|
Name |
Accession |
Description |
Interval |
E-value |
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
7-299 |
4.16e-136 |
|
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: 386.96 E-value: 4.16e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 7 GSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKV 86
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 87 PCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLLNPAPA 166
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 167 LRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVD 246
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1531161233 247 TSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 299
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
2-294 |
2.26e-132 |
|
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: 377.66 E-value: 2.26e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLL 161
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 162 NPAPAlRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFK 241
Cdd:cd01174 161 NPAPA-RPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1531161233 242 VNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPS 294
Cdd:cd01174 240 VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
2-299 |
4.53e-94 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 281.63 E-value: 4.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:PTZ00292 17 DVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 82 YVEKVPCTSSGVAPIFVN-ANSSNSILIIKGANKFLSPEDIDRAAEDL-KKCKLIVLQLEVQLETVYHAIEFGKKNGIEV 159
Cdd:PTZ00292 97 FVSRTENSSTGLAMIFVDtKTGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGCYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 160 LLNPAPALRELDMSYACKC----DFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE- 234
Cdd:PTZ00292 177 VFNPAPAPKLAEVEIIKPFlkyvSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEp 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1531161233 235 VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 299
Cdd:PTZ00292 257 VHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELP 321
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-298 |
1.42e-82 |
|
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: 251.34 E-value: 1.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVLQL-----EVQLETVYHAIEFGKKNG 156
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 157 IEVLLNPA------PALRELDMSYACKCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDKGLNNIIVTMSEKGALWMT 230
Cdd:COG0524 159 VPVSLDPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1531161233 231 RDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQF 298
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
3-303 |
8.15e-72 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 223.98 E-value: 8.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:PRK11142 5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLLN 162
Cdd:PRK11142 85 VSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 163 PAPAlRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKV 242
Cdd:PRK11142 165 PAPA-RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1531161233 243 NAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFNEFLT 303
Cdd:PRK11142 244 QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
2-269 |
7.16e-57 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 185.24 E-value: 7.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 2 DIAVIGSNMVDLITYTNQMPkeGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIV----LQLEVQLETVYHAIEFGKKNGI 157
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYisgsLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 158 E--VLLNPAPALRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV 235
Cdd:pfam00294 159 FdpNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1531161233 236 HVPAF-KVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:pfam00294 239 HVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLE 273
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
2-269 |
1.98e-41 |
|
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: 145.03 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 2 DIAVIGSNMVDLitytnqMPKEGETLE-APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINT 80
Cdd:cd01166 1 DVVTIGEVMVDL------SPPGGGRLEqADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 81 TYVEKVPCTSSGVAPIFVNANSSNSILI-IKG-ANKFLSPEDIDRAAedLKKCKLIVL------QLEVQLETVYHAIEFG 152
Cdd:cd01166 75 SHVRVDPGRPTGLYFLEIGAGGERRVLYyRAGsAASRLTPEDLDEAA--LAGADHLHLsgitlaLSESAREALLEALEAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 153 KKNGIEVL--LNPAPALR-ELDMSYAC-----KCDFFIPNETELEILTGMSVDTydhiRLAARSL-VDKGLNNIIVTMSE 223
Cdd:cd01166 153 KARGVTVSfdLNYRPKLWsAEEAREALeellpYVDIVLPSEEEAEALLGDEDPT----DAAERALaLALGVKAVVVKLGA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1531161233 224 KGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01166 229 EGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLE 274
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
2-269 |
1.18e-38 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 137.44 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 82 YVEKVPCTSSGVApiFVNANSSNSILII--KGANKFLSPEDIDRAAEDLKkckliVLQLEVQLETVYHAIEFgKKNGIEV 159
Cdd:cd01942 81 HVRVVDEDSTGVA--FILTDGDDNQIAYfyPGAMDELEPNDEADPDGLAD-----IVHLSSGPGLIELAREL-AAGGITV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 160 LLNPAPALRELDMSYA----CKCDFFIPNETELEILtgmsvdtydhIRLAARSL--VDKGLNNIIVTMSEKGALWMTRDQ 233
Cdd:cd01942 153 SFDPGQELPRLSGEELeeilERADILFVNDYEAELL----------KERTGLSEaeLASGVRVVVVTLGPKGAIVFEDGE 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 1531161233 234 EVHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01942 223 EVEVPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYDLE 259
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
6-294 |
8.30e-33 |
|
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: 122.40 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 6 IGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDD-----IFADntirnLESWGINT 80
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDaigrlILAE-----LAAEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 81 TYVEKVPCTSSGVAPIFVNANSSNSILIIKGANKF----LSPEDIDRAAedlkkcklIVLQLEVQLETVYHAIEFGKKNG 156
Cdd:cd01945 80 SFIVVAPGARSPISSITDITGDRATISITAIDTQAapdsLPDAILGGAD--------AVLVDGRQPEAALHLAQEARARG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 157 IEVLLN----PAPALRELdmsyACKCDFFIPNETELEILTGMSVDtydhirLAARSLVDKGLNNIIVTMSEKGALWMTRD 232
Cdd:cd01945 152 IPIPLDldggGLRVLEEL----LPLADHAICSENFLRPNTGSADD------EALELLASLGIPFVAVTLGEAGCLWLERD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1531161233 233 QEV-HVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPS 294
Cdd:cd01945 222 GELfHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-256 |
5.65e-31 |
|
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: 117.74 E-value: 5.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITytNQMPKEGETLEAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:cd01167 2 VVCFGEALIDFIP--EGSGAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAeDLKKCKL-----IVLQLEVQLETVYHAIEFGKKNGI 157
Cdd:cd01167 74 IQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPD-LLSEADIlhfgsIALASEPSRSALLELLEAAKKAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 158 EVLLNP---------APALRELDMSYACKCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDKGLNNIIVTMSEKGALW 228
Cdd:cd01167 153 LISFDPnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALL 227
|
250 260
....*....|....*....|....*...
gi 1531161233 229 MTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:cd01167 228 YTKGGVGEVPGIPVEVVDTTGAGDAFVA 255
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-269 |
2.12e-28 |
|
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: 111.17 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 1 MDIAVIGSNMVDLITYTN-----------------QMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDD 63
Cdd:cd01168 2 YDVLGLGNALVDILAQVDdafleklglkkgdmilaDMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 64 IFADNTIRNLESWGINTTYVEKvPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVL---QLEV 140
Cdd:cd01168 82 KLGDFLLKDLRAAGVDTRYQVQ-PDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSL--LAKAKYLYLegyLLTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 141 QLETVYHAIEFGKKNGIEVLLN-PAP--------ALRELdmsyACKCDFFIPNETELEILTGMSVDtydHIRLAARSLVD 211
Cdd:cd01168 159 PPEAILLAAEHAKENGVKIALNlSAPfivqrfkeALLEL----LPYVDILFGNEEEAEALAEAETT---DDLEAALKLLA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1531161233 212 KGLNNIIVTMSEKGALWMTRDQEVHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01168 232 LRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEPLE 290
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
1-269 |
6.30e-28 |
|
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: 109.61 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 1 MDIAVIGSNMVDLitYTNQMpkeGETLE-APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGIN 79
Cdd:TIGR04382 2 LDVITIGRVGVDL--YPQQI---GVPLEdVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 80 TTYVEKVPCTSSGVApifvnanssnsILIIKGANKF-------------LSPEDIDraAEDLKKCKLIV-----LQLEVQ 141
Cdd:TIGR04382 77 TSHVVTDPGRRTSLV-----------FLEIKPPDEFpllfyrenaadlaLTPDDVD--EDYIASARALLvsgtaLSQEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 142 LETVYHAIEFGKKNGIEVLL----------NPAPALRELDMSYAcKCDFFIPNETELEILTGMSVDtydhiRLAARSLVD 211
Cdd:TIGR04382 144 REAVLKALEYARAAGVRVVLdidyrpylwkSPEEAGIYLRLVLP-LVDVIIGTREEFDIAGGEGDD-----EAAARALLD 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1531161233 212 KGLNNIIVTMSEKGALWMTRDQE-VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:TIGR04382 218 AGVEILVVKRGPEGSLVYTGDGEgVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLE 276
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-269 |
5.31e-27 |
|
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: 107.01 E-value: 5.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMPKEGETLEAPAfKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTy 82
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTSNPGHV-KQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 vekvPCTSSGVA-PIFVNANSSNSILIIKGAN----KFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGI 157
Cdd:cd01941 80 ----GIVFEGRStASYTAILDKDGDLVVALADmdiyELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 158 EVLLNPAPALRELDMSYACK-CDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV- 235
Cdd:cd01941 156 PVAFEPTSAPKLKKLFYLLHaIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVe 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1531161233 236 --HVPAFKV-NAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01941 236 tkLFPAPQPeTVVNVTGAGDAFVAGLVAGLLEGMSLD 272
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
3-263 |
4.44e-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: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLnskvlmltkvgddifadntirnleswgintty 82
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 vekvpctssGVAPIFVNAnssnSILIIKGANkflspedidraaedlkkcklivLQLEVQLETVYHAIEFGKKngieVLLN 162
Cdd:cd00287 50 ---------GVSVTLVGA----DAVVISGLS----------------------PAPEAVLDALEEARRRGVP----VVLD 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 163 PAPALRELD----MSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRD-QEVHV 237
Cdd:cd00287 91 PGPRAVRLDgeelEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGgTEVHV 170
|
250 260
....*....|....*....|....*.
gi 1531161233 238 PAFKVNAVDTSGAGDAFIGCFSHYYV 263
Cdd:cd00287 171 PAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
3-259 |
6.61e-25 |
|
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: 101.48 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQmpkEGETLEAP--AFKIG-----CGGkGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLES 75
Cdd:cd01172 2 VLVVGDVILDEYLYGDV---ERISPEAPvpVVKVEreeirLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 76 WGINTTYVekvpcTSSGVAPIFVNAnssnsilIIKGANK-----FLSPEDIDRAAED---------LKKCKLIVLQ---- 137
Cdd:cd01172 78 EGIDTDGI-----VDEGRPTTTKTR-------VIARNQQllrvdREDDSPLSAEEEQrlieriaerLPEADVVILSdygk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 138 --LEVQLetVYHAIEFGKKNGIEVLLNPapalRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDK-GL 214
Cdd:cd01172 146 gvLTPRV--IEALIAAARELGIPVLVDP----KGRDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1531161233 215 NNIIVTMSEKGALWMTRDQEV-HVPAFKVNAVDTSGAGDAFIGCFS 259
Cdd:cd01172 220 EALLVTLGEEGMTLFERDGEVqHIPALAKEVYDVTGAGDTVIATLA 265
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
11-269 |
1.08e-22 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 95.59 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 11 VDLITYTNQMpKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDdiFADNTIRN-LESWGINTTYVEkvpct 89
Cdd:COG1105 10 LDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGG--FTGEFIEElLDEEGIPTDFVP----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 90 ssgVAP-----IFVNANSSNSILIIKGANKFLSPEDIDRAAEDL----KKCKLIVL----------QLEVQLetvyhaIE 150
Cdd:COG1105 82 ---IEGetrinIKIVDPSDGTETEINEPGPEISEEELEALLERLeellKEGDWVVLsgslppgvppDFYAEL------IR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 151 FGKKNGIEVLLN-PAPALRE-LDMS-YACKcdffiPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGAL 227
Cdd:COG1105 153 LARARGAKVVLDtSGEALKAaLEAGpDLIK-----PNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGAL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1531161233 228 WMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:COG1105 228 LVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLE 269
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
11-269 |
1.44e-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: 86.86 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 11 VDLITYTNQMpKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLML----TKVGDDIFAdntirNLESWGINTTYVEKV 86
Cdd:TIGR03168 10 IDLTIEVDGL-TPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATgflgGFTGEFIEA-----LLAEEGIKNDFVEVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 87 PCTSSGVApiFVNANSSNSILIIKGANkfLSPEDIDRAAED----LKKCKLIV----LQLEVQLETVYHAIEFGKKNGIE 158
Cdd:TIGR03168 84 GETRINVK--IKESSGEETELNEPGPE--ISEEELEQLLEKlrelLASGDIVVisgsLPPGVPPDFYAQLIAIARKKGAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 159 VLLNPA-PALRE-LDMS-YACKcdffiPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV 235
Cdd:TIGR03168 160 VILDTSgEALREaLAAKpFLIK-----PNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGAL 234
|
250 260 270
....*....|....*....|....*....|....
gi 1531161233 236 HVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:TIGR03168 235 KATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLE 268
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
11-269 |
1.20e-18 |
|
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: 84.12 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 11 VDLITYTNQmPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDiFADNTIRNLESWGINTTYVEkvpctS 90
Cdd:cd01164 11 IDLTIELDQ-LQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE-----V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 91 SGVAPIFVN-ANSSNSILIIKGANKFLSPEDIDRAAEDLK----KCKLIVL----------QLEVQLetvyhaIEFGKKN 155
Cdd:cd01164 84 AGETRINVKiKEEDGTETEINEPGPEISEEELEALLEKLKallkKGDIVVLsgslppgvpaDFYAEL------VRLAREK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 156 GIEVLLNPA-PALRELdmsYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE 234
Cdd:cd01164 158 GARVILDTSgEALLAA---LAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGV 234
|
250 260 270
....*....|....*....|....*....|....*
gi 1531161233 235 VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01164 235 YRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLE 269
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
3-260 |
4.73e-18 |
|
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: 82.08 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGI-NTT 81
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDkHTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 82 YVEKVPctsSGVAPIFVNANSSNSILIIKGANKFLSPEDIdraaedLKKCKLIVLQLEVQLETVYHAIEFGKKngieVLL 161
Cdd:cd01947 82 AWRDKP---TRKTLSFIDPNGERTITVPGERLEDDLKWPI------LDEGDGVFITAAAVDKEAIRKCRETKL----VIL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 162 NPAPALRELDMSYACK-CDFFIPNETELEILTGMSVDtydhirlaarslVDKGLNNIIVTMSEKGALWMTRDQEVHVPAF 240
Cdd:cd01947 149 QVTPRVRVDELNQALIpLDILIGSRLDPGELVVAEKI------------AGPFPRYLIVTEGELGAILYPGGRYNHVPAK 216
|
250 260
....*....|....*....|
gi 1531161233 241 KVNAVDTSGAGDAFIGCFSH 260
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIY 236
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
28-256 |
1.86e-17 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 81.21 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 28 EAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKVPCTSSGVAPIFVNANSSNSIL 107
Cdd:PLN02323 34 EAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 108 IIK--GANKFLSPEDIDraAEDLKKCKL-----IVLQLEVQLETVYHAIEFGKKNGIEVLLNP---------APALRELD 171
Cdd:PLN02323 114 FYRnpSADMLLRESELD--LDLIRKAKIfhygsISLITEPCRSAHLAAMKIAKEAGALLSYDPnlrlplwpsAEAAREGI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 172 MSYACKCDFFIPNETELEILTGmSVDTYDHirlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAG 251
Cdd:PLN02323 192 MSIWDEADIIKVSDEEVEFLTG-GDDPDDD---TVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAG 267
|
....*
gi 1531161233 252 DAFIG 256
Cdd:PLN02323 268 DAFVG 272
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
3-267 |
8.70e-17 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 78.82 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLItytnqmP-KEGETLEAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:PRK09434 5 VWVLGDAVVDLI------PeGENRYLKCP------GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 82 YVEKVPC--TSSGVAPIFVNANSSNSILIIKGANKFLSPEDID--RAAEDLKKCKlIVLQLEVQLETVYHAIEFGKKNGI 157
Cdd:PRK09434 73 YLRLDPAhrTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPpfRQGEWLHLCS-IALSAEPSRSTTFEAMRRIKAAGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 158 EVLLNP---------APALRELDMSYACKCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDK-GLNNIIVTMSEKGAL 227
Cdd:PRK09434 152 FVSFDPnlredlwqdEAELRECLRQALALADVVKLSEEELCFLSGT-----SQLEDAIYALADRyPIALLLVTLGAEGVL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1531161233 228 WMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:PRK09434 227 VHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGL 266
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
1-256 |
1.52e-16 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 79.49 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 1 MDIAVIGSNMVDLITYTNQMP-----KEGETLE-----APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTI 70
Cdd:PLN02341 73 IDVATLGNLCVDIVLPVPELPppsreERKAYMEelaasPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 71 RNLESWGINTtyVEKVPCTSSGVApifVNANSSNSI--LIIKGANK--FLSPEDI-------------DRAAEDLKKCKL 133
Cdd:PLN02341 153 DVLAEEGISV--VGLIEGTDAGDS---SSASYETLLcwVLVDPLQRhgFCSRADFgpepafswisklsAEAKMAIRQSKA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 134 IVLQ----LEVQLETVYHAIEFGKKNGIEVLLNPAP--------------ALRE-LDMSyackcDFFIPNETELEILTGM 194
Cdd:PLN02341 228 LFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgksllvgtpderrALEHlLRMS-----DVLLLTSEEAEALTGI 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1531161233 195 SVDTydhirLAARSLVDKGLNN--IIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:PLN02341 303 RNPI-----LAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAA 361
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
3-267 |
5.32e-12 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 64.68 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMpkegetleAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM--------YP------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 VEKVPcTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIvlqlevqletvyHAIEFGKKNGIEVLL- 161
Cdd:cd01940 68 CRVKE-GENAVADVELVDGDRIFGLSNKGGVAREHPFEADLEY--LSQFDLV------------HTGIYSHEGHLEKALq 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 162 --NPAPALRELDMSY---ACKCDFFIPNeTELEILTGMSVDTyDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVH 236
Cdd:cd01940 133 alVGAGALISFDFSDrwdDDYLQLVCPY-VDFAFFSASDLSD-EEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYS 210
|
250 260 270
....*....|....*....|....*....|.
gi 1531161233 237 VPAFKVNAVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:cd01940 211 VAPRPVEVVDTLGAGDSFIAGFLLSLLAGGT 241
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-258 |
2.32e-11 |
|
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: 63.21 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGkGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTy 82
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDR---AAEDL---------KKCKLIVLQLEVQLETvyhaie 150
Cdd:cd01944 80 LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATltvAPYDYvylsgytlaSENASKVILLEWLEAL------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 151 fgkKNGIEVLLNPAPALRELD---MSYACKCDFFIP-NETELEILTGmsvdTYD-HIRLAARSLVDKGLNNIIVTMSEKG 225
Cdd:cd01944 154 ---PAGTTLVFDPGPRISDIPdtiLQALMAKRPIWScNREEAAIFAE----RGDpAAEASALRIYAKTAAPVVVRLGSNG 226
|
250 260 270
....*....|....*....|....*....|....*
gi 1531161233 226 AlWM--TRDQEVHVPAFKVNAVDTSGAGDAFIGCF 258
Cdd:cd01944 227 A-WIrlPDGNTHIIPGFKVKAVDTIGAGDTHAGGM 260
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
183-256 |
1.25e-09 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 58.17 E-value: 1.25e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1531161233 183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVG 259
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
177-269 |
4.64e-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: 56.31 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 177 KCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT-------MSEK-GALWMTRDQEVHVPAFKVNaVDTS 248
Cdd:COG2240 138 LADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtPADKiGNLAVTADGAWLVETPLLP-FSPN 216
|
90 100
....*....|....*....|.
gi 1531161233 249 GAGDAFIGCFSHYYVQSGDVE 269
Cdd:COG2240 217 GTGDLFAALLLAHLLRGKSLE 237
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
165-269 |
8.02e-09 |
|
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: 55.28 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 165 PALRELDMSYAckcDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT------MSEKGALWMTRDQ--EVH 236
Cdd:cd01173 127 PVYRDLLVPLA---DIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEawLVQ 203
|
90 100 110
....*....|....*....|....*....|...
gi 1531161233 237 VPAFKVNAvDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01173 204 RPKIPFPA-YFNGTGDLFAALLLARLLKGKSLA 235
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
3-264 |
8.50e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 55.76 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMPKEGETlEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADS-NPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 VEKVP--CTSSGVAPIfvnANSSNSILIIKGAN--KFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKngIE 158
Cdd:PRK09850 86 CLIVPgeNTSSYLSLL---DNTGEMLVAINDMNisNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAAN--VP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 159 VLLNPAPALRELDM-SYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVH- 236
Cdd:PRK09850 161 VFVDPVSAWKCVKVrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGw 240
|
250 260
....*....|....*....|....*...
gi 1531161233 237 VPAFKVNAVDTSGAGDAFIGCFSHYYVQ 264
Cdd:PRK09850 241 SAPIKTNVINVTGAGDAMMAGLASCWVD 268
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
126-258 |
1.47e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 55.18 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 126 EDLKKCKLIVLQLEVQ-LETVYHAIEFGKKNGI---------EVLLNPAPALRELDMSYacKCDFFIPNETE-LEILTGM 194
Cdd:PLN02379 173 EDFKGSKWLVLRYGFYnLEVIEAAIRLAKQEGLsvsldlasfEMVRNFRSPLLQLLESG--KIDLCFANEDEaRELLRGE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1531161233 195 SVDTYDhirlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFK-VNAVDTSGAGDAFIGCF 258
Cdd:PLN02379 251 QESDPE----AALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAVDATGAGDLFASGF 311
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
177-268 |
2.51e-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: 54.01 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 177 KCDFFIPNETELEILTGMsvdtYDHIRlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAV-DTSGAGDAFI 255
Cdd:cd01946 163 KVDVVIINDGEARQLTGA----ANLVK-AARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDTFA 237
|
90
....*....|...
gi 1531161233 256 GCFSHYYVQSGDV 268
Cdd:cd01946 238 GGFIGYLASQKDT 250
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
1-258 |
3.24e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 53.59 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 1 MDIAVIGSNMVDLitytnqMPKEGEtleapAFKigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINT 80
Cdd:PRK09813 1 KKLATIGDNCVDI------YPQLGK-----AFS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 81 TYVEkvpcTSSGVAPI-FVNANSSNSIL--IIKG--ANKFLSPEDIDRAAE-DLkkcklivlqlevqletVYHAIeFGKK 154
Cdd:PRK09813 67 SHVH----TKHGVTAQtQVELHDNDRVFgdYTEGvmADFALSEEDYAWLAQyDI----------------VHAAI-WGHA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 155 NgiEVLlnpaPALRE----LDMSYACKCDffipneTELEILTGMSVD---TYDH-----IRLAARSLVDKGLNNIIVTMS 222
Cdd:PRK09813 126 E--DAF----PQLHAagklTAFDFSDKWD------SPLWQTLVPHLDyafASAPqedefLRLKMKAIVARGAGVVIVTLG 193
|
250 260 270
....*....|....*....|....*....|....*.
gi 1531161233 223 EKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCF 258
Cdd:PRK09813 194 ENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGF 229
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
3-267 |
3.45e-07 |
|
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: 50.87 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:cd01939 2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 83 V----EKVPCTSSgvapIFVNANSSNSILIIKGANKFLSPEDIDRAaeDLKKCKLIVLQ---LEVQLETVYHAIEFGKKN 155
Cdd:cd01939 82 CyrkdIDEPASSY----IIRSRAGGRTTIVNDNNLPEVTYDDFSKI--DLTQYGWIHFEgrnPDETLRMMQHIEEHNNRR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 156 GIEV------LLNPAPALRELdMSYackCDFFIPNETELEILTGMSVDTydhiRLAARSLVDKGLNNIIVTMSEKGALWM 229
Cdd:cd01939 156 PEIRitisveVEKPREELLEL-AAY---CDVVFVSKDWAQSRGYKSPEE----CLRGEGPRAKKAALLVCTWGDQGAGAL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1531161233 230 TRDQE-VHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:cd01939 228 GPDGEyVHSPAHKpIRVVDTLGAGDTFNAAVIYALNKGPD 267
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
217-269 |
4.31e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 50.58 E-value: 4.31e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1531161233 217 IIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVP 258
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
3-269 |
6.26e-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: 49.71 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 3 IAVIGSNMVDLITyTNQMPKegetleapafkIGCGGKGANQAVAAAKLNSKVLMLTKVGDD------IFADNTIRNLESW 76
Cdd:cd01937 2 IVIIGHVTIDEIV-TNGSGV-----------VKPGGPATYASLTLSRLGLTVKLVTKVGRDypdkwsDLFDNGIEVISLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 77 GINTTYVEKVPCTSS--------GVAPIFVNANSSnsilIIKGANKFLSP--EDIDRaaEDLKKCKLIVLQLEVQLEtvy 146
Cdd:cd01937 70 STETTTFELNYTNEGrtrtllakCAAIPDTESPLS----TITAEIVILGPvpEEISP--SLFRKFAFISLDAQGFLR--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 147 haiEFGKKNGIEVLLNPapalreldmsyacKCDFFIPNETELE-ILTGMSvdtydhirlAARSLVDKGLNNIIVTMSEKG 225
Cdd:cd01937 141 ---RANQEKLIKCVILK-------------LHDVLKLSRVEAEvISTPTE---------LARLIKETGVKEIIVTDGEEG 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1531161233 226 ALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01937 196 GYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIK 239
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
183-256 |
1.09e-06 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 49.40 E-value: 1.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1531161233 183 PNETELEILTGMSVDTYDHIRLAARSLVDKG-LNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:PRK10294 186 PNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVG 260
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
19-269 |
1.84e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 48.87 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 19 QMPKEGETLEAPAFKIGCGGKGANQA-VAAAKL---NSKVLMLTKVGDDIFADNTIRNLESWGINTT--YVEKVPctsSG 92
Cdd:PTZ00247 44 QLPIFEELESIPNVSYVPGGSALNTArVAQWMLqapKGFVCYVGCVGDDRFAEILKEAAEKDGVEMLfeYTTKAP---TG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 93 VAPIFVNaNSSNSILIIKGANKFLSPEDIDRAA--EDLKKCKLIVLQ---LEVQLETVYHAIEFGKKNGIEVLLN-PAP- 165
Cdd:PTZ00247 121 TCAVLVC-GKERSLVANLGAANHLSAEHMQSHAvqEAIKTAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPf 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 166 -------ALRELdMSYackCDFFIPNETELEIL-TGMSVDTYDHIRLAARSLVDKGLNN-----IIVTMSEKGALWMTRD 232
Cdd:PTZ00247 200 isqfffeRLLQV-LPY---VDILFGNEEEAKTFaKAMKWDTEDLKEIAARIAMLPKYSGtrprlVVFTQGPEPTLIATKD 275
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1531161233 233 QEVHVPAFKVNA---VDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:PTZ00247 276 GVTSVPVPPLDQekiVDTNGAGDAFVGGFLAQYANGKDID 315
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
183-254 |
1.54e-05 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 45.80 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTmSEKGA--------LWMTRDQeVHVPAFKVNAVDTSGAGDAF 254
Cdd:PRK08176 158 PNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVIT-SAAGNeenqemqvVVVTADS-VNVISHPRVDTDLKGTGDLF 235
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
183-254 |
1.95e-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: 45.03 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVtmseKGA---------LWMTRDQEVHVPAFKVNAVDTSGAGDA 253
Cdd:COG0351 132 PNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLV----KGGhlpgdeavdVLYDGDGVREFSAPRIDTGNTHGTGCT 207
|
.
gi 1531161233 254 F 254
Cdd:COG0351 208 L 208
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
183-254 |
1.28e-04 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 42.47 E-value: 1.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1531161233 183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT---MSEKGA----LWMTRDQEVHVPAFKVNAVDTSGAGDAF 254
Cdd:pfam08543 125 PNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghLEGEEAvvtdVLYDGGGFYTLEAPRIPTKNTHGTGCTL 203
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
25-254 |
1.94e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 42.49 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 25 ETLEAPAFKIGCGGKGANQAVAAAKLNSK--------VLMLTKVGDDIFADNTIRNLESWGINTTyVEKVPCTSSGVAPI 96
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHFL-SQPVKDGTTGTVIV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 97 FVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVLQ-----LEVQLETVYHAIEFGKKNGIEVLLNPA------- 164
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSSTVNYDSCLASA--ISKSRVLVVEgylweLPQTIEAIAQACEEAHRAGALVAVTASdvscier 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 165 --PALRELDMSYAckcDFFIPNETELEILTGMSVDTydhirlaARSLVDKGLNN----IIVTMSEKGALWMTRDQEVHVP 238
Cdd:PLN02813 271 hrDDFWDVMGNYA---DILFANSDEARALCGLGSEE-------SPESATRYLSHfcplVSVTDGARGSYIGVKGEAVYIP 340
|
250
....*....|....*.
gi 1531161233 239 AFKVNAVDTSGAGDAF 254
Cdd:PLN02813 341 PSPCVPVDTCGAGDAY 356
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
164-269 |
2.62e-04 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 41.78 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 164 APALRELDMSYAckcDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT-------MSEK-GALWMTRDQEV 235
Cdd:PRK05756 128 AEFLRDRALPAA---DIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragyPADRfEMLLVTADGAW 204
|
90 100 110
....*....|....*....|....*....|....*
gi 1531161233 236 HVPAFKV-NAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:PRK05756 205 HISRPLVdFMRQPVGVGDLTSALFLARLLQGGSLE 239
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
37-267 |
4.34e-04 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 41.46 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 37 GGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKVPCTSSGVAPIFVNANSSnSILIIKGAN--K 114
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDE-TVLAINDTHilQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 115 FLSPEDIDrAAEDLKKCKLIVLqleVQLETVYHAIE--FGKKNGIEVLLNPAPALRELDM-SYACKCDFFIPNETELEIL 191
Cdd:PRK09954 172 QLTPQLLN-GSRDLIRHAGVVL---ADCNLTAEALEwvFTLADEIPVFVDTVSEFKAGKIkHWLAHIHTLKPTQPELEIL 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1531161233 192 TGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE---VHVPAFKVnaVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:PRK09954 248 WGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEqflLTAPAHTT--VDSFGADDGFMAGLVYSFLEGYS 324
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
164-220 |
1.06e-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: 40.20 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1531161233 164 APALRELDMSYACK-CDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT 220
Cdd:TIGR00687 124 APDLLEVYREKAIPvADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT 181
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
148-254 |
1.97e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 38.89 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 148 AIEFGK-KNGIEVLLNPAPALREL-DMSYACKCDFFI----------PNETELEILTGMSVDTYDHIRLAARSLVDKGLN 215
Cdd:PRK12413 88 ALDFIKgHPGIPVVLDPVLVCKEThDVEVSELRQELIqffpyvtvitPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAK 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1531161233 216 NIIVT----MSEKGALWMTRD-QEVHVPAFKVNAVDTSGAGDAF 254
Cdd:PRK12413 168 AVVIKggnrLSQKKAIDLFYDgKEFVILESPVLEKNNIGAGCTF 211
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
40-269 |
4.24e-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: 38.48 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 40 GANQAVAAAKLNSKvLMLTKVGDDiFADNTIRNLESWGINTTYVEKVP-CTSSGVApIFVNAN-----SSNSILIIKGAN 113
Cdd:cd01943 35 GARLFLPPPLSRSI-SWIVDKGSD-FPKSVEDELESWGTGMVFRRDPGrLTTRGLN-IYDGNDrrffkYLTPKKRIDVSD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 114 KFLSPEDIDRAA----EDLKKCKLIVLQLEVQLETvyhaIEFGKKNGIEVLLNPAPALRE----LDMSYAC-KCDFFIPN 184
Cdd:cd01943 112 DLNSTPLIRSSCihliCSPERCASIVDDIINLFKL----LKGNSPTRPKIVWEPLPDSCDpenlEDLLQALpRVDVFSPN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531161233 185 ETELEILTGMSVDT---------YDHIRLAARSLvDKGLNNIIVTMSEKGALWMTRDQ--EVHVPAF-----KVnaVDTS 248
Cdd:cd01943 188 LEEAARLLGLPTSEpssdeekeaVLQALLFSGIL-QDPGGGVVLRCGKLGCYVGSADSgpELWLPAYhtkstKV--VDPT 264
|
250 260
....*....|....*....|.
gi 1531161233 249 GAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01943 265 GGGNSFLGGFAAGLALTKSID 285
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
183-254 |
9.31e-03 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 37.03 E-value: 9.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1531161233 183 PNETELEILTGMSVDTYDHI-RLAARSLVDKGLNNIIVT---MSEKGA---LWMTRDQEVHVPAFKVNAVDTSGAGDAF 254
Cdd:PRK06427 139 PNLPEAEALTGLPIADTEDEmKAAARALHALGCKAVLIKgghLLDGEEsvdWLFDGEGEERFSAPRIPTKNTHGTGCTL 217
|
|
| |
