 VGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVILNPAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 183 MADLDPqFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSqaEPVPKHIPTEAVKA 262
Cdd:cd01174 166 RPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS--GGEVEHVPAFKVKA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 23397419 263 VDTTGAGDSFVGALAFYLAYYPnlSLEEMLKRSNFIAAVSVQATGTQSSYPY 314
Cdd:cd01174 243 VDTTGAGDTFIGALAAALARGL--SLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
23-319 |
1.74e-111 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 326.69 E-value: 1.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:PTZ00292 22 GSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 RDAATGTASIIVNNE-GQNIIVIVAGANLFLNSEDLKKAASVI-SRAKVMICQLEISPAASLEALTMARRSGVKTLFNPA 180
Cdd:PTZ00292 102 ENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGCYTVFNPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 181 PAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQaEPVPKHIP 256
Cdd:PTZ00292 182 PAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEK-ENEPVHVP 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397419 257 TEAVKAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQATGTQSSYPYKKDLP 319
Cdd:PTZ00292 261 GKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISVTRHGTQSSYPHPSELP 321
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
23-318 |
6.83e-81 |
|
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: 247.49 E-value: 6.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:COG0524 6 GEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSGVRRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAAsvISRAKVMICQL-----EISPAASLEALTMARRSGVKTLF 177
Cdd:COG0524 86 PGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAGVPVSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 178 NPA------PAMADLDPQFYTLSSIFCCNESEAEILTGHavsdpTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPV 251
Cdd:COG0524 164 DPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397419 252 pkHIPTEAVKAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQATGTQSSYPYKKDL 318
Cdd:COG0524 239 --HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
36-319 |
5.57e-76 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 235.15 E-value: 5.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 36 LPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVN 115
Cdd:PRK11142 22 FPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 116 NEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEiSPAAS-LEALTMARRSGVKTLFNPAPAMAdLDPQFYTLS 194
Cdd:PRK11142 102 DEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLE-TPLETvLAAAKIAKQHGTKVILNPAPARE-LPDELLALV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 195 SIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGcVILSQAEPvPKHIPTEAVKAVDTTGAGDSFVG 274
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRG-VWLSENGE-GQRVPGFRVQAVDTIAAGDTFNG 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 23397419 275 ALAfyLAYYPNLSLEEMLKRSNFIAAVSVQATGTQSSYPYKKDLP 319
Cdd:PRK11142 258 ALV--TALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEID 300
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
23-310 |
7.65e-63 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 201.03 E-value: 7.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPktGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:pfam00294 6 GEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVM----ICQLEiSPAASLEALTMARRSGVKT--- 175
Cdd:pfam00294 84 EDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLG-LPEATLEELIEAAKNGGTFdpn 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 176 LFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHI 255
Cdd:pfam00294 163 LLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV-HVP 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397419 256 PTEAVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEEMLKRSNFIAAVSVQATGTQS 310
Cdd:pfam00294 242 AVPKVKVVDTTGAGDSFVGGfLAGLLA---GKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
23-307 |
1.54e-36 |
|
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: 132.70 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVsltsrlPKTGETIHGHEFF-IGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQ 101
Cdd:cd01166 6 GEVMVDLS------PPGGGRLEQADSFrKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 102 TRDAATGTASIIV--NNEGQNIIVIVAGANLFLNSEDLKKAAsvISRAK-VMICqlEISPAAS-------LEALTMARRS 171
Cdd:cd01166 80 DPGRPTGLYFLEIgaGGERRVLYYRAGSAASRLTPEDLDEAA--LAGADhLHLS--GITLALSesarealLEALEAAKAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 172 GVKTLF--NPAPAMADLD------PQFYTLSSIFCCNESEAEILTGHAvSDPTTAGKAAMilLERGCQVVVITLGASGCV 243
Cdd:cd01166 156 GVTVSFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDE-DPTDAAERALA--LALGVKAVVVKLGAEGAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397419 244 ILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEEMLKRSNFIAAVSVQATG 307
Cdd:cd01166 233 VYTGGGRV--FVPAYPVEVVDTTGAGDAFAAGfLAGLLE---GWDLEEALRFANAAAALVVTRPG 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
53-308 |
4.74e-36 |
|
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: 131.97 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTrDAATGTASIIVNNEGQNIIVIVAGANLFL 132
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQP-DGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 133 NSEDLKKAAsvISRAKVMIC---QLEISPAASLEALTMARRSGVKTLFN-PAPAMAD-----LDPQFYTLSSIFcCNESE 203
Cdd:cd01168 134 SPDDLDWSL--LAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlSAPFIVQrfkeaLLELLPYVDILF-GNEEE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 204 AEILTGHAVSDPTTAGKAamiLLERGCQVVVITLGASGCVILSQAE--PVPkhiPTEAVKAVDTTGAGDSFVGalAFYLA 281
Cdd:cd01168 211 AEALAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVEGGEvyPVP---AIPVEKIVDTNGAGDAFAG--GFLYG 282
|
250 260
....*....|....*....|....*..
gi 23397419 282 YYPNLSLEEMLKRSNFIAAVSVQATGT 308
Cdd:cd01168 283 LVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
53-307 |
2.13e-34 |
|
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: 127.37 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAG--ANL 130
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGpaADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 131 FLNSEDLKkaaSVISRAK-VMICQL----EISPAASLEALTMARRSGVKTLF----------NPAPAMADLdPQFYTLSS 195
Cdd:cd01167 108 LLDTELNP---DLLSEADiLHFGSIalasEPSRSALLELLEAAKKAGVLISFdpnlrpplwrDEEEARERI-AELLELAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 196 IFCCNESEAEILTGHavSDPTtagKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGA 275
Cdd:cd01167 184 IVKLSDEELELLFGE--EDPE---EIAALLLLFGLKLVLVTRGADGALLYTKGGVG--EVPGIPVEVVDTTGAGDAFVAG 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 23397419 276 LAFYLAYYPNLS-----LEEMLKRSNFIAAVSVQATG 307
Cdd:cd01167 257 LLAQLLSRGLLAldedeLAEALRFANAVGALTCTKAG 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
23-309 |
2.72e-34 |
|
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: 126.66 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01942 6 GHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLnseDLKKAASVISRAKVmicqLEISPAASLEALTMARRSGVKTL-FNPAP 181
Cdd:cd01942 86 DEDSTGVAFILTDGDDNQIAYFYPGAMDEL---EPNDEADPDGLADI----VHLSSGPGLIELARELAAGGITVsFDPGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 182 AMADLD----PQFYTLSSIFCCNESEAEIL---TGhaVSDPTTAgkaamilleRGCQVVVITLGASGCVILSQAEPVpKH 254
Cdd:cd01942 159 ELPRLSgeelEEILERADILFVNDYEAELLkerTG--LSEAELA---------SGVRVVVVTLGPKGAIVFEDGEEV-EV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 23397419 255 IPTEAVKAVDTTGAGDSFvgALAFYLAYYPNLSLEEMLKRSNFIAAVSVQATGTQ 309
Cdd:cd01942 227 PAVPAVKVVDTTGAGDAF--RAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
23-314 |
7.87e-31 |
|
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: 117.39 E-value: 7.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01945 6 GLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 RDAATGTASIIVNNEGQNIIVIVAG----ANLFLNSEDLKKAASVI--SRAkvmicqleisPAASLEALTMARRSGVktl 176
Cdd:cd01945 86 PGARSPISSITDITGDRATISITAIdtqaAPDSLPDAILGGADAVLvdGRQ----------PEAALHLAQEARARGI--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 177 fnpaPAMADLDPQF-------YTLSSIFCCNESEAEILTGhaVSDPttagKAAMILLERGCQVVVITLGASGCVILSQAE 249
Cdd:cd01945 153 ----PIPLDLDGGGlrvleelLPLADHAICSENFLRPNTG--SADD----EALELLASLGIPFVAVTLGEAGCLWLERDG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397419 250 PVpKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPNLSLEEMLKRSNFIAAVSVQATGTQSSYPY 314
Cdd:cd01945 223 EL-FHVPAFPVEVVDTTGAGDVFHGAFAHALA--EGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
53-308 |
1.29e-25 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 104.12 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGkGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATgTASIIVNNEGQNIIVIVAGANLFL 132
Cdd:COG2870 56 GG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPT-TTKTRVIAGGQQLLRLDFEDRFPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 133 NSED----LKKAASVISRAKVMIcqLE------ISPAASLEALTMARRSGVKTLFNPAPAmadlDPQFYTLSSIFCCNES 202
Cdd:COG2870 134 SAELearlLAALEAALPEVDAVI--LSdygkgvLTPELIQALIALARAAGKPVLVDPKGR----DFSRYRGATLLTPNLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 203 EAEILTGHAVSDPTTAGKAAMILLER-GCQVVVITLGASGCVILSQAEPvPKHIPTEAVKAVDTTGAGDSFVGALAFYLA 281
Cdd:COG2870 208 EAEAAVGIPIADEEELVAAAAELLERlGLEALLVTRGEEGMTLFDADGP-PHHLPAQAREVFDVTGAGDTVIATLALALA 286
|
250 260
....*....|....*....|....*..
gi 23397419 282 YypNLSLEEMLKRSNFIAAVSVQATGT 308
Cdd:COG2870 287 A--GASLEEAAELANLAAGIVVGKLGT 311
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
52-304 |
2.96e-25 |
|
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: 102.39 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 52 FGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQ---NHISTEFtyqtRDAATGTASIIVNNEGqNIIVIVAGA 128
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKaglNVRGIVF----EGRSTASYTAILDKDG-DLVVALADM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 129 NLF--LNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPA-----PAMADLDPQFYTLSsifcCNE 201
Cdd:cd01941 109 DIYelLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAFEPTsapklKKLFYLLHAIDLLT----PNR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 202 SEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPV-PKHIPTEAV-KAVDTTGAGDSFVGALAFY 279
Cdd:cd01941 185 AELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVeTKLFPAPQPeTVVNVTGAGDAFVAGLVAG 264
|
250 260
....*....|....*....|....*
gi 23397419 280 LAYypNLSLEEMLKRSNFIAAVSVQ 304
Cdd:cd01941 265 LLE--GMSLDDSLRFAQAAAALTLE 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
54-313 |
2.33e-24 |
|
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: 100.33 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 54 GKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEF-TYQTRDAATGTAsiivnnegqniiVIVAGANLF- 131
Cdd:cd01172 40 GGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGiVDEGRPTTTKTR------------VIARNQQLLr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 132 LNSED------------LKKAASVISRAKVMIcqLE------ISPAASLEALTMARRSGVKTLFNPAPamadLDPQFYTL 193
Cdd:cd01172 108 VDREDdsplsaeeeqrlIERIAERLPEADVVI--LSdygkgvLTPRVIEALIAAARELGIPVLVDPKG----RDYSKYRG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 194 SSIFCCNESEAEILTGHAVSDPTTAGKAAMILLER-GCQVVVITLGASGCVILSQAEPvPKHIPTEAVKAVDTTGAGDSF 272
Cdd:cd01172 182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGE-VQHIPALAKEVYDVTGAGDTV 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 23397419 273 VGALAFYLAyyPNLSLEEMLKRSNFIAAVSVQATGTQSSYP 313
Cdd:cd01172 261 IATLALALA--AGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
53-318 |
9.60e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 95.77 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQtrDAATGTASIIV--NNEGQN--IIVIVAGA 128
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRL--DPAHRTSTVVVdlDDQGERsfTFMVRPSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 129 NLFLNSEDLK--KAASVISRAKVMICQlEISPAASLEALTMARRSGVKTLFNP---------APAMADLDPQFYTLSSIF 197
Cdd:PRK09434 106 DLFLQPQDLPpfRQGEWLHLCSIALSA-EPSRSTTFEAMRRIKAAGGFVSFDPnlredlwqdEAELRECLRQALALADVV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 198 CCNESEAEILTGhavSDPTTAGKAAmILLERGCQVVVITLGASGCVILSQAEPvpKHIPTEAVKAVDTTGAGDSFVGALA 277
Cdd:PRK09434 185 KLSEEELCFLSG---TSQLEDAIYA-LADRYPIALLLVTLGAEGVLVHTRGQV--QHFPAPSVDPVDTTGAGDAFVAGLL 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 23397419 278 FYLAYYPNLS----LEEMLKRSNFIAAVSVQATGTQSSYPYKKDL 318
Cdd:PRK09434 259 AGLSQAGLWTdeaeLAEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
23-281 |
1.37e-20 |
|
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: 87.54 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVckvgndsfgndyienlkqnhisteftyqt 102
Cdd:cd00287 6 GSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLV----------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 rdaatgTASIIVNNEGQniivivaganlflnsedlkkaasvisrakvmicqleISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:cd00287 57 ------GADAVVISGLS------------------------------------PAPEAVLDALEEARRRGVPVVLDPGPR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 183 MADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHIPTE 258
Cdd:cd00287 95 AVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTE-VHVPAF 173
|
250 260
....*....|....*....|...
gi 23397419 259 AVKAVDTTGAGDSFVGALAFYLA 281
Cdd:cd00287 174 PVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
53-317 |
9.06e-19 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 85.44 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIV--AGANL 130
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSADM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 131 FLNSEDLKKaaSVISRAKV-------MICqlEISPAASLEALTMARRSGVKTLFNP---------APAMADLDPQFYTLS 194
Cdd:PLN02323 123 LLRESELDL--DLIRKAKIfhygsisLIT--EPCRSAHLAAMKIAKEAGALLSYDPnlrlplwpsAEAAREGIMSIWDEA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 195 SIFCCNESEAEILTGhavSDPTTaGKAAMILLERGCQVVVITLGASGCVILSQAepVPKHIPTEAVKAVDTTGAGDSFVG 274
Cdd:PLN02323 199 DIIKVSDEEVEFLTG---GDDPD-DDTVVKLWHPNLKLLLVTEGEEGCRYYTKD--FKGRVEGFKVKAVDTTGAGDAFVG 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 23397419 275 ALAFYLAYYPNL-----SLEEMLKRSNFIAAVSVQATGTQSSYPYKKD 317
Cdd:PLN02323 273 GLLSQLAKDLSLledeeRLREALRFANACGAITTTERGAIPALPTKEA 320
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
23-307 |
2.54e-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: 83.24 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGkGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHIstEFTYQT 102
Cdd:cd01944 6 GAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGI--EILLPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 103 R-DAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKkAASVISRAKVMICQLEI-SPAASLEALT---MARRSGVKTLF 177
Cdd:cd01944 83 RgGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFA-TLTVAPYDYVYLSGYTLaSENASKVILLewlEALPAGTTLVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 178 NPAPAMADLDPQFYT----LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGcqvVVITLGASGCVILSQAEPvPK 253
Cdd:cd01944 162 DPGPRISDIPDTILQalmaKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAP---VVVRLGSNGAWIRLPDGN-TH 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397419 254 HIPTEAVKAVDTTGAGDSFVGALAFYLAyyPNLSLEEMLKRSNFIAAVSVQATG 307
Cdd:cd01944 238 IIPGFKVKAVDTIGAGDTHAGGMLAGLA--KGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
54-307 |
3.58e-18 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 84.88 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 54 GKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTeftyqTRDAATGTASIIVNNEGQNIIVIV----AGAN 129
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV-----VGLIEGTDAGDSSSASYETLLCWVlvdpLQRH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 130 LFLNSEDLKK-------------AASVISRAKVMICQ----LEISPAASLEALTMARRSGVKTLFNPAP---AMADLDP- 188
Cdd:PLN02341 195 GFCSRADFGPepafswisklsaeAKMAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgkSLLVGTPd 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 189 ------QFYTLSSIFCCNESEAEILTGhaVSDPTTAGKAamiLLERGC--QVVVITLGASGCVILSQAEPVPKhiPTEAV 260
Cdd:PLN02341 275 erraleHLLRMSDVLLLTSEEAEALTG--IRNPILAGQE---LLRPGIrtKWVVVKMGSKGSILVTRSSVSCA--PAFKV 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 23397419 261 KAVDTTGAGDSFVGALAFylAYYPNLSLEEMLKRSNFIAAVSvqATG 307
Cdd:PLN02341 348 NVVDTVGCGDSFAAAIAL--GYIHNLPLVNTLTLANAVGAAT--AMG 390
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
28-304 |
1.02e-17 |
|
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: 81.31 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 28 DLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHIstEFTYQTRDAAT 107
Cdd:cd01947 11 DIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KHTVAWRDKPT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 108 GTASIIVNNEGQNIIVIVAGanlflNSEDLKKAASVISRAKVMIcqleISPAASLEALTMARRSGVKTLFNPAPAMADLD 187
Cdd:cd01947 89 RKTLSFIDPNGERTITVPGE-----RLEDDLKWPILDEGDGVFI----TAAAVDKEAIRKCRETKLVILQVTPRVRVDEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 188 PQFYTLSSIFCCNESEAEILtghavsdpTTAGKAAMilleRGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKAVDTTG 267
Cdd:cd01947 160 NQALIPLDILIGSRLDPGEL--------VVAEKIAG----PFPRYLIVTEGELGAILYPGGR--YNHVPAKKAKVPDSTG 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 23397419 268 AGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQ 304
Cdd:cd01947 226 AGDSFAAGFIYGLLK--GWSIEEALELGAQCGAICVS 260
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
200-309 |
1.81e-17 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 81.33 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 200 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAfy 279
Cdd:COG1105 184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVSTVGAGDSMVAGFL-- 259
|
90 100 110
....*....|....*....|....*....|
gi 23397419 280 LAYYPNLSLEEMLKRSNFIAAVSVQATGTQ 309
Cdd:COG1105 260 AGLARGLDLEEALRLAVAAGAAAALSPGTG 289
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
200-309 |
1.37e-14 |
|
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: 72.56 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 200 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAfy 279
Cdd:cd01164 184 NREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVY--RASPPKVKVVSTVGAGDSMVAGFV-- 259
|
90 100 110
....*....|....*....|....*....|
gi 23397419 280 LAYYPNLSLEEMLKRSNFIAAVSVQATGTQ 309
Cdd:cd01164 260 AGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
53-318 |
1.80e-14 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 73.14 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQC-VQAARLGAKAAIVCKVG---NDSFGNDYIENLKQNHISTEFTYqTRDAATGT-ASIIVNNEGQNIIVIVAG 127
Cdd:PTZ00247 62 GGSALNTArVAQWMLQAPKGFVCYVGcvgDDRFAEILKEAAEKDGVEMLFEY-TTKAPTGTcAVLVCGKERSLVANLGAA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 128 ANL---FLNSEDLKKAasvISRAKVMICQ---LEISPAASLEALTMARRSGVKTLFN-PAP-AMADLDPQFYTL---SSI 196
Cdd:PTZ00247 141 NHLsaeHMQSHAVQEA---IKTAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFFFERLLQVlpyVDI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 197 FCCNESEAEILtGHAVSDPTT-----AGKAAMILLERGCQ--VVVITLGASGCVILSQAE----PVPkhiPTEAVKAVDT 265
Cdd:PTZ00247 218 LFGNEEEAKTF-AKAMKWDTEdlkeiAARIAMLPKYSGTRprLVVFTQGPEPTLIATKDGvtsvPVP---PLDQEKIVDT 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397419 266 TGAGDSFVGAlafYLAYYPN-LSLEEMLKRSNFIAAVSVQATGtqSSYPYKKDL 318
Cdd:PTZ00247 294 NGAGDAFVGG---FLAQYANgKDIDRCVEAGHYSAQVIIQHNG--CTYPEKPPF 342
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
53-281 |
9.71e-12 |
|
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: 64.30 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTyQTRDAATGTASIIVNNeGQNIIV-----IVAG 127
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVD-GDRIFGlsnkgGVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 128 ANLFlnSEDLKKaasvISRAKVMICQLEISPAASLEALTMARRSGVKTLF----NPAPAMADLDPQFYTLSSIFCCNESE 203
Cdd:cd01940 100 EHPF--EADLEY----LSQFDLVHTGIYSHEGHLEKALQALVGAGALISFdfsdRWDDDYLQLVCPYVDFAFFSASDLSD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397419 204 AEIltghavsdpttaGKAAMILLERGCQVVVITLGASGCVILSQAEPVPKHIptEAVKAVDTTGAGDSFVGALAFYLA 281
Cdd:cd01940 174 EEV------------KAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAP--RPVEVVDTLGAGDSFIAGFLLSLL 237
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
67-318 |
9.34e-11 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 62.04 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 67 GAKAAIVCkVGNDSFGNDYIENLKQNHISTEFtYQTRDAATGTASIIVNNEGQNIIVIVAGANLFlNSEDLKKAAS--VI 144
Cdd:PLN02548 70 GATSYMGC-IGKDKFGEEMKKCATAAGVNVHY-YEDESTPTGTCAVLVVGGERSLVANLSAANCY-KVEHLKKPENwaLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 145 SRAKVMICQ---LEISPAASLEALTMARRSGVKTLFN-PAPAMADL--DPQFYTL---SSIFCcNESEAEILT---GHAV 212
Cdd:PLN02548 147 EKAKFYYIAgffLTVSPESIMLVAEHAAANNKTFMMNlSAPFICEFfkDQLMEALpyvDFLFG-NETEARTFAkvqGWET 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 213 SD-PTTAGKAAMILLERGCQ--VVVITLGAsGCVILSQAEPVPKH--IPTEAVKAVDTTGAGDSFVGalAFYLAYYPNLS 287
Cdd:PLN02548 226 EDvEEIALKISALPKASGTHkrTVVITQGA-DPTVVAEDGKVKEFpvIPLPKEKLVDTNGAGDAFVG--GFLSQLVQGKD 302
|
250 260 270
....*....|....*....|....*....|.
gi 23397419 288 LEEMLKRSNFIAAVSVQATGTqsSYPYKKDL 318
Cdd:PLN02548 303 IEECVRAGNYAANVIIQRSGC--TYPEKPDF 331
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
63-293 |
2.83e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 60.57 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 63 AARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEfTYQTRDAATGTASIIVNNEGQ--------NIIVIVAGAnlfLNS 134
Cdd:PLN02379 97 SAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLS-RLRAKKGPTAQCVCLVDALGNrtmrpclsSAVKLQADE---LTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 135 EDLKKAASVISR----------AKVMICQLE-ISPAASLEALTMAR--RSGVKTLFNPApamaDLDPQFytlssifcCNE 201
Cdd:PLN02379 173 EDFKGSKWLVLRygfynlevieAAIRLAKQEgLSVSLDLASFEMVRnfRSPLLQLLESG----KIDLCF--------ANE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 202 SEA-EILTGHAVSDPttagKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIP-TEAVKAVDTTGAGDSFVGalAFY 279
Cdd:PLN02379 241 DEArELLRGEQESDP----EAALEFLAKYCNWAVVTLGSKGCIARHGKEVV--RVPaIGETNAVDATGAGDLFAS--GFL 312
|
250
....*....|....
gi 23397419 280 LAYYPNLSLEEMLK 293
Cdd:PLN02379 313 YGLIKGLSLEECCK 326
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
53-277 |
4.15e-10 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 60.00 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIV-AGANLF 131
Cdd:PRK09850 40 GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 132 LNSEDLKKAASVISRAKVMICQLEISPAASLEALTMArrSGVKTLFNPAPA-----MADLDPQFYTLSSifccNESEAEI 206
Cdd:PRK09850 120 ITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNA--ANVPVFVDPVSAwkcvkVRDRLNQIHTLKP----NRLEAET 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397419 207 LTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGcVILSQAEPVPKHIPTEAVKAVDTTGAGDSFVGALA 277
Cdd:PRK09850 194 LSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDG-VYYSDISGESGWSAPIKTNVINVTGAGDAMMAGLA 263
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
41-309 |
1.23e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 59.05 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 41 ETIHGHEFFIGFGGKGANQCVQAARLGAKA--------AIVCKVGNDSFGNDYIENLKQNHIstEFTYQ-TRDAATGTAS 111
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANV--HFLSQpVKDGTTGTVI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 112 IIVNNEGQNIIVIVAGANLFLN-SEDLkkaASVISRAKVMICQ-----LEISPAASLEALTMARRSGVKTlfnpapAMAD 185
Cdd:PLN02813 192 VLTTPDAQRTMLSYQGTSSTVNyDSCL---ASAISKSRVLVVEgylweLPQTIEAIAQACEEAHRAGALV------AVTA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 186 LDP--------QFYTL----SSIFCCNESEAEILTGHAVSDpttAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpk 253
Cdd:PLN02813 263 SDVscierhrdDFWDVmgnyADILFANSDEARALCGLGSEE---SPESATRYLSHFCPLVSVTDGARGSYIGVKGEAV-- 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397419 254 HIPTEAVKAVDTTGAGDSFV-GALAFYLAYYPNL-SLEEMLKRsnfIAAVSVQATGTQ 309
Cdd:PLN02813 338 YIPPSPCVPVDTCGAGDAYAaGILYGLLRGVSDLrGMGELAAR---VAATVVGQQGTR 392
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
196-291 |
1.97e-09 |
|
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: 57.48 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 196 IFCCNESEAEILTGHAvsdptTAGKAAMILLERGCQVVVITLGASGCVILSQ----AEPVpkhIPTEAVkaVDTTGAGDS 271
Cdd:cd01946 166 VVIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDdgyfAAPA---YPLESV--FDPTGAGDT 235
|
90 100
....*....|....*....|
gi 23397419 272 FVGALAFYLAYYPNLSLEEM 291
Cdd:cd01946 236 FAGGFIGYLASQKDTSEANM 255
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
53-293 |
3.64e-09 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 57.10 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNdSFGNDYIENLKQNHISTEfTYQTRDAATGTASIIVNNEGQNIIVIVAGANLfl 132
Cdd:PRK10294 38 GGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVA-TVEAKDWTRQNLHVHVEASGEQYRFVMPGAAL-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 133 nSED----LKKAASVISRAKVMICQLEISPAASLEALTM----ARRSGVKTLFNPA--PAMADLDPQFYTLSSIfccNES 202
Cdd:PRK10294 114 -NEDefrqLEEQVLEIESGAILVISGSLPPGVKLEKLTQlisaAQKQGIRCIIDSSgdALSAALAIGNIELVKP---NQK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 203 EAEILTGHAVSDPTTAGKAAMILLERG-CQVVVITLGASGCVILS-----QAEPVPkhipteaVKAVDTTGAGDSFVGAL 276
Cdd:PRK10294 190 ELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDsenciQVVPPP-------VKSQSTVGAGDSMVGAM 262
|
250
....*....|....*..
gi 23397419 277 AFYLAyyPNLSLEEMLK 293
Cdd:PRK10294 263 TLKLA--ENASLEEMVR 277
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
196-281 |
1.41e-07 |
|
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: 52.34 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 196 IFCCNESEAEILTGHAVSDPTTAGKA----AMILLERGCQ----VVVITLGASGCVILSQAEPVPKHIP---TEAVKAVD 264
Cdd:cd01943 183 VFSPNLEEAARLLGLPTSEPSSDEEKeavlQALLFSGILQdpggGVVLRCGKLGCYVGSADSGPELWLPayhTKSTKVVD 262
|
90
....*....|....*..
gi 23397419 265 TTGAGDSFVGALAFYLA 281
Cdd:cd01943 263 PTGGGNSFLGGFAAGLA 279
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
53-302 |
2.06e-07 |
|
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: 51.25 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDsfgndYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAGANLfl 132
Cdd:cd01937 24 GGPATYASLTLSRLGLTVKLVTKVGRD-----YPDKWSDLFDNGIEVISLLSTETTTFELNYTNEGRTRTLLAKCAAI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 133 nsEDLKKAASVISRAKVMICQL--EISPAASLEaltmarrsgvktlfnPAPAMadLDPQFY-----TLSSIFCCNESEAE 205
Cdd:cd01937 97 --PDTESPLSTITAEIVILGPVpeEISPSLFRK---------------FAFIS--LDAQGFlrranQEKLIKCVILKLHD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 206 ILTGHAVS--DPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALaFYLAYY 283
Cdd:cd01937 158 VLKLSRVEaeVISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKY--TIPASKKDVVDPTGAGDVFLAAF-LYSRLS 234
|
250
....*....|....*....
gi 23397419 284 PNlsleEMLKRSNFIAAVS 302
Cdd:cd01937 235 GK----DIKEAAEFAAAAA 249
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
200-303 |
5.45e-07 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 50.46 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 200 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILS-----QAEPvPKhipteaVKAVDTTGAGDSFVG 274
Cdd:PRK09513 187 NRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNasgewIAKP-PA------CDVVSTVGAGDSMVG 259
|
90 100
....*....|....*....|....*....
gi 23397419 275 ALAFYLAYypNLSLEEMLKRSNFIAAVSV 303
Cdd:PRK09513 260 GLIYGLLM--RESSEHTLRLATAVSALAV 286
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
54-308 |
2.10e-06 |
|
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: 49.06 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 54 GKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFtYQTRDAATGTaSIIVNNEGQNIIVivaganlfLN 133
Cdd:PRK11316 51 GGAANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDF-VSVPTHPTIT-KLRVLSRNQQLIR--------LD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 134 SED----------LKKAASVISRAKVMIcqleISPAA-----SLEAL-TMARRSGVKTLFNPAPAmadlDPQFYTLSSIF 197
Cdd:PRK11316 121 FEEgfegvdpqplLERIEQALPSIGALV----LSDYAkgalaSVQAMiQLARKAGVPVLIDPKGT----DFERYRGATLL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 198 CCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPvPKHIPTEAVKAVDTTGAGDSFVGALA 277
Cdd:PRK11316 193 TPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLLQPGKA-PLHLPTQAREVYDVTGAGDTVISVLA 271
|
250 260 270
....*....|....*....|....*....|.
gi 23397419 278 FYLAyyPNLSLEEMLKRSNFIAAVSVQATGT 308
Cdd:PRK11316 272 AALA--AGNSLEEACALANAAAGVVVGKLGT 300
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
53-307 |
4.23e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 47.42 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFtYQTRDAATgtASIIVNNEGQNIIV--IVAG--A 128
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISH-VHTKHGVT--AQTQVELHDNDRVFgdYTEGvmA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 129 NLFLNSEDLKkaasvisrakvMICQLEISPAA----SLEALTMARRSGVKTLFNPA-----PAMADLDPQF-YTLSSifc 198
Cdd:PRK09813 100 DFALSEEDYA-----------WLAQYDIVHAAiwghAEDAFPQLHAAGKLTAFDFSdkwdsPLWQTLVPHLdYAFAS--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 199 cneseaeiltgHAVSDPTTAgKAAMILLERGCQVVVITLGASGCVILSQAEpVPKHiPTEAVKAVDTTGAGDSFVGalAF 278
Cdd:PRK09813 166 -----------APQEDEFLR-LKMKAIVARGAGVVIVTLGENGSIAWDGAQ-FWRQ-APEPVTVVDTMGAGDSFIA--GF 229
|
250 260
....*....|....*....|....*....
gi 23397419 279 YLAYYPNLSLEEMLKRSNFIAAVSVQATG 307
Cdd:PRK09813 230 LCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
181-306 |
5.04e-05 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 43.98 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 181 PAMADLDPQFYTLSSIFCC--------------NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT--------LG 238
Cdd:COG2240 112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpAD 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397419 239 ASGCVILSQAEpvPKHIPTEAVkAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKR-SNFIAAVsVQAT 306
Cdd:COG2240 192 KIGNLAVTADG--AWLVETPLL-PFSPNGTGDLFAALLLAHLLR--GKSLEEALERaAAFVYEV-LERT 254
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
53-278 |
5.90e-05 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 44.15 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAGANL-F 131
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDETVLAINDTHILqQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 132 LNSEDLKKAASVISRAKVMICQLEISPAAsLEaltmarrsGVKTLFNPAPAMADLDPQFYT------LSSIFCC--NESE 203
Cdd:PRK09954 173 LTPQLLNGSRDLIRHAGVVLADCNLTAEA-LE--------WVFTLADEIPVFVDTVSEFKAgkikhwLAHIHTLkpTQPE 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397419 204 AEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGcVILSQAEPVPKHIPTEAVKAVDTTGAGDSFVGALAF 278
Cdd:PRK09954 244 LEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDES-VFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLVY 317
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
228-307 |
7.46e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 44.03 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 228 RGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGalAFYLAYYPNLSLEEMLKRSNFIAAVSVQATG 307
Cdd:PLN02630 201 RQKCCVIVTNGKKGCRIYWKDGEM--RVPPFPAIQVDPTGAGDSFLG--GFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
200-281 |
9.97e-05 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 43.10 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 200 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT---LGASGCV-ILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGA 275
Cdd:COG0351 133 NLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghLPGDEAVdVLYDGDGV-REFSAPRIDTGNTHGTGCTLSSA 211
|
....*.
gi 23397419 276 LAFYLA 281
Cdd:COG0351 212 IAALLA 217
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
203-290 |
1.37e-04 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 42.47 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 203 EAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT----LGASGCV--ILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGAL 276
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVVtdVLYDGGGF-YTLEAPRIPTKNTHGTGCTLSAAI 207
|
90
....*....|....
gi 23397419 277 AFYLAYypNLSLEE 290
Cdd:pfam08543 208 AANLAK--GLSLPE 219
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
199-306 |
3.13e-04 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 41.42 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 199 CNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT-----LGASGCVILSQAEP-----VPKhIPTEAvkavDTTGA 268
Cdd:cd01173 142 PNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelaDDDRIEMLGSTATEawlvqRPK-IPFPA----YFNGT 216
|
90 100 110
....*....|....*....|....*....|....*....
gi 23397419 269 GDSFVGALAFYLAYYPnlSLEEMLKRS-NFIAAVsVQAT 306
Cdd:cd01173 217 GDLFAALLLARLLKGK--SLAEALEKAlNFVHEV-LEAT 252
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
47-179 |
8.82e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 40.66 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 47 EFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIV--NNEGQNIIVI 124
Cdd:PLN02543 166 EFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIkfRDGGKMVAET 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397419 125 VAGAnlflnSEDLKKAA----SVISRAKVMICQLEISPAASLE-----ALTMARRSGVKTLFNP 179
Cdd:PLN02543 246 VKEA-----AEDSLLASelnlAVLKEARMFHFNSEVLTSPSMQstlfrAIELSKKFGGLIFFDL 304
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
203-286 |
5.45e-03 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 37.80 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397419 203 EAEILTGHAVSDPTTAGK-AAMILLERGCQVVVITlgasGCVILSQAEPVP--------KHIPTEAVKAVDTTGAGDSFV 273
Cdd:PRK06427 143 EAEALTGLPIADTEDEMKaAARALHALGCKAVLIK----GGHLLDGEESVDwlfdgegeERFSAPRIPTKNTHGTGCTLS 218
|
90
....*....|...
gi 23397419 274 GALAFYLAYYPNL 286
Cdd:PRK06427 219 AAIAAELAKGASL 231
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
193-236 |
7.29e-03 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 37.75 E-value: 7.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 23397419 193 LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 236
Cdd:PTZ00344 139 YADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| |
