|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
11-302 |
8.38e-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: 361.10 E-value: 8.38e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 11 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 90
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 91 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLL 170
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 171 IRLRHCVSRYVYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKV 250
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 13469792 251 NAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPS 302
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
16-307 |
8.68e-125 |
|
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: 358.45 E-value: 8.68e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 16 GSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKV 95
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 96 PCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLL----- 170
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILnpapa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 171 IRlrhcVSRYVYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKV 250
Cdd:TIGR02152 161 IK----DLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13469792 251 NAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 307
Cdd:TIGR02152 237 KAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
9-307 |
9.49e-89 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 268.14 E-value: 9.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 9 EMDIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGIN 88
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 89 TTYVEKVPCTSSGVAPIFVN-ANSSNSILIIKGANKFLSPEDIDRAAEDL-KKCKLIVLQLEVQLETVYHAIEFGKKNGI 166
Cdd:PTZ00292 95 TSFVSRTENSSTGLAMIFVDtKTGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 167 ----------EVLLIRLRHCVSRYVyackcDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALW 236
Cdd:PTZ00292 175 ytvfnpapapKLAEVEIIKPFLKYV-----SLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLI 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13469792 237 MTRDQE-VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 307
Cdd:PTZ00292 250 VEKENEpVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELP 321
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-306 |
1.74e-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: 240.94 E-value: 1.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 11 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 90
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 91 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVLQL-----EVQLETVYHAIEFGKKNG 165
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 166 IEVLL---IR----------LRHCVSRyvyackCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDKGLNNIIVTMSEK 232
Cdd:COG0524 159 VPVSLdpnYRpalweparelLRELLAL------VDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13469792 233 GALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQF 306
Cdd:COG0524 228 GALLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
12-311 |
1.33e-63 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 203.18 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 91
Cdd:PRK11142 5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLL- 170
Cdd:PRK11142 85 VSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILn 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 171 ----IRLRHCVSRYVyackcDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVP 246
Cdd:PRK11142 165 papaRELPDELLALV-----DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVP 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13469792 247 AFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFNEFLT 311
Cdd:PRK11142 240 GFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
11-277 |
7.91e-55 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 180.23 E-value: 7.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 11 DIAVIGSNMVDLITYTNQMPkeGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 90
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 91 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIV----LQLEVQLETVYHAIEFGKKNGI 166
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYisgsLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 167 EVLLIRL-----RHCVSRYVYacKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQ 241
Cdd:pfam00294 159 FDPNLLDplgaaREALLELLP--LADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDG 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 13469792 242 EVHVPAF-KVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:pfam00294 237 EVHVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLE 273
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
11-277 |
2.87e-39 |
|
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: 139.63 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 11 DIAVIGSNMVDLitytnqMPKEGETLE-APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINT 89
Cdd:cd01166 1 DVVTIGEVMVDL------SPPGGGRLEqADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 90 TYVEKVPCTSSGVAPIFVNANSSNSILI-IKG-ANKFLSPEDIDRAAedLKKCKLIVL------QLEVQLETVYHAIEFG 161
Cdd:cd01166 75 SHVRVDPGRPTGLYFLEIGAGGERRVLYyRAGsAASRLTPEDLDEAA--LAGADHLHLsgitlaLSESAREALLEALEAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 162 KKNGIEV--------LLIRLRHCVSRYVYAC-KCDFFIPNETELEILTGMSVDTydhiRLAARSL-VDKGLNNIIVTMSE 231
Cdd:cd01166 153 KARGVTVsfdlnyrpKLWSAEEAREALEELLpYVDIVLPSEEEAEALLGDEDPT----DAAERALaLALGVKAVVVKLGA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 13469792 232 KGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:cd01166 229 EGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLE 274
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
11-277 |
1.37e-36 |
|
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: 132.43 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 11 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 90
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 91 YVEKVPCTSSGVApiFVNANSSNSILII--KGANKFLSPEDIDRAAEDLKkckliVLQLEVQLETVYHAIEFgKKNGIEV 168
Cdd:cd01942 81 HVRVVDEDSTGVA--FILTDGDDNQIAYfyPGAMDELEPNDEADPDGLAD-----IVHLSSGPGLIELAREL-AAGGITV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 169 -----------LLIRLRHCVSRyvyackCDFFIPNETELEILtgmsvdtydhIRLAARSL--VDKGLNNIIVTMSEKGAL 235
Cdd:cd01942 153 sfdpgqelprlSGEELEEILER------ADILFVNDYEAELL----------KERTGLSEaeLASGVRVVVVTLGPKGAI 216
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13469792 236 WMTRDQEVHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:cd01942 217 VFEDGEEVEVPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYDLE 259
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
15-302 |
2.29e-30 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 115.85 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 15 IGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDD-----IFADntirnLESWGINT 89
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDaigrlILAE-----LAAEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 90 TYVEKVPCTSSGVAPIFVNANSSNSILIIKGANKF----LSPEDIDRAAedlkkcklIVLQLEVQLETVYHAIEFGKKNG 165
Cdd:cd01945 80 SFIVVAPGARSPISSITDITGDRATISITAIDTQAapdsLPDAILGGAD--------AVLVDGRQPEAALHLAQEARARG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 166 IEVLLI--RLRHCVSRYVYACkCDFFIPNETELEILTGMSVDtydhirLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV 243
Cdd:cd01945 152 IPIPLDldGGGLRVLEELLPL-ADHAICSENFLRPNTGSADD------EALELLASLGIPFVAVTLGEAGCLWLERDGEL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 244 -HVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPS 302
Cdd:cd01945 225 fHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
12-264 |
8.54e-30 |
|
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: 114.66 E-value: 8.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITytNQMPKEGETLEAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 91
Cdd:cd01167 2 VVCFGEALIDFIP--EGSGAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAeDLKKCKL-----IVLQLEVQLETVYHAIEFGKKNGI 166
Cdd:cd01167 74 IQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPD-LLSEADIlhfgsIALASEPSRSALLELLEAAKKAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 167 EVLL---IRLRHCVSRYVYACKCDFFIP-------NETELEILTGMsvdtyDHIRLAARSLVDKGLNNIIVTMSEKGALW 236
Cdd:cd01167 153 LISFdpnLRPPLWRDEEEARERIAELLEladivklSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALL 227
|
250 260
....*....|....*....|....*...
gi 13469792 237 MTRDQEVHVPAFKVNAVDTSGAGDAFIG 264
Cdd:cd01167 228 YTKGGVGEVPGIPVEVVDTTGAGDAFVA 255
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
10-277 |
3.56e-27 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 108.07 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 10 MDIAVIGSNMVDLitYTNQMpkeGETLE-APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGIN 88
Cdd:TIGR04382 2 LDVITIGRVGVDL--YPQQI---GVPLEdVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 89 TTYVEKVPCTSSGVApifvnanssnsILIIKGANKF-------------LSPEDIDraAEDLKKCKLIV-----LQLEVQ 150
Cdd:TIGR04382 77 TSHVVTDPGRRTSLV-----------FLEIKPPDEFpllfyrenaadlaLTPDDVD--EDYIASARALLvsgtaLSQEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 151 LETVYHAIEFGKKNGIEVLL-IRLR-------HCVSRYV--YACKCDFFIPNETELEILTGMSVDtydhiRLAARSLVDK 220
Cdd:TIGR04382 144 REAVLKALEYARAAGVRVVLdIDYRpylwkspEEAGIYLrlVLPLVDVIIGTREEFDIAGGEGDD-----EAAARALLDA 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 13469792 221 GLNNIIVTMSEKGALWMTRDQE-VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:TIGR04382 219 GVEILVVKRGPEGSLVYTGDGEgVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLE 276
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
9-277 |
1.56e-26 |
|
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: 106.16 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 9 EMDIAVIGSNMVDLITYTN-----------------QMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGD 71
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDdafleklglkkgdmilaDMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 72 DIFADNTIRNLESWGINTTYVEKvPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVL---QLE 148
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRYQVQ-PDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSL--LAKAKYLYLegyLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 149 VQLETVYHAIEFGKKNGIEVLLiRL--RHCVSRY-----VYACKCDFFIPNETELEILTGMSVDtydHIRLAARSLVDKG 221
Cdd:cd01168 158 VPPEAILLAAEHAKENGVKIAL-NLsaPFIVQRFkeallELLPYVDILFGNEEEAEALAEAETT---DDLEAALKLLALR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13469792 222 LNNIIVTMSEKGALWMTRDQEVHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:cd01168 234 CRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEPLE 290
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
12-271 |
5.19e-26 |
|
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: 102.17 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLnskvlmltkvgddifadntirnleswgintty 91
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 vekvpctssGVAPIFVNAnssnSILIIKGANkfLSPEDIDRAAEDLKKCKLIVLqlevqLETVYHAIEFGKkngiEVLLI 171
Cdd:cd00287 50 ---------GVSVTLVGA----DAVVISGLS--PAPEAVLDALEEARRRGVPVV-----LDPGPRAVRLDG----EELEK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 172 RLRHCvsryvyackcDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRD-QEVHVPAFKV 250
Cdd:cd00287 106 LLPGV----------DILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGgTEVHVPAFPV 175
|
250 260
....*....|....*....|.
gi 13469792 251 NAVDTSGAGDAFIGCFSHYYV 271
Cdd:cd00287 176 KVVDTTGAGDAFLAALAAGLA 196
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
12-277 |
1.95e-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: 102.78 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMPKEGETLEAPAfKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTy 91
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTSNPGHV-KQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 vekvPCTSSGVA-PIFVNANSSNSILIIKGAN----KFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGI 166
Cdd:cd01941 80 ----GIVFEGRStASYTAILDKDGDLVVALADmdiyELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 167 EVLLI-----RLRHCVSRyvyACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQ 241
Cdd:cd01941 156 PVAFEptsapKLKKLFYL---LHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 13469792 242 EV---HVPAFKV-NAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:cd01941 233 GVetkLFPAPQPeTVVNVTGAGDAFVAGLVAGLLEGMSLD 272
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
20-277 |
4.96e-24 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 99.44 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 20 VDLITYTNQMpKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDdiFADNTIRN-LESWGINTTYVEkvpct 98
Cdd:COG1105 10 LDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGG--FTGEFIEElLDEEGIPTDFVP----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 99 ssgVAP-----IFVNANSSNSILIIKGANKFLSPEDIDRAAEDL----KKCKLIVL----------QLEVQLetvyhaIE 159
Cdd:COG1105 82 ---IEGetrinIKIVDPSDGTETEINEPGPEISEEELEALLERLeellKEGDWVVLsgslppgvppDFYAEL------IR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 160 FGKKNGIEVLLI----RLRHCVSRYVYACKcdffiPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGAL 235
Cdd:COG1105 153 LARARGAKVVLDtsgeALKAALEAGPDLIK-----PNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGAL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 13469792 236 WMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:COG1105 228 LVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLE 269
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
12-267 |
5.62e-23 |
|
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: 96.47 E-value: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQmpkEGETLEAP--AFKIG-----CGGkGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLES 84
Cdd:cd01172 2 VLVVGDVILDEYLYGDV---ERISPEAPvpVVKVEreeirLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 85 WGINTTYVekvpcTSSGVAPIFVNAnssnsilIIKGANK-----FLSPEDIDRAAED---------LKKCKLIVLQ---- 146
Cdd:cd01172 78 EGIDTDGI-----VDEGRPTTTKTR-------VIARNQQllrvdREDDSPLSAEEEQrlieriaerLPEADVVILSdygk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 147 --LEVQLetVYHAIEFGKKNGIEVLLIRLRHCVSRYVyacKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDK-GLN 223
Cdd:cd01172 146 gvLTPRV--IEALIAAARELGIPVLVDPKGRDYSKYR---GATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLE 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 13469792 224 NIIVTMSEKGALWMTRDQEV-HVPAFKVNAVDTSGAGDAFIGCFS 267
Cdd:cd01172 221 ALLVTLGEEGMTLFERDGEVqHIPALAKEVYDVTGAGDTVIATLA 265
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
20-277 |
2.39e-19 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 86.48 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 20 VDLITYTNQMpKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLML----TKVGDDIFAdntirNLESWGINTTYVEKV 95
Cdd:TIGR03168 10 IDLTIEVDGL-TPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATgflgGFTGEFIEA-----LLAEEGIKNDFVEVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 96 PCTSSGVApiFVNANSSNSILIIKGANkfLSPEDIDRAAED----LKKCKLIV----LQLEVQLETVYHAIEFGKKNGIE 167
Cdd:TIGR03168 84 GETRINVK--IKESSGEETELNEPGPE--ISEEELEQLLEKlrelLASGDIVVisgsLPPGVPPDFYAQLIAIARKKGAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 168 VLL----IRLRHCVSRYVYACKcdffiPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV 243
Cdd:TIGR03168 160 VILdtsgEALREALAAKPFLIK-----PNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGAL 234
|
250 260 270
....*....|....*....|....*....|....
gi 13469792 244 HVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:TIGR03168 235 KATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLE 268
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
20-277 |
2.93e-19 |
|
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: 85.66 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 20 VDLITYTNQmPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDiFADNTIRNLESWGINTTYVEkvpctS 99
Cdd:cd01164 11 IDLTIELDQ-LQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE-----V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 100 SGVAPIFVN-ANSSNSILIIKGANKFLSPEDIDRAAEDLK----KCKLIVL----------QLEVQLetvyhaIEFGKKN 164
Cdd:cd01164 84 AGETRINVKiKEEDGTETEINEPGPEISEEELEALLEKLKallkKGDIVVLsgslppgvpaDFYAEL------VRLAREK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 165 GIEVLL----IRLRHCVSRYVYACKcdffiPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRD 240
Cdd:cd01164 158 GARVILdtsgEALLAALAAKPFLIK-----PNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKD 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 13469792 241 QEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:cd01164 233 GVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLE 269
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
12-268 |
3.07e-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: 79.77 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGI-NTT 90
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDkHTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 91 YVEKVPctsSGVAPIFVNANSSNSILIIKGANK--------------FLSPEDIDraAEDLKKC---KLIVLQlevqlet 153
Cdd:cd01947 82 AWRDKP---TRKTLSFIDPNGERTITVPGERLEddlkwpildegdgvFITAAAVD--KEAIRKCretKLVILQ------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 154 vyhaieFGKKNGIEVLLIRLRHCvsryvyackcDFFIPNETELEILTGMSVDtydhirlaarslVDKGLNNIIVTMSEKG 233
Cdd:cd01947 150 ------VTPRVRVDELNQALIPL----------DILIGSRLDPGELVVAEKI------------AGPFPRYLIVTEGELG 201
|
250 260 270
....*....|....*....|....*....|....*
gi 13469792 234 ALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSH 268
Cdd:cd01947 202 AILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIY 236
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
12-275 |
1.55e-16 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 78.44 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLItytnqmP-KEGETLEAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 90
Cdd:PRK09434 5 VWVLGDAVVDLI------PeGENRYLKCP------GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 91 YVEKVPC--TSSGVAPIFVNANSSNSILIIKGANKFLSPEDID--RAAEDLKKCKlIVLQLEVQLETVYHAIEFGKKNGI 166
Cdd:PRK09434 73 YLRLDPAhrTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPpfRQGEWLHLCS-IALSAEPSRSTTFEAMRRIKAAGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 167 EVLL---IR---------LRHCVSRYV-YACKCDFfipNETELEILTGMsvdtyDHIRLAARSLVDK-GLNNIIVTMSEK 232
Cdd:PRK09434 152 FVSFdpnLRedlwqdeaeLRECLRQALaLADVVKL---SEEELCFLSGT-----SQLEDAIYALADRyPIALLLVTLGAE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13469792 233 GALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGD 275
Cdd:PRK09434 224 GVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGL 266
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
37-264 |
1.21e-13 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 70.42 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 37 EAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKVPCTSSGVAPIFVNANSSNSIL 116
Cdd:PLN02323 34 EAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 117 IIK--GANKFLSPEDIDraAEDLKKCKL-----IVLQLEVQLETVYHAIEFGKKNGieVLL-----IRL----------R 174
Cdd:PLN02323 114 FYRnpSADMLLRESELD--LDLIRKAKIfhygsISLITEPCRSAHLAAMKIAKEAG--ALLsydpnLRLplwpsaeaarE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 175 HCVSRYVYAckcDFFIPNETELEILTGmSVDTYDHirlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVD 254
Cdd:PLN02323 190 GIMSIWDEA---DIIKVSDEEVEFLTG-GDDPDDD---TVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVD 262
|
250
....*....|
gi 13469792 255 TSGAGDAFIG 264
Cdd:PLN02323 263 TTGAGDAFVG 272
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
6-264 |
9.40e-13 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 68.32 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 6 RGSEMDIAVIGSNMVDLITYTNQMP-----KEGETLE-----APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFA 75
Cdd:PLN02341 69 AGKEIDVATLGNLCVDIVLPVPELPppsreERKAYMEelaasPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 76 DNTIRNLESWGINTtyVEKVPCTSSGVApifVNANSSNSI--LIIKGANK--FLSPEDI-------------DRAAEDLK 138
Cdd:PLN02341 149 KFLLDVLAEEGISV--VGLIEGTDAGDS---SSASYETLLcwVLVDPLQRhgFCSRADFgpepafswisklsAEAKMAIR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 139 KCKLIVLQ----LEVQLETVYHAIEFGKKNGIEVL---------LIR--------LRHCVSRyvyackCDFFIPNETELE 197
Cdd:PLN02341 224 QSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFfdpgprgksLLVgtpderraLEHLLRM------SDVLLLTSEEAE 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13469792 198 ILTGMSVDTydhirLAARSLVDKGLNN--IIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 264
Cdd:PLN02341 298 ALTGIRNPI-----LAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAA 361
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
12-275 |
7.21e-11 |
|
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: 61.60 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMpkegetleAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 91
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM--------YP------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 VEKVPcTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIvlqlevqletvyHAIEFGKKNGIEVLLI 171
Cdd:cd01940 68 CRVKE-GENAVADVELVDGDRIFGLSNKGGVAREHPFEADLEY--LSQFDLV------------HTGIYSHEGHLEKALQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 172 RLRHCVSRYVYAC-------KCDFFIPNeTELEILTGMSVDTyDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVH 244
Cdd:cd01940 133 ALVGAGALISFDFsdrwdddYLQLVCPY-VDFAFFSASDLSD-EEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYS 210
|
250 260 270
....*....|....*....|....*....|.
gi 13469792 245 VPAFKVNAVDTSGAGDAFIGCFSHYYVQSGD 275
Cdd:cd01940 211 VAPRPVEVVDTLGAGDSFIAGFLLSLLAGGT 241
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
191-264 |
1.33e-09 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 58.17 E-value: 1.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13469792 191 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 264
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVG 259
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
185-277 |
3.73e-09 |
|
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: 56.69 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 185 KCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT-------MSEK-GALWMTRDQEVHVPAFKVNaVDTS 256
Cdd:COG2240 138 LADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtPADKiGNLAVTADGAWLVETPLLP-FSPN 216
|
90 100
....*....|....*....|.
gi 13469792 257 GAGDAFIGCFSHYYVQSGDVE 277
Cdd:COG2240 217 GTGDLFAALLLAHLLRGKSLE 237
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
12-272 |
5.37e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 56.53 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMPKEGETlEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 91
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADS-NPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 VEKVP--CTSSGVAPIfvnANSSNSILIIKGAN--KFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIE 167
Cdd:PRK09850 86 CLIVPgeNTSSYLSLL---DNTGEMLVAINDMNisNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAANVPVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 168 VLLIRLRHCVSRYVYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVH-VP 246
Cdd:PRK09850 163 VDPVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGwSA 242
|
250 260
....*....|....*....|....*.
gi 13469792 247 AFKVNAVDTSGAGDAFIGCFSHYYVQ 272
Cdd:PRK09850 243 PIKTNVINVTGAGDAMMAGLASCWVD 268
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
12-266 |
1.11e-08 |
|
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: 55.12 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGkGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTy 91
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDR---AAEDL-------------KKCKLIVLQLEVQLETVY 155
Cdd:cd01944 80 LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATltvAPYDYvylsgytlasenaSKVILLEWLEALPAGTTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 156 hAIEFGKKNGI--EVLLIRLRHCvsRYVYACkcdffipNETELEILTGmsvdTYD-HIRLAARSLVDKGLNNIIVTMSEK 232
Cdd:cd01944 160 -VFDPGPRISDipDTILQALMAK--RPIWSC-------NREEAAIFAE----RGDpAAEASALRIYAKTAAPVVVRLGSN 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 13469792 233 GAlWM--TRDQEVHVPAFKVNAVDTSGAGDAFIGCF 266
Cdd:cd01944 226 GA-WIrlPDGNTHIIPGFKVKAVDTIGAGDTHAGGM 260
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
185-276 |
2.04e-08 |
|
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: 54.39 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 185 KCDFFIPNETELEILTGMsvdtYDHIRlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAV-DTSGAGDAFI 263
Cdd:cd01946 163 KVDVVIINDGEARQLTGA----ANLVK-AARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDTFA 237
|
90
....*....|...
gi 13469792 264 GCFSHYYVQSGDV 276
Cdd:cd01946 238 GGFIGYLASQKDT 250
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
10-266 |
6.09e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 52.82 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 10 MDIAVIGSNMVDLitytnqMPKEGEtleapAFKigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINT 89
Cdd:PRK09813 1 KKLATIGDNCVDI------YPQLGK-----AFS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 90 TYVEkvpcTSSGVAPI-FVNANSSNSIL--IIKG--ANKFLSPEDIDRAAE-DLkkcklivlqlevqletVYHAIeFGKk 163
Cdd:PRK09813 67 SHVH----TKHGVTAQtQVELHDNDRVFgdYTEGvmADFALSEEDYAWLAQyDI----------------VHAAI-WGH- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 164 ngIEVLLIRLRHCVSRYVYackcDFFIPNETELEILTGMSVD---TYDH-----IRLAARSLVDKGLNNIIVTMSEKGAL 235
Cdd:PRK09813 125 --AEDAFPQLHAAGKLTAF----DFSDKWDSPLWQTLVPHLDyafASAPqedefLRLKMKAIVARGAGVVIVTLGENGSI 198
|
250 260 270
....*....|....*....|....*....|.
gi 13469792 236 WMTRDQEVHVPAFKVNAVDTSGAGDAFIGCF 266
Cdd:PRK09813 199 AWDGAQFWRQAPEPVTVVDTMGAGDSFIAGF 229
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
190-277 |
1.70e-07 |
|
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: 51.43 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 190 IPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT------MSEKGALWMTRDQ--EVHVPAFKVNAvDTSGAGDA 261
Cdd:cd01173 141 TPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEawLVQRPKIPFPA-YFNGTGDL 219
|
90
....*....|....*.
gi 13469792 262 FIGCFSHYYVQSGDVE 277
Cdd:cd01173 220 FAALLLARLLKGKSLA 235
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
135-266 |
2.55e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 51.33 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 135 EDLKKCKLIVLQLEVQ-LETVYHAIEFGKKNGIEVLL-------IR-LRHCVSRYVYACKCDFFIPNETE-LEILTGMSV 204
Cdd:PLN02379 173 EDFKGSKWLVLRYGFYnLEVIEAAIRLAKQEGLSVSLdlasfemVRnFRSPLLQLLESGKIDLCFANEDEaRELLRGEQE 252
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13469792 205 DTYDhirlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFK-VNAVDTSGAGDAFIGCF 266
Cdd:PLN02379 253 SDPE----AALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAVDATGAGDLFASGF 311
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
12-277 |
2.64e-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: 50.86 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITyTNQMPKegetleapafkIGCGGKGANQAVAAAKLNSKVLMLTKVGDD------IFADNTIRNLESW 85
Cdd:cd01937 2 IVIIGHVTIDEIV-TNGSGV-----------VKPGGPATYASLTLSRLGLTVKLVTKVGRDypdkwsDLFDNGIEVISLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 86 GINTTYVEKVPCTSS--------GVAPIFVNANSSnsilIIKGANKFLSP--EDIDRaaEDLKKCKLIVLQLEVQLEtvy 155
Cdd:cd01937 70 STETTTFELNYTNEGrtrtllakCAAIPDTESPLS----TITAEIVILGPvpEEISP--SLFRKFAFISLDAQGFLR--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 156 haiEFGKKNGIevllirlrhcvsRYVYACKCDFFIPNETELE-ILTGMSvdtydhirlAARSLVDKGLNNIIVTMSEKGA 234
Cdd:cd01937 141 ---RANQEKLI------------KCVILKLHDVLKLSRVEAEvISTPTE---------LARLIKETGVKEIIVTDGEEGG 196
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13469792 235 LWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:cd01937 197 YIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIK 239
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
225-277 |
4.65e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 50.58 E-value: 4.65e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 13469792 225 IIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVP 258
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
191-264 |
1.15e-06 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 49.40 E-value: 1.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13469792 191 PNETELEILTGMSVDTYDHIRLAARSLVDKG-LNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 264
Cdd:PRK10294 186 PNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVG 260
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
191-262 |
1.46e-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: 45.41 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 191 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVtmseKGA---------LWMTRDQEVHVPAFKVNAVDTSGAGDA 261
Cdd:COG0351 132 PNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLV----KGGhlpgdeavdVLYDGDGVREFSAPRIDTGNTHGTGCT 207
|
.
gi 13469792 262 F 262
Cdd:COG0351 208 L 208
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
191-262 |
1.61e-05 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 45.80 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 191 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTmSEKGA--------LWMTRDQeVHVPAFKVNAVDTSGAGDAF 262
Cdd:PRK08176 158 PNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVIT-SAAGNeenqemqvVVVTADS-VNVISHPRVDTDLKGTGDLF 235
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
34-262 |
2.95e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 45.18 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 34 ETLEAPAFKIGCGGKGANQAVAAAKLNSK--------VLMLTKVGDDIFADNTIRNLESWGINTTyVEKVPCTSSGVAPI 105
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHFL-SQPVKDGTTGTVIV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 106 FVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVLQ-----LEVQLETVYHAIEFGKKNGIEVLLIRLR-HCVSR 179
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSSTVNYDSCLASA--ISKSRVLVVEgylweLPQTIEAIAQACEEAHRAGALVAVTASDvSCIER 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 180 Y------VYACKCDFFIPNETELEILTGMSVDTydhirlaARSLVDKGLNN----IIVTMSEKGALWMTRDQEVHVPAFK 249
Cdd:PLN02813 271 HrddfwdVMGNYADILFANSDEARALCGLGSEE-------SPESATRYLSHfcplVSVTDGARGSYIGVKGEAVYIPPSP 343
|
250
....*....|...
gi 13469792 250 VNAVDTSGAGDAF 262
Cdd:PLN02813 344 CVPVDTCGAGDAY 356
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
12-275 |
5.91e-05 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 43.93 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 12 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 91
Cdd:cd01939 2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 92 V----EKVPCTSSgvapIFVNANSSNSILIIKGANKFLSPEDIDRAaeDLKKCKLIVLQ---LEVQLETVYHAIEFGKKN 164
Cdd:cd01939 82 CyrkdIDEPASSY----IIRSRAGGRTTIVNDNNLPEVTYDDFSKI--DLTQYGWIHFEgrnPDETLRMMQHIEEHNNRR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 165 G-----IEVLLIRLRHCVsrYVYACKCDFFIPNETELEILTGMSVDTydhiRLAARSLVDKGLNNIIVTMSEKGALWMTR 239
Cdd:cd01939 156 PeiritISVEVEKPREEL--LELAAYCDVVFVSKDWAQSRGYKSPEE----CLRGEGPRAKKAALLVCTWGDQGAGALGP 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 13469792 240 DQE-VHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGD 275
Cdd:cd01939 230 DGEyVHSPAHKpIRVVDTLGAGDTFNAAVIYALNKGPD 267
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
191-262 |
1.05e-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: 42.85 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13469792 191 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT---MSEKGA----LWMTRDQEVHVPAFKVNAVDTSGAGDAF 262
Cdd:pfam08543 125 PNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghLEGEEAvvtdVLYDGGGFYTLEAPRIPTKNTHGTGCTL 203
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
28-277 |
1.59e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 42.71 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 28 QMPKEGETLEAPAFKIGCGGKGANQA-VAAAKL---NSKVLMLTKVGDDIFADNTIRNLESWGINTT--YVEKVPctsSG 101
Cdd:PTZ00247 44 QLPIFEELESIPNVSYVPGGSALNTArVAQWMLqapKGFVCYVGCVGDDRFAEILKEAAEKDGVEMLfeYTTKAP---TG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 102 VAPIFVNaNSSNSILIIKGANKFLSPEDIDRAA--EDLKKCKLIVLQ---LEVQLETVYHAIEFGKKNGI---------- 166
Cdd:PTZ00247 121 TCAVLVC-GKERSLVANLGAANHLSAEHMQSHAvqEAIKTAQLYYLEgffLTVSPNNVLQVAKHARESGKlfclnlsapf 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 167 ------EVLLIRLRHCvsryvyackcDFFIPNETELEIL-TGMSVDTYDHIRLAARSLVDKGLNN-----IIVTMSEKGA 234
Cdd:PTZ00247 200 isqfffERLLQVLPYV----------DILFGNEEEAKTFaKAMKWDTEDLKEIAARIAMLPKYSGtrprlVVFTQGPEPT 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 13469792 235 LWMTRDQEVHVPAFKVNA---VDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:PTZ00247 270 LIATKDGVTSVPVPPLDQekiVDTNGAGDAFVGGFLAQYANGKDID 315
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
46-275 |
4.63e-04 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 41.46 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 46 GGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKVPCTSSGVAPIFVNANSSnSILIIKGAN--K 123
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDE-TVLAINDTHilQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 124 FLSPEDIDrAAEDLKKCKLIVLqleVQLETVYHAIE--FGKKNGIEVLL--------IRLRHCVSRyVYACKcdffiPNE 193
Cdd:PRK09954 172 QLTPQLLN-GSRDLIRHAGVVL---ADCNLTAEALEwvFTLADEIPVFVdtvsefkaGKIKHWLAH-IHTLK-----PTQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 194 TELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE---VHVPAFKVnaVDTSGAGDAFIGCFSHYY 270
Cdd:PRK09954 242 PELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEqflLTAPAHTT--VDSFGADDGFMAGLVYSF 319
|
....*
gi 13469792 271 VQSGD 275
Cdd:PRK09954 320 LEGYS 324
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
187-277 |
1.43e-03 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 39.85 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 187 DFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT-------MSEK-GALWMTRDQEVHVPAFKV-NAVDTSG 257
Cdd:PRK05756 140 DIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragyPADRfEMLLVTADGAWHISRPLVdFMRQPVG 219
|
90 100
....*....|....*....|
gi 13469792 258 AGDAFIGCFSHYYVQSGDVE 277
Cdd:PRK05756 220 VGDLTSALFLARLLQGGSLE 239
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
187-228 |
1.95e-03 |
|
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273221 [Multi-domain] Cd Length: 287 Bit Score: 39.43 E-value: 1.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 13469792 187 DFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT 228
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT 181
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
185-277 |
7.17e-03 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 37.71 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13469792 185 KCDFFIPNETELEILTGMSVDT---------YDHIRLAARSLvDKGLNNIIVTMSEKGALWMTRDQ--EVHVPAF----- 248
Cdd:cd01943 180 RVDVFSPNLEEAARLLGLPTSEpssdeekeaVLQALLFSGIL-QDPGGGVVLRCGKLGCYVGSADSgpELWLPAYhtkst 258
|
90 100
....*....|....*....|....*....
gi 13469792 249 KVnaVDTSGAGDAFIGCFSHYYVQSGDVE 277
Cdd:cd01943 259 KV--VDPTGGGNSFLGGFAAGLALTKSID 285
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
191-262 |
8.33e-03 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 37.03 E-value: 8.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13469792 191 PNETELEILTGMSV-DTYDHIRLAARSLVDKGLNNIIVT---MSEKGA---LWMTRDQEVHVPAFKVNAVDTSGAGDAF 262
Cdd:PRK06427 139 PNLPEAEALTGLPIaDTEDEMKAAARALHALGCKAVLIKgghLLDGEEsvdWLFDGEGEERFSAPRIPTKNTHGTGCTL 217
|
|
| |
