|
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 |
7.73e-141 |
|
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: 399.67 E-value: 7.73e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLKKAAHVISRAKVMICQLEISPAASLEALTMARSSGVKTLFNPAPA 182
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 183 IADLDPRFYTLSTVFCCNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLSQAEpvPKHIPTEAVKA 262
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157823079 263 VDTTGAGDSFVGALAFYLAYYPslSLEEMLKRSNSIAAVSVQATGTQSSYPYKKDLP 319
Cdd:TIGR02152 239 VDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
23-314 |
5.28e-126 |
|
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: 361.87 E-value: 5.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:cd01174 6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLKKAAHVISRAKVMICQLEISPAASLEALTMARSSGVKTLFNPAPA 182
Cdd:cd01174 86 VGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVILNPAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 183 IADLDPrFYTLSTVFCCNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLSqaEPVPKHIPTEAVKA 262
Cdd:cd01174 166 RPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS--GGEVEHVPAFKVKA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 157823079 263 VDTTGAGDSFVGALAFYLAYYPslSLEEMLKRSNSIAAVSVQATGTQSSYPY 314
Cdd:cd01174 243 VDTTGAGDTFIGALAAALARGL--SLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
23-319 |
7.21e-108 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 317.45 E-value: 7.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:PTZ00292 22 GSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNE-GQNIIVIVAGANLLLNTEDLKKAAHVI-SRAKVMICQLEISPAASLEALTMARSSGVKTLFNPA 180
Cdd:PTZ00292 102 ENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGCYTVFNPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 181 PAIADLDPR----FYTLSTVFCCNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVtLSQAEPVPKHIP 256
Cdd:PTZ00292 182 PAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCL-IVEKENEPVHVP 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823079 257 TEAVKAVDTTGAGDSFVGALAFYLAYypSLSLEEMLKRSNSIAAVSVQATGTQSSYPYKKDLP 319
Cdd:PTZ00292 261 GKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISVTRHGTQSSYPHPSELP 321
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
23-318 |
6.61e-78 |
|
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: 240.17 E-value: 6.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:COG0524 6 GEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSGVRRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLKKAAhvISRAKVMICQL-----EISPAASLEALTMARSSGVKTLF 177
Cdd:COG0524 86 PGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAGVPVSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 178 NPAPAIADLDP------RFYTLSTVFCCNESEAEILTGHavndpTTAGTAALVLLERGCQVVVITLGASGCVTLSQAEPV 251
Cdd:COG0524 164 DPNYRPALWEParellrELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823079 252 pkHIPTEAVKAVDTTGAGDSFVGALAFYLAYypSLSLEEMLKRSNSIAAVSVQATGTQSSYPYKKDL 318
Cdd:COG0524 239 --HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
36-319 |
1.83e-73 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 228.60 E-value: 1.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 36 LPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQTRDAATGTASIIVN 115
Cdd:PRK11142 22 FPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 116 NEGQNIIVIVAGANLLLNTEDLKKAAHVISRAKVMICQLEiSPAAS-LEALTMARSSGVKTLFNPAPAiADLDPRFYTLS 194
Cdd:PRK11142 102 DEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLE-TPLETvLAAAKIAKQHGTKVILNPAPA-RELPDELLALV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 195 TVFCCNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGcVTLSQAEPvPKHIPTEAVKAVDTTGAGDSFVG 274
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRG-VWLSENGE-GQRVPGFRVQAVDTIAAGDTFNG 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 157823079 275 ALAfyLAYYPSLSLEEMLKRSNSIAAVSVQATGTQSSYPYKKDLP 319
Cdd:PRK11142 258 ALV--TALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEID 300
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
23-310 |
4.40e-60 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 194.10 E-value: 4.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPktGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:pfam00294 6 GEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLKKAAHVISRAKVM----ICQLEISPAASLEALTMARSSG--VKTL 176
Cdd:pfam00294 84 EDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGtfDPNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 177 FNPAPAIADLDPRFYTLSTVFCCNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLSQAEPVpKHIP 256
Cdd:pfam00294 164 LDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV-HVPA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157823079 257 TEAVKAVDTTGAGDSFVGA-LAFYLAyypSLSLEEMLKRSNSIAAVSVQATGTQS 310
Cdd:pfam00294 243 VPKVKVVDTTGAGDSFVGGfLAGLLA---GKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
23-307 |
1.80e-34 |
|
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: 127.31 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVsltsrlPKTGETIHGHKFF-IGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQ 101
Cdd:cd01166 6 GEVMVDLS------PPGGGRLEQADSFrKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 102 TRDAATGTASIIV--NNEGQNIIVIVAGANLLLNTEDLKKAAhvISRAK-VMICqlEISPAAS-------LEALTMARSS 171
Cdd:cd01166 80 DPGRPTGLYFLEIgaGGERRVLYYRAGSAASRLTPEDLDEAA--LAGADhLHLS--GITLALSesarealLEALEAAKAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 172 GVKTLF--NPAPAIADLD------PRFYTLSTVFCCNESEAEILTGHAVnDPTTAgtAALVLLERGCQVVVITLGASGCV 243
Cdd:cd01166 156 GVTVSFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDED-PTDAA--ERALALALGVKAVVVKLGAEGAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823079 244 TLSQAEPVpkHIPTEAVKAVDTTGAGDSFVGA-LAFYLAYypsLSLEEMLKRSNSIAAVSVQATG 307
Cdd:cd01166 233 VYTGGGRV--FVPAYPVEVVDTTGAGDAFAAGfLAGLLEG---WDLEEALRFANAAAALVVTRPG 292
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
53-307 |
3.37e-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: 126.60 E-value: 3.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAG--ANL 130
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGpaADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 131 LLNTEDLKKaahVISRAK-VMICQL----EISPAASLEALTMARSSGVKTLFNP---------APAIADLDPRFYTLSTV 196
Cdd:cd01167 108 LLDTELNPD---LLSEADiLHFGSIalasEPSRSALLELLEAAKKAGVLISFDPnlrpplwrdEEEARERIAELLELADI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 197 FCCNESEAEILTGHAVNDpttagTAALVLLERGCQVVVITLGASGCvTLSQAEpVPKHIPTEAVKAVDTTGAGDSFVGAL 276
Cdd:cd01167 185 VKLSDEELELLFGEEDPE-----EIAALLLLFGLKLVLVTRGADGA-LLYTKG-GVGEVPGIPVEVVDTTGAGDAFVAGL 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 157823079 277 AFYLAYYPSLS-----LEEMLKRSNSIAAVSVQATG 307
Cdd:cd01167 258 LAQLLSRGLLAldedeLAEALRFANAVGALTCTKAG 293
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
53-308 |
1.43e-33 |
|
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: 125.42 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQTrDAATGTASIIVNNEGQNIIVIVAGANLLL 132
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQP-DGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 133 NTEDLKKAAhvISRAKVMIC---QLEISPAASLEALTMARSSGVKTLFN-PAPAIAD-----LDPRFYTLSTVFcCNESE 203
Cdd:cd01168 134 SPDDLDWSL--LAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlSAPFIVQrfkeaLLELLPYVDILF-GNEEE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 204 AEILTGHAVNDPTTAGTAalvLLERGCQVVVITLGASGCVTLSQAE--PVPkhiPTEAVKAVDTTGAGDSFVGalAFYLA 281
Cdd:cd01168 211 AEALAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVEGGEvyPVP---AIPVEKIVDTNGAGDAFAG--GFLYG 282
|
250 260
....*....|....*....|....*..
gi 157823079 282 YYPSLSLEEMLKRSNSIAAVSVQATGT 308
Cdd:cd01168 283 LVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
23-314 |
1.95e-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: 118.94 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:cd01945 6 GLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNEGQNIIVIVAG----ANLLLNTEDLKKAA--HVISRAkvmicqleisPAASLEALTMARSSGVktl 176
Cdd:cd01945 86 PGARSPISSITDITGDRATISITAIdtqaAPDSLPDAILGGADavLVDGRQ----------PEAALHLAQEARARGI--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 177 fnpaPAIADLDP-------RFYTLSTVFCCNESEAEILTGhavndptTAGTAALVLL-ERGCQVVVITLGASGCVTLSQA 248
Cdd:cd01945 153 ----PIPLDLDGgglrvleELLPLADHAICSENFLRPNTG-------SADDEALELLaSLGIPFVAVTLGEAGCLWLERD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823079 249 EPVpKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPSLSLEEMLKRSNSIAAVSVQATGTQSSYPY 314
Cdd:cd01945 222 GEL-FHVPAFPVEVVDTTGAGDVFHGAFAHALA--EGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
23-309 |
1.28e-29 |
|
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: 113.95 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:cd01942 6 GHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNEGQNIIVIVAGANLLLnteDLKKAAHVISRAKVmicqleISPAASLEALTMARS---SGVKTLFNP 179
Cdd:cd01942 86 DEDSTGVAFILTDGDDNQIAYFYPGAMDEL---EPNDEADPDGLADI------VHLSSGPGLIELARElaaGGITVSFDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 180 APAIADLD----PRFYTLSTVFCCNESEAEILTghavndpTTAGTAALVLLErGCQVVVITLGASGCVTLSQAEPVpKHI 255
Cdd:cd01942 157 GQELPRLSgeelEEILERADILFVNDYEAELLK-------ERTGLSEAELAS-GVRVVVVTLGPKGAIVFEDGEEV-EVP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157823079 256 PTEAVKAVDTTGAGDSFvgALAFYLAYYPSLSLEEMLKRSNSIAAVSVQATGTQ 309
Cdd:cd01942 228 AVPAVKVVDTTGAGDAF--RAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
53-308 |
1.61e-24 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 101.04 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGkGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQTRDAATgTASIIVNNEGQNIIVIVAGANLLL 132
Cdd:COG2870 56 GG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPT-TTKTRVIAGGQQLLRLDFEDRFPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 133 NTED----LKKAAHVISRAKVMIcqLE------ISPAASLEALTMARSSGVKTLFNPAPAiadlDPRFYTLSTVFCCNES 202
Cdd:COG2870 134 SAELearlLAALEAALPEVDAVI--LSdygkgvLTPELIQALIALARAAGKPVLVDPKGR----DFSRYRGATLLTPNLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 203 EAEILTGHAVNDPTTAGTAALVLLER-GCQVVVITLGASGcVTLSQAEPVPKHIPTEAVKAVDTTGAGDSFVGALAFYLA 281
Cdd:COG2870 208 EAEAAVGIPIADEEELVAAAAELLERlGLEALLVTRGEEG-MTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALA 286
|
250 260
....*....|....*....|....*..
gi 157823079 282 YypSLSLEEMLKRSNSIAAVSVQATGT 308
Cdd:COG2870 287 A--GASLEEAAELANLAAGIVVGKLGT 311
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
54-313 |
2.41e-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: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 54 GKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEF-TYQTRDAATGTAsiivnnegqniiVIVAGANLL- 131
Cdd:cd01172 40 GGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGiVDEGRPTTTKTR------------VIARNQQLLr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 132 LNTED------------LKKAAHVISRAKVMIcqLE------ISPAASLEALTMARSSGVKTLFNPAPaiadLDPRFYTL 193
Cdd:cd01172 108 VDREDdsplsaeeeqrlIERIAERLPEADVVI--LSdygkgvLTPRVIEALIAAARELGIPVLVDPKG----RDYSKYRG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 194 STVFCCNESEAEILTGHAVNDPTTAGTAALVLLER-GCQVVVITLGASGCvTLSQAEPVPKHIPTEAVKAVDTTGAGDSF 272
Cdd:cd01172 182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGM-TLFERDGEVQHIPALAKEVYDVTGAGDTV 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 157823079 273 VGALAFYLAyyPSLSLEEMLKRSNSIAAVSVQATGTQSSYP 313
Cdd:cd01172 261 IATLALALA--AGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
52-281 |
3.93e-24 |
|
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: 99.31 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 52 FGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQ---NHISTEFtyqtRDAATGTASIIVNNEGqNIIVIVAGA 128
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKaglNVRGIVF----EGRSTASYTAILDKDG-DLVVALADM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 129 NL--LLNTEDLKKAAHVISRAKVMICQLEISPAASLEALTMARSSGVKTLFNP--APAIADLDPRFYTLSTVFCcNESEA 204
Cdd:cd01941 109 DIyeLLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAFEPtsAPKLKKLFYLLHAIDLLTP-NRAEL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823079 205 EILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLSQAEPV-PKHIPTEAV-KAVDTTGAGDSFVGALAFYLA 281
Cdd:cd01941 188 EALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVeTKLFPAPQPeTVVNVTGAGDAFVAGLVAGLL 266
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
53-318 |
1.30e-22 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 95.77 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQtrDAATGTASIIV--NNEGQN--IIVIVAGA 128
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRL--DPAHRTSTVVVdlDDQGERsfTFMVRPSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 129 NLLLNTEDL-----KKAAHVISRAkvmICQlEISPAASLEALTMARSSGVKTLFNP---------APAIADLDPRFYTLS 194
Cdd:PRK09434 106 DLFLQPQDLppfrqGEWLHLCSIA---LSA-EPSRSTTFEAMRRIKAAGGFVSFDPnlredlwqdEAELRECLRQALALA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 195 TVFCCNESEAEILTGHAVNDpttAGTAALVLlERGCQVVVITLGASGCVTLSQAEPvpKHIPTEAVKAVDTTGAGDSFVG 274
Cdd:PRK09434 182 DVVKLSEEELCFLSGTSQLE---DAIYALAD-RYPIALLLVTLGAEGVLVHTRGQV--QHFPAPSVDPVDTTGAGDAFVA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 157823079 275 ALAFYLAYYPSLS----LEEMLKRSNSIAAVSVQATGTQSSYPYKKDL 318
Cdd:PRK09434 256 GLLAGLSQAGLWTdeaeLAEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
53-317 |
5.83e-20 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 88.52 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIV--AGANL 130
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSADM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 131 LLNTEDLKKaaHVISRAKV-------MICqlEISPAASLEALTMARSSGVKTLFNP---------APAIADLDPRFYTLS 194
Cdd:PLN02323 123 LLRESELDL--DLIRKAKIfhygsisLIT--EPCRSAHLAAMKIAKEAGALLSYDPnlrlplwpsAEAAREGIMSIWDEA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 195 TVFCCNESEAEILTGhavNDPTTAGTAaLVLLERGCQVVVITLGASGCVTLSQAepVPKHIPTEAVKAVDTTGAGDSFVG 274
Cdd:PLN02323 199 DIIKVSDEEVEFLTG---GDDPDDDTV-VKLWHPNLKLLLVTEGEEGCRYYTKD--FKGRVEGFKVKAVDTTGAGDAFVG 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 157823079 275 ALAFYLAYYPSL-----SLEEMLKRSNSIAAVSVQATGTQSSYPYKKD 317
Cdd:PLN02323 273 GLLSQLAKDLSLledeeRLREALRFANACGAITTTERGAIPALPTKEA 320
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
23-281 |
4.16e-19 |
|
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: 83.68 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVckvgndsfgnnyienlkqnhisteftyqt 102
Cdd:cd00287 6 GSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLV----------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 rdaatgTASIIVNNEGQniivivaganlllntedlkkaahvisrakvmicqleISPAASLEALTMARSSGVKTLFNPAPA 182
Cdd:cd00287 57 ------GADAVVISGLS------------------------------------PAPEAVLDALEEARRRGVPVVLDPGPR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 183 IADLDP----RFYTLSTVFCCNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLSQAEPVpKHIPTE 258
Cdd:cd00287 95 AVRLDGeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTE-VHVPAF 173
|
250 260
....*....|....*....|...
gi 157823079 259 AVKAVDTTGAGDSFVGALAFYLA 281
Cdd:cd00287 174 PVKVVDTTGAGDAFLAALAAGLA 196
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
23-307 |
3.28e-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: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGkGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHIstEFTYQT 102
Cdd:cd01944 6 GAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGI--EILLPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 R-DAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLKkAAHVISRAKVMICQLEI-SPAASLEALT---MARSSGVKTLF 177
Cdd:cd01944 83 RgGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFA-TLTVAPYDYVYLSGYTLaSENASKVILLewlEALPAGTTLVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 178 NPAPAIADLDP----RFYTLSTVFCCNESEAEILTGhavndpTTAGTAALVLLERGCQV---VVITLGASGCVTLSQAEP 250
Cdd:cd01944 162 DPGPRISDIPDtilqALMAKRPIWSCNREEAAIFAE------RGDPAAEASALRIYAKTaapVVVRLGSNGAWIRLPDGN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157823079 251 vPKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPSLSLEEMLKRSNSIAAVSVQATG 307
Cdd:cd01944 236 -THIIPGFKVKAVDTIGAGDTHAGGMLAGLA--KGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
200-309 |
2.33e-17 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 80.95 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 200 NESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAfy 279
Cdd:COG1105 184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVSTVGAGDSMVAGFL-- 259
|
90 100 110
....*....|....*....|....*....|
gi 157823079 280 LAYYPSLSLEEMLKRSNSIAAVSVQATGTQ 309
Cdd:COG1105 260 AGLARGLDLEEALRLAVAAGAAAALSPGTG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
54-307 |
1.21e-16 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 80.26 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 54 GKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHIST-EFTYQTRDAATGTAsiivNNEGQNIIVIVAGAN--- 129
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVvGLIEGTDAGDSSSA----SYETLLCWVLVDPLQrhg 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 130 -----------LLLNTEDLKKAAH-VISRAKVMICQ----LEISPAASLEALTMARSSGVKTLFNPAP-----AIADLDP 188
Cdd:PLN02341 196 fcsradfgpepAFSWISKLSAEAKmAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgkslLVGTPDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 189 R-----FYTLSTVFCCNESEAEILTGhaVNDPTTAGTAalvLLERGC--QVVVITLGASGC--VTLSQAEPVPkhipTEA 259
Cdd:PLN02341 276 RralehLLRMSDVLLLTSEEAEALTG--IRNPILAGQE---LLRPGIrtKWVVVKMGSKGSilVTRSSVSCAP----AFK 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 157823079 260 VKAVDTTGAGDSFVGALAFylAYYPSLSLEEMLKRSNSIAAVSvqATG 307
Cdd:PLN02341 347 VNVVDTVGCGDSFAAAIAL--GYIHNLPLVNTLTLANAVGAAT--AMG 390
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
28-304 |
8.54e-16 |
|
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: 75.92 E-value: 8.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 28 DLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHIstEFTYQTRDAAT 107
Cdd:cd01947 11 DIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KHTVAWRDKPT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 108 GTASIIVNNEGQNIIVIVAGanlllNTEDLKKAAHVISRAKVMIcqleISPAASLEALTMARSSGVKTLFNPAPAIADLD 187
Cdd:cd01947 89 RKTLSFIDPNGERTITVPGE-----RLEDDLKWPILDEGDGVFI----TAAAVDKEAIRKCRETKLVILQVTPRVRVDEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 188 PRFYTLSTVFCCNESEAEILtghavndpttagTAALVLLERGCQVVVITLGASGCVTLSQAEpvPKHIPTEAVKAVDTTG 267
Cdd:cd01947 160 NQALIPLDILIGSRLDPGEL------------VVAEKIAGPFPRYLIVTEGELGAILYPGGR--YNHVPAKKAKVPDSTG 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 157823079 268 AGDSFVGALAFYLAYypSLSLEEMLKRSNSIAAVSVQ 304
Cdd:cd01947 226 AGDSFAAGFIYGLLK--GWSIEEALELGAQCGAICVS 260
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
200-309 |
7.47e-15 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 73.34 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 200 NESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAfy 279
Cdd:cd01164 184 NREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVY--RASPPKVKVVSTVGAGDSMVAGFV-- 259
|
90 100 110
....*....|....*....|....*....|
gi 157823079 280 LAYYPSLSLEEMLKRSNSIAAVSVQATGTQ 309
Cdd:cd01164 260 AGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
53-318 |
1.83e-11 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 64.28 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQC-VQAARLGAKAAMVCKVG---NDSFGNNYIENLKQNHISTEFTYqTRDAATGTASIIVNNEGQNIIVIVAGA 128
Cdd:PTZ00247 62 GGSALNTArVAQWMLQAPKGFVCYVGcvgDDRFAEILKEAAEKDGVEMLFEY-TTKAPTGTCAVLVCGKERSLVANLGAA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 129 NLL----LNTEDLKKAahvISRAKVMICQ---LEISPAASLEALTMARSSGVKTLFN-PAP-AIADLDPRFYTL----ST 195
Cdd:PTZ00247 141 NHLsaehMQSHAVQEA---IKTAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFFFERLLQVlpyvDI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 196 VFCcNESEAEILtGHAVNDPTTAGT---AALVLLERGC----QVVVITLGAS----GCVTLSQAEPVPkhiPTEAVKAVD 264
Cdd:PTZ00247 218 LFG-NEEEAKTF-AKAMKWDTEDLKeiaARIAMLPKYSgtrpRLVVFTQGPEptliATKDGVTSVPVP---PLDQEKIVD 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157823079 265 TTGAGDSFVGA-LAFYLAYYPslsLEEMLKRSNSIAAVSVQATGtqSSYPYKKDL 318
Cdd:PTZ00247 293 TNGAGDAFVGGfLAQYANGKD---IDRCVEAGHYSAQVIIQHNG--CTYPEKPPF 342
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
53-300 |
1.22e-10 |
|
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: 60.83 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTyQTRDAATGTASIIVNNeGQNIIVIV---AGAN 129
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVD-GDRIFGLSnkgGVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 130 LLLNTED---LKKAAHVISrakvmicqLEISPAASLEALTMARS-SGVKTLF----NPAPAIADLDPRFYTLSTVFCCNE 201
Cdd:cd01940 100 EHPFEADleyLSQFDLVHT--------GIYSHEGHLEKALQALVgAGALISFdfsdRWDDDYLQLVCPYVDFAFFSASDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 202 SEAEIltghavndpttaGTAALVLLERGCQVVVITLGASGCVTLSQAEPVPKHIptEAVKAVDTTGAGDSFVGALAFYLA 281
Cdd:cd01940 172 SDEEV------------KAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAP--RPVEVVDTLGAGDSFIAGFLLSLL 237
|
250
....*....|....*....
gi 157823079 282 YYpSLSLEEMLKRSNSIAA 300
Cdd:cd01940 238 AG-GTAIAEAMRQGAQFAA 255
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
200-307 |
9.94e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 59.03 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 200 NESEA-EILTGHAVNDPTtagtAALVLLERGCQVVVITLGASGCVTLSQAEPVpkHIP-TEAVKAVDTTGAGDSFVGalA 277
Cdd:PLN02379 239 NEDEArELLRGEQESDPE----AALEFLAKYCNWAVVTLGSKGCIARHGKEVV--RVPaIGETNAVDATGAGDLFAS--G 310
|
90 100 110
....*....|....*....|....*....|
gi 157823079 278 FYLAYYPSLSLEEMLKRSNSIAAVSVQATG 307
Cdd:PLN02379 311 FLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
67-318 |
1.96e-08 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 54.72 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 67 GAKAAMVCkVGNDSFGNNYIENLKQNHISTEFtYQTRDAATGTASIIVNNEGQNIIVIVAGANLLlNTEDLKKAAH--VI 144
Cdd:PLN02548 70 GATSYMGC-IGKDKFGEEMKKCATAAGVNVHY-YEDESTPTGTCAVLVVGGERSLVANLSAANCY-KVEHLKKPENwaLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 145 SRAKVMICQ---LEISPAASLEALTMARSSGVKTLFN-PAPAIADL--DPRFYTLSTV--FCCNESEAEILTGHAVNDPT 216
Cdd:PLN02548 147 EKAKFYYIAgffLTVSPESIMLVAEHAAANNKTFMMNlSAPFICEFfkDQLMEALPYVdfLFGNETEARTFAKVQGWETE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 217 TAGTAALVLLE----RGCQ--VVVITLGA-------SGCVTLSQAEPVPKHipteavKAVDTTGAGDSFVGalAFYLAYY 283
Cdd:PLN02548 227 DVEEIALKISAlpkaSGTHkrTVVITQGAdptvvaeDGKVKEFPVIPLPKE------KLVDTNGAGDAFVG--GFLSQLV 298
|
250 260 270
....*....|....*....|....*....|....*
gi 157823079 284 PSLSLEEMLKRSNSIAAVSVQATGTqsSYPYKKDL 318
Cdd:PLN02548 299 QGKDIEECVRAGNYAANVIIQRSGC--TYPEKPDF 331
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
53-277 |
3.77e-08 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 53.84 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIV-AGANLL 131
Cdd:PRK09850 40 GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 132 LNTEDLKKAAHVISRAKVMICQLEISPAAsLEALtMARSSGVKTLFNPAPA-----IADLDPRFYTLSTvfccNESEAEI 206
Cdd:PRK09850 120 ITAEYLAQHREFIQRAKVIVADCNISEEA-LAWI-LDNAANVPVFVDPVSAwkcvkVRDRLNQIHTLKP----NRLEAET 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823079 207 LTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGcVTLSQAEPVPKHIPTEAVKAVDTTGAGDSFVGALA 277
Cdd:PRK09850 194 LSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDG-VYYSDISGESGWSAPIKTNVINVTGAGDAMMAGLA 263
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
200-303 |
1.45e-07 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 52.00 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 200 NESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGCVTLS-----QAEPvPKhipteaVKAVDTTGAGDSFVG 274
Cdd:PRK09513 187 NRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNasgewIAKP-PA------CDVVSTVGAGDSMVG 259
|
90 100
....*....|....*....|....*....
gi 157823079 275 ALAFYLAYypSLSLEEMLKRSNSIAAVSV 303
Cdd:PRK09513 260 GLIYGLLM--RESSEHTLRLATAVSALAV 286
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
196-291 |
1.48e-07 |
|
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: 51.70 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 196 VFCCNESEAEILTGHAvndptTAGTAALVLLERGCQVVVITLGASGCVTLSQ----AEPVpkhIPTEAVkaVDTTGAGDS 271
Cdd:cd01946 166 VVIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDdgyfAAPA---YPLESV--FDPTGAGDT 235
|
90 100
....*....|....*....|
gi 157823079 272 FVGALAFYLAYYPSLSLEEM 291
Cdd:cd01946 236 FAGGFIGYLASQKDTSEANM 255
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
53-293 |
1.57e-07 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 52.09 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNdSFGNNYIENLKQNHISTEfTYQTRDAATGTASIIVNNEGQNIIVIVAGANLll 132
Cdd:PRK10294 38 GGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVA-TVEAKDWTRQNLHVHVEASGEQYRFVMPGAAL-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 133 nTED----LKKAAHVISRAKVMICQLEISPAASLEALTM----ARSSGVKTL-------FNPAPAIADLdprfytlsTVF 197
Cdd:PRK10294 114 -NEDefrqLEEQVLEIESGAILVISGSLPPGVKLEKLTQlisaAQKQGIRCIidssgdaLSAALAIGNI--------ELV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 198 CCNESEAEILTGHAVNDPTTAGTAALVLLERG-CQVVVITLGASGCVTLS-----QAEPVPkhipteaVKAVDTTGAGDS 271
Cdd:PRK10294 185 KPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDsenciQVVPPP-------VKSQSTVGAGDS 257
|
250 260
....*....|....*....|..
gi 157823079 272 FVGALAFYLAyyPSLSLEEMLK 293
Cdd:PRK10294 258 MVGAMTLKLA--ENASLEEMVR 277
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
196-281 |
2.66e-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: 51.57 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 196 VFCCNESEAEILTGHAVNDPTTAGTAALVL--------LERGCQVVVITLGASGCVTLSQAEPVPKHIP---TEAVKAVD 264
Cdd:cd01943 183 VFSPNLEEAARLLGLPTSEPSSDEEKEAVLqallfsgiLQDPGGGVVLRCGKLGCYVGSADSGPELWLPayhTKSTKVVD 262
|
90
....*....|....*..
gi 157823079 265 TTGAGDSFVGALAFYLA 281
Cdd:cd01943 263 PTGGGNSFLGGFAAGLA 279
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
53-278 |
1.20e-06 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 49.54 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIvAGANLL- 131
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDETVLAI-NDTHILq 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 132 -LNTEDLKKAAHVISRAKVMICQLEISPAASLEALTMA-------------RSSGVKTLFnpapaiadldPRFYTLSTvf 197
Cdd:PRK09954 172 qLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLAdeipvfvdtvsefKAGKIKHWL----------AHIHTLKP-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 198 ccNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVITLGASGcVTLSQAEPVPKHIPTEAVKAVDTTGAGDSFVGALA 277
Cdd:PRK09954 240 --TQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDES-VFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLV 316
|
.
gi 157823079 278 F 278
Cdd:PRK09954 317 Y 317
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
41-309 |
2.65e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 48.65 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 41 ETIHGHKFFIGFGGKGANQCVQAARLGAKA--------AMVCKVGNDSFGNNYIENLKQNHIstEFTYQ-TRDAATGTAS 111
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANV--HFLSQpVKDGTTGTVI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 112 IIVNNEGQNIIVIVAGANLLLN-TEDLKKAahvISRAKVMICQ-----LEISPAASLEALTMARSSGVKTlfnpapAIAD 185
Cdd:PLN02813 192 VLTTPDAQRTMLSYQGTSSTVNyDSCLASA---ISKSRVLVVEgylweLPQTIEAIAQACEEAHRAGALV------AVTA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 186 LDP----RFY--------TLSTVFCCNESEAEILTGHAVNDPTTAGTAALvllERGCQVVVITLGASGCVTLSQAEPVpk 253
Cdd:PLN02813 263 SDVscieRHRddfwdvmgNYADILFANSDEARALCGLGSEESPESATRYL---SHFCPLVSVTDGARGSYIGVKGEAV-- 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 157823079 254 HIPTEAVKAVDTTGAGDSFV-GALAFYLAYYPSL-SLEEMLKRsnsIAAVSVQATGTQ 309
Cdd:PLN02813 338 YIPPSPCVPVDTCGAGDAYAaGILYGLLRGVSDLrGMGELAAR---VAATVVGQQGTR 392
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
53-307 |
5.62e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 47.04 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFtYQTRDAATgtASIIVNNEGQNIIV--IVAG--A 128
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISH-VHTKHGVT--AQTQVELHDNDRVFgdYTEGvmA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 129 NLLLNTEDLKkaahvisrakvMICQLEISPAA----SLEALTMARSSGVKTLFNPA-----PAIADLDPRF-YTLSTvfc 198
Cdd:PRK09813 100 DFALSEEDYA-----------WLAQYDIVHAAiwghAEDAFPQLHAAGKLTAFDFSdkwdsPLWQTLVPHLdYAFAS--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 199 cneseaeiltgHAVNDPTTAGTAALVLlERGCQVVVITLGASGCVTLSQAEpVPKHiPTEAVKAVDTTGAGDSFVGalAF 278
Cdd:PRK09813 166 -----------APQEDEFLRLKMKAIV-ARGAGVVIVTLGENGSIAWDGAQ-FWRQ-APEPVTVVDTMGAGDSFIA--GF 229
|
250 260
....*....|....*....|....*....
gi 157823079 279 YLAYYPSLSLEEMLKRSNSIAAVSVQATG 307
Cdd:PRK09813 230 LCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
168-308 |
1.01e-05 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 46.75 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 168 ARSSGVKTLFNPAPAiadlDPRFYTLSTVFCCNESEAEILTGHAVNDpttagtAALVllERGCQVV--------VITLGA 239
Cdd:PRK11316 167 ARKAGVPVLIDPKGT----DFERYRGATLLTPNLSEFEAVVGKCKDE------AELV--EKGMKLIadydlsalLVTRSE 234
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823079 240 SGcVTLSQAEPVPKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPSLSLEEMLKRSNSIAAVSVQATGT 308
Cdd:PRK11316 235 QG-MTLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALA--AGNSLEEACALANAAAGVVVGKLGT 300
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
53-300 |
5.69e-05 |
|
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: 43.93 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 53 GGKGANQCVQAARLGAKAAMVCKVGNDsfgnnYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAGANLLL 132
Cdd:cd01937 24 GGPATYASLTLSRLGLTVKLVTKVGRD-----YPDKWSDLFDNGIEVISLLSTETTTFELNYTNEGRTRTLLAKCAAIPD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 133 NTEDLKkaahVISRAKVMICQL--EISPAASLE-ALTMARSSGVKTLFNPAPAIADldpRFYTLSTVFCCNESEAEILtg 209
Cdd:cd01937 99 TESPLS----TITAEIVILGPVpeEISPSLFRKfAFISLDAQGFLRRANQEKLIKC---VILKLHDVLKLSRVEAEVI-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 210 havNDPTTAgtaALVLLERGCQVVVITLGASGCVTLSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPSlsle 289
Cdd:cd01937 170 ---STPTEL---ARLIKETGVKEIIVTDGEEGGYIFDGNGKY--TIPASKKDVVDPTGAGDVFLAAFLYSRLSGKD---- 237
|
250
....*....|.
gi 157823079 290 emLKRSNSIAA 300
Cdd:cd01937 238 --IKEAAEFAA 246
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
199-306 |
2.08e-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: 42.19 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 199 CNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVIT----LGASGCVTLSQAEPVPKHIPTEAVKAVDT-TGAGDSFV 273
Cdd:cd01173 142 PNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelADDDRIEMLGSTATEAWLVQRPKIPFPAYfNGTGDLFA 221
|
90 100 110
....*....|....*....|....*....|....
gi 157823079 274 GALAFYLAYYPslSLEEMLKRS-NSIAAVsVQAT 306
Cdd:cd01173 222 ALLLARLLKGK--SLAEALEKAlNFVHEV-LEAT 252
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
182-290 |
7.47e-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: 40.54 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 182 AIADLDPRFYTLSTVFCCNESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVIT----LGASGCVT--LSQAEPVpKHI 255
Cdd:pfam08543 108 AIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVVTdvLYDGGGF-YTL 186
|
90 100 110
....*....|....*....|....*....|....*
gi 157823079 256 PTEAVKAVDTTGAGDSFVGALAFYLAYYpsLSLEE 290
Cdd:pfam08543 187 EAPRIPTKNTHGTGCTLSAAIAANLAKG--LSLPE 219
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
200-281 |
8.00e-04 |
|
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: 40.41 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 200 NESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVIT-------------LGASGCVTLSQaepvpKHIPTEAvkavdTT 266
Cdd:COG0351 133 NLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghlpgdeavdvlYDGDGVREFSA-----PRIDTGN-----TH 202
|
90
....*....|....*
gi 157823079 267 GAGDSFVGALAFYLA 281
Cdd:COG0351 203 GTGCTLSSAIAALLA 217
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
23-308 |
9.01e-04 |
|
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: 40.47 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 23 GSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAKAAMVCKVGNDSFGNNYIENLKQNHISTEFTYQT 102
Cdd:cd01939 6 GLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISHCYRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 103 RDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLKKAA-------HVISR-----AKVMICQLEISPAASLEALTMARS 170
Cdd:cd01939 86 DIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDltqygwiHFEGRnpdetLRMMQHIEEHNNRRPEIRITISVE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 171 sgvktLFNPAPAIADL----DPRFYTLSTV--FCCNESEAEIltghaVNDPTTAGTAALVLLERGCQvvvitlGASGCVT 244
Cdd:cd01939 166 -----VEKPREELLELaaycDVVFVSKDWAqsRGYKSPEECL-----RGEGPRAKKAALLVCTWGDQ------GAGALGP 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823079 245 LSQAEPVPKHIPteaVKAVDTTGAGDSFVGALAFYLAYYPSlSLEEMLKRSNSIAAVSVQATGT 308
Cdd:cd01939 230 DGEYVHSPAHKP---IRVVDTLGAGDTFNAAVIYALNKGPD-DLSEALDFGNRVASQKCTGVGF 289
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
228-307 |
1.89e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 39.40 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 228 RGCQVVVITLGASGCVTLSQAEPVpkHIPTEAVKAVDTTGAGDSFVGalAFYLAYYPSLSLEEMLKRSNSIAAVSVQATG 307
Cdd:PLN02630 201 RQKCCVIVTNGKKGCRIYWKDGEM--RVPPFPAIQVDPTGAGDSFLG--GFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
181-306 |
2.29e-03 |
|
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: 38.98 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823079 181 PAIADLDPRFYTLSTVFCC--------------NESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVIT--------LG 238
Cdd:COG2240 112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpAD 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823079 239 ASGCVTLSQAEpvPKHIPTEAVkAVDTTGAGDSFVGALAFYLAYypSLSLEEMLKRSNSIAAVSVQAT 306
Cdd:COG2240 192 KIGNLAVTADG--AWLVETPLL-PFSPNGTGDLFAALLLAHLLR--GKSLEEALERAAAFVYEVLERT 254
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
200-236 |
2.70e-03 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 38.91 E-value: 2.70e-03
10 20 30
....*....|....*....|....*....|....*..
gi 157823079 200 NESEAEILTGHAVNDPTTAGTAALVLLERGCQVVVIT 236
Cdd:PTZ00344 146 NQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| |
