|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-300 |
8.74e-141 |
|
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: 398.85 E-value: 8.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 5 VAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAF 84
Cdd:cd01174 2 VVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 85 VGQTADAVTGTASIIVNSEGQNVIVIVPGANLLLSSEDLKRASDIICKAKVAVCQLEITPAVSLEALKMARASGVKTLFN 164
Cdd:cd01174 82 VEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVILN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 165 PAPALADLdPEFYTHSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEpiPKHVPAE 244
Cdd:cd01174 162 PAPARPLP-AELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGE--VEHVPAF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 513175214 245 KVRAVDTTGAGDSFVGALAFYLAHYPELpvEEMVRKCNYIASVSVQASGTQSSYPY 300
Cdd:cd01174 239 KVKAVDTTGAGDTFIGALAAALARGLSL--EEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
9-305 |
1.37e-140 |
|
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: 398.51 E-value: 1.37e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 9 GSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQT 88
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 89 ADAVTGTASIIVNSEGQNVIVIVPGANLLLSSEDLKRASDIICKAKVAVCQLEITPAVSLEALKMARASGVKTLFNPAPA 168
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 169 LADLDPEFYTHSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEpiPKHVPAEKVRA 248
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 513175214 249 VDTTGAGDSFVGALAFYLAHYPelPVEEMVRKCNYIASVSVQASGTQSSYPYRKDLP 305
Cdd:TIGR02152 239 VDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-308 |
6.89e-114 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 332.09 E-value: 6.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 1 MAAEVAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGV 80
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 81 STAFVGQTADAVTGTASIIVNSE-GQNVIVIVPGANLLLSSEDLKRASDIICK-AKVAVCQLEITPAVSLEALKMARASG 158
Cdd:PTZ00292 94 NTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 159 VKTLFNPAPALADLDPE----FYTHSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVE 234
Cdd:PTZ00292 174 CYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKE 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 513175214 235 EPiPKHVPAEKVRAVDTTGAGDSFVGALAFYLAHypELPVEEMVRKCNYIASVSVQASGTQSSYPYRKDLPQDL 308
Cdd:PTZ00292 254 NE-PVHVPGKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPADV 324
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-304 |
4.09e-86 |
|
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: 260.59 E-value: 4.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 5 VAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAF 84
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 85 VGQTADAVTGTASIIVNSEGQNVIVIVPGANLLLSSEDLKRAsdIICKAKVAVCQL-----EITPAVSLEALKMARASGV 159
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEA--LLAGADILHLGGitlasEPPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 160 KTLFNPAPALADLDP------EFYTHSDIFCCNETEAEILTGIpvgnlEDTEKVGRLLLERGCKLVIVTLGAEGCMMISV 233
Cdd:COG0524 160 PVSLDPNYRPALWEParellrELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 513175214 234 EEPIpkHVPAEKVRAVDTTGAGDSFVGALAFYLAHypELPVEEMVRKCNYIASVSVQASGTQSSYPYRKDL 304
Cdd:COG0524 235 GEVV--HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
1-308 |
5.30e-78 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 239.77 E-value: 5.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 1 MAAEVAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGV 80
Cdd:PRK11142 1 TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 81 STAFVGQTADAVTGTASIIVNSEGQNVIVIVPGANLLLSSEDLKRASDIICKAKVAVCQLEiTPAVS-LEALKMARASGV 159
Cdd:PRK11142 81 DTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLE-TPLETvLAAAKIAKQHGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 160 KTLFNPAPAlADLDPEFYTHSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGcMMISVEEPiPK 239
Cdd:PRK11142 160 KVILNPAPA-RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRG-VWLSENGE-GQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 513175214 240 HVPAEKVRAVDTTGAGDSFVGALAFYLAHypELPVEEMVRKCNYIASVSVQASGTQSSYPYRKDLPQDL 308
Cdd:PRK11142 237 RVPGFRVQAVDTIAAGDTFNGALVTALLE--GKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-296 |
2.67e-66 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 209.51 E-value: 2.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 4 EVAVVGSCMTDLVSFTTRLPraGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTA 83
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 84 FVGQTADAVTGTASIIVNSEGQNVIVIVPGANLLLSSEDLKRASDIICKAKV----AVCQLEITPAVSLEALKMARASG- 158
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLlyisGSLPLGLPEATLEELIEAAKNGGt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 159 -VKTLFNPAPALADLDPEFYTHSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPI 237
Cdd:pfam00294 159 fDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 513175214 238 pKHVPAEKVRAVDTTGAGDSFVGALAFYLAHypELPVEEMVRKCNYIASVSVQASGTQS 296
Cdd:pfam00294 239 -HVPAVPKVKVVDTTGAGDSFVGGFLAGLLA--GKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-293 |
3.35e-43 |
|
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: 150.03 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 4 EVAVVGSCMTDLVsfttrlPRAGETILGQKFF-IGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVST 82
Cdd:cd01166 1 DVVTIGEVMVDLS------PPGGGRLEQADSFrKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 83 AFVGQTADAVTGTASIIVNSEGQNVIVIVPG--ANLLLSSEDLKRasDIICKAK-VAVCqlEITPAVS-------LEALK 152
Cdd:cd01166 75 SHVRVDPGRPTGLYFLEIGAGGERRVLYYRAgsAASRLTPEDLDE--AALAGADhLHLS--GITLALSesarealLEALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 153 MARASGVKTLF--NPAPALADLD------PEFYTHSDIFCCNETEAEILTGIPVgnLEDTEKVGRlLLERGCKLVIVTLG 224
Cdd:cd01166 151 AAKARGVTVSFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDED--PTDAAERAL-ALALGVKAVVVKLG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 225 AEGCMMISVEEPIpkHVPAEKVRAVDTTGAGDSFVGA-LAFYLAHypeLPVEEMVRKCNYIASVSVQASG 293
Cdd:cd01166 228 AEGALVYTGGGRV--FVPAYPVEVVDTTGAGDAFAAGfLAGLLEG---WDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-295 |
1.93e-41 |
|
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: 144.76 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 5 VAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAF 84
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 85 VGQTADAVTGTASIIVNSEGQNVIVIVPGANlllssEDLKRASDIICKAKVAVCQLEITPAVsLEALKMARASGVKTLFN 164
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAM-----DELEPNDEADPDGLADIVHLSSGPGL-IELARELAAGGITVSFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 165 PAPALADLD----PEFYTHSDIFCCNETEAEIL---TGIPVgnledtekvgrLLLERGCKLVIVTLGAEGCMMISVEEPI 237
Cdd:cd01942 156 PGQELPRLSgeelEEILERADILFVNDYEAELLkerTGLSE-----------AELASGVRVVVVTLGPKGAIVFEDGEEV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 513175214 238 pkHVPAEK-VRAVDTTGAGDSFvgALAFYLAHYPELPVEEMVRKCNYIASVSVQASGTQ 295
Cdd:cd01942 225 --EVPAVPaVKVVDTTGAGDAF--RAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-300 |
6.92e-38 |
|
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: 135.88 E-value: 6.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 5 VAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAF 84
Cdd:cd01945 2 VLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 85 VGQTADAVTGTASIIVNSEGQNVIVIV----PGANLLLSSEDLKRASDIIckakVAVCQleitPAVSLEALKMARASGVk 160
Cdd:cd01945 82 IVVAPGARSPISSITDITGDRATISITaidtQAAPDSLPDAILGGADAVL----VDGRQ----PEAALHLAQEARARGI- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 161 tlfnpaPALADLDP-------EFYTHSDIFCCNETEAEILTGIPvgnledTEKVGRLLLERGCKLVIVTLGAEGCMMISV 233
Cdd:cd01945 153 ------PIPLDLDGgglrvleELLPLADHAICSENFLRPNTGSA------DDEALELLASLGIPFVAVTLGEAGCLWLER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513175214 234 EEPIpKHVPAEKVRAVDTTGAGDSFVGALAFYLAHYPelPVEEMVRKCNYIASVSVQASGTQSSYPY 300
Cdd:cd01945 221 DGEL-FHVPAFPVEVVDTTGAGDVFHGAFAHALAEGM--PLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
39-293 |
2.95e-35 |
|
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: 128.91 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQTADAVTGTA--SIIVNSEGQNVIVIVPGANL 116
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAfvTLDADGERSFEFYRGPAADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 117 LLSSE---DLKRASDIICkakvaVCQLEITPAVS----LEALKMARASGVKTLFNP---------APALADLDPEFYTHS 180
Cdd:cd01167 108 LLDTElnpDLLSEADILH-----FGSIALASEPSrsalLELLEAAKKAGVLISFDPnlrpplwrdEEEARERIAELLELA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 181 DIFCCNETEAEILTGIpvgnlEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEpiPKHVPAEKVRAVDTTGAGDSFVG 260
Cdd:cd01167 183 DIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGG--VGEVPGIPVEVVDTTGAGDAFVA 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 513175214 261 ALAFYLAHYPEL-----PVEEMVRKCNYIASVSVQASG 293
Cdd:cd01167 256 GLLAQLLSRGLLaldedELAEALRFANAVGALTCTKAG 293
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
39-294 |
4.31e-35 |
|
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: 128.89 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQTaDAVTGTAsiivnsegqnVIVIVPGAN--- 115
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQP-DGPTGTC----------AVLVTPDAErtm 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 116 --LLLSSEDLKRASDIICK-AKVAVCQLE-----ITPAVSLEALKMARASGVKTLFNpapaLADLD-PEFY--------T 178
Cdd:cd01168 124 ctYLGAANELSPDDLDWSLlAKAKYLYLEgylltVPPEAILLAAEHAKENGVKIALN----LSAPFiVQRFkeallellP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 179 HSDIFCCNETEAEILTGipvGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPIpkHVPAEK-VRAVDTTGAGDS 257
Cdd:cd01168 200 YVDILFGNEEEAEALAE---AETTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVY--PVPAIPvEKIVDTNGAGDA 274
|
250 260 270
....*....|....*....|....*....|....*..
gi 513175214 258 FVGALAFYLAHypELPVEEMVRKCNYIASVSVQASGT 294
Cdd:cd01168 275 FAGGFLYGLVQ--GEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
28-299 |
3.02e-30 |
|
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: 116.12 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 28 TILGQKFFIGFGGKGANQCvqsARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQTaDAVTGTASIIVnSEGQNV 107
Cdd:cd01172 31 KVEREEIRLGGAANVANNL---ASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDE-GRPTTTKTRVI-ARNQQL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 108 IVIVPGANLLLSSEDLKRASDIIcKAKVAVCQLEI---------TPAVSLEALKMARASGVKTLFNPAPaladLDPEFYT 178
Cdd:cd01172 106 LRVDREDDSPLSAEEEQRLIERI-AERLPEADVVIlsdygkgvlTPRVIEALIAAARELGIPVLVDPKG----RDYSKYR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 179 HSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLER-GCKLVIVTLGAEGCMMISVEEPiPKHVPAEKVRAVDTTGAGDS 257
Cdd:cd01172 181 GATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGE-VQHIPALAKEVYDVTGAGDT 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 513175214 258 FVGALAFYLAHypELPVEEMVRKCNYIASVSVQASGTQSSYP 299
Cdd:cd01172 260 VIATLALALAA--GADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
4-268 |
1.72e-26 |
|
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: 105.47 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 4 EVAVVGSCMTDLVSFTTRLPRAGETILGQKFFiGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTA 83
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQ-SPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 84 FVgQTADAVTGTASIIVNSEGQNVIVIV-PGANLLLSSEDLKRASDIICKAKVAVCQLEITPAVSLEALKMARASGVKTL 162
Cdd:cd01941 80 GI-VFEGRSTASYTAILDKDGDLVVALAdMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 163 FNPAPALADLDPEFYTHS-DIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEP-IPKH 240
Cdd:cd01941 159 FEPTSAPKLKKLFYLLHAiDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGvETKL 238
|
250 260
....*....|....*....|....*....
gi 513175214 241 VPAEKV-RAVDTTGAGDSFVGALAFYLAH 268
Cdd:cd01941 239 FPAPQPeTVVNVTGAGDAFVAGLVAGLLE 267
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
39-262 |
2.98e-25 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 103.16 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQTADAVTGTASIIVNSEGQNVIVIV--PGANL 116
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSADM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 117 LLSSEDLKRasDIICKAKV---AVCQLEITPAVS--LEALKMARASGVKTLFNPAPALAdLDP----------EFYTHSD 181
Cdd:PLN02323 123 LLRESELDL--DLIRKAKIfhyGSISLITEPCRSahLAAMKIAKEAGALLSYDPNLRLP-LWPsaeaaregimSIWDEAD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 182 IFCCNETEAEILTGipvGNLEDTEKVGRLLlERGCKLVIVTLGAEGCMMISVEepIPKHVPAEKVRAVDTTGAGDSFVGA 261
Cdd:PLN02323 200 IIKVSDEEVEFLTG---GDDPDDDTVVKLW-HPNLKLLLVTEGEEGCRYYTKD--FKGRVEGFKVKAVDTTGAGDAFVGG 273
|
.
gi 513175214 262 L 262
Cdd:PLN02323 274 L 274
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
39-304 |
1.49e-24 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 100.78 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQTADAVTGTASIIVNSEGQN--VIVIVPGANL 116
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 117 LLSSEDLK--RASDIICKAKVAVCQlEITPAVSLEALKMARASGVKTLFNP-------------------APALADldpe 175
Cdd:PRK09434 108 FLQPQDLPpfRQGEWLHLCSIALSA-EPSRSTTFEAMRRIKAAGGFVSFDPnlredlwqdeaelreclrqALALAD---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 176 fythsdIFCCNETEAEILTGIPvgNLED-TEKVGRLLlerGCKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDTTGA 254
Cdd:PRK09434 183 ------VVKLSEEELCFLSGTS--QLEDaIYALADRY---PIALLLVTLGAEGVLVHTRGQVQ--HFPAPSVDPVDTTGA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 513175214 255 GDSFVGALAFYLAHYPELP----VEEMVRKCNYIASVSVQASGTQSSYPYRKDL 304
Cdd:PRK09434 250 GDAFVAGLLAGLSQAGLWTdeaeLAEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
5-293 |
8.68e-23 |
|
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: 95.57 E-value: 8.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 5 VAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGkGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAF 84
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 85 VGQTADAvTGTASIIVNSEGQNVIVIVPGANLLLSSEDLKR----ASDII----------CKAKVAVCQLeitpavsLEA 150
Cdd:cd01944 81 PPRGGDD-GGCLVALVEPDGERSFISISGAEQDWSTEWFATltvaPYDYVylsgytlaseNASKVILLEW-------LEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 151 LkmarASGVKTLFNPAPALADLDPEFYTH----SDIFCCNETEAEILTGipVGNLEDtEKVGRLLLERGCKLVIVTLGAE 226
Cdd:cd01944 153 L----PAGTTLVFDPGPRISDIPDTILQAlmakRPIWSCNREEAAIFAE--RGDPAA-EASALRIYAKTAAPVVVRLGSN 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513175214 227 GCMmISVEEPIPKHVPAEKVRAVDTTGAGDSFVGALAFYLAHypELPVEEMVRKCNYIASVSVQASG 293
Cdd:cd01944 226 GAW-IRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAK--GMSLADAVLLANAAAAIVVTRSG 289
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
4-267 |
8.93e-23 |
|
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: 93.31 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 4 EVAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLIckvgkdsfgndyvanlkkngvsta 83
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLV------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 84 fvgqTADAVtgtasiivnsegqnvivivpganlLLSSEDLKrasdiickakvavcqleitPAVSLEALKMARASGVKTLF 163
Cdd:cd00287 57 ----GADAV------------------------VISGLSPA-------------------PEAVLDALEEARRRGVPVVL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 164 NPAPALADLDPE----FYTHSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPIpK 239
Cdd:cd00287 90 DPGPRAVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTE-V 168
|
250 260
....*....|....*....|....*...
gi 513175214 240 HVPAEKVRAVDTTGAGDSFVGALAFYLA 267
Cdd:cd00287 169 HVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
186-295 |
4.23e-20 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 88.27 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 186 NETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDTTGAGDSFVGALAFY 265
Cdd:COG1105 184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVSTVGAGDSMVAGFLAG 261
|
90 100 110
....*....|....*....|....*....|
gi 513175214 266 LAHypELPVEEMVRKCNYIASVSVQASGTQ 295
Cdd:COG1105 262 LAR--GLDLEEALRLAVAAGAAAALSPGTG 289
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
39-295 |
6.71e-20 |
|
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: 87.59 E-value: 6.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDsFGNDYVANLKKNGVSTAFVgqTADAVTGTASIIVNSEGQNVIVIVPGAnlLL 118
Cdd:cd01164 36 GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFV--EVAGETRINVKIKEEDGTETEINEPGP--EI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 119 SSED----LKRASDIICKAKVAVCQLEITPAVSLEA----LKMARASGVKTLF--NPAPALADLDpefythSDIFCC--N 186
Cdd:cd01164 111 SEEElealLEKLKALLKKGDIVVLSGSLPPGVPADFyaelVRLAREKGARVILdtSGEALLAALA------AKPFLIkpN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 187 ETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDTTGAGDSFVGALAFYL 266
Cdd:cd01164 185 REELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVY--RASPPKVKVVSTVGAGDSMVAGFVAGL 262
|
250 260
....*....|....*....|....*....
gi 513175214 267 AHypELPVEEMVRKCNYIASVSVQASGTQ 295
Cdd:cd01164 263 AQ--GLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
4-264 |
8.07e-18 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 83.34 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 4 EVAVVGSCMTDLVSFTTRLPRAG----ETILGQ-------KFFIGFGGKgANQCVQSARLGAKTSLICKVGKDSFGNDYV 72
Cdd:PLN02341 74 DVATLGNLCVDIVLPVPELPPPSreerKAYMEElaasppdKKSWEAGGN-CNFAIAAARLGLRCSTIGHVGDEIYGKFLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 73 ANLKKNGVSTafVGQTADAVTGtASIIVNSEGQNVIVIVPGA--NLLLSSEDLKR------ASDIICKAKVAVCQL---- 140
Cdd:PLN02341 153 DVLAEEGISV--VGLIEGTDAG-DSSSASYETLLCWVLVDPLqrHGFCSRADFGPepafswISKLSAEAKMAIRQSkalf 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 141 -------EITPAVSLEALKMARASGVKTLFNPAP---ALADLDPE-------FYTHSDIFCCNETEAEILTGIpvgnlED 203
Cdd:PLN02341 230 cngyvfdELSPSAIASAVDYAIDVGTAVFFDPGPrgkSLLVGTPDerralehLLRMSDVLLLTSEEAEALTGI-----RN 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 513175214 204 TEKVGRLLLERGC--KLVIVTLGAEGCMMISVEEPipKHVPAEKVRAVDTTGAGDSFVGALAF 264
Cdd:PLN02341 305 PILAGQELLRPGIrtKWVVVKMGSKGSILVTRSSV--SCAPAFKVNVVDTVGCGDSFAAAIAL 365
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
5-293 |
3.32e-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: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 5 VAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKkNGVSTAF 84
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELE-SGGDKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 85 VGQTaDAVTGTASIIVNSEGQNVIvIVPGANLL-------LSSEDLkrasdiickakvavcqLEITPAVSL-EALKMARA 156
Cdd:cd01947 81 VAWR-DKPTRKTLSFIDPNGERTI-TVPGERLEddlkwpiLDEGDG----------------VFITAAAVDkEAIRKCRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 157 SGVKTLFNPAPALADLDPEFYTHSDIFCCNETEAEILTgipvgnledtekVGRLLLERGCKLVIVTLGAEGcmmISVEEP 236
Cdd:cd01947 143 TKLVILQVTPRVRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELG---AILYPG 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 513175214 237 IP-KHVPAEKVRAVDTTGAGDSFVGALAFYLAHypELPVEEMVRKCNYIASVSVQASG 293
Cdd:cd01947 208 GRyNHVPAKKAKVPDSTGAGDSFAAGFIYGLLK--GWSIEEALELGAQCGAICVSHFG 263
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
56-304 |
9.04e-15 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 73.60 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 56 TSLICKVGKDSFGNDYVANLKKNGVSTAFVgQTADAVTGTASIIVNSEGQNVIVIVPGANLLlSSEDLKRASD--IICKA 133
Cdd:PLN02548 72 TSYMGCIGKDKFGEEMKKCATAAGVNVHYY-EDESTPTGTCAVLVVGGERSLVANLSAANCY-KVEHLKKPENwaLVEKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 134 KVAVCQ---LEITPAVSLEALKMARASGVKTLFN-PAPALADL--DP--EFYTHSDIFCCNETEAEILTGIPVGNLEDTE 205
Cdd:PLN02548 150 KFYYIAgffLTVSPESIMLVAEHAAANNKTFMMNlSAPFICEFfkDQlmEALPYVDFLFGNETEARTFAKVQGWETEDVE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 206 ----KVGRLLLERGC--KLVIVTLGAeGCMMISVE--------EPIPKhvpaEKVraVDTTGAGDSFVGAlafYLAHY-P 270
Cdd:PLN02548 230 eialKISALPKASGThkRTVVITQGA-DPTVVAEDgkvkefpvIPLPK----EKL--VDTNGAGDAFVGG---FLSQLvQ 299
|
250 260 270
....*....|....*....|....*....|....
gi 513175214 271 ELPVEEMVRKCNYIASVSVQASGTqsSYPYRKDL 304
Cdd:PLN02548 300 GKDIEECVRAGNYAANVIIQRSGC--TYPEKPDF 331
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
39-269 |
1.73e-13 |
|
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: 68.92 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVgQTADAVTGTAsIIVNSEGQNVIVIVP---GAN 115
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVA-DVELVDGDRIFGLSNkggVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 116 LLLSSEDLK--RASDIICKAKVAVCQLeitpavSLEALKMARASGVKTLFNpapaladldpefythsdiFCCNETEAEIL 193
Cdd:cd01940 100 EHPFEADLEylSQFDLVHTGIYSHEGH------LEKALQALVGAGALISFD------------------FSDRWDDDYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 194 TGIP-------VGNLEDTEKVGRLLLE---RGCKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDTTGAGDSFVGALA 263
Cdd:cd01940 156 LVCPyvdfaffSASDLSDEEVKAKLKEavsRGAKLVIVTRGEDGAIAYDGAVFY--SVAPRPVEVVDTLGAGDSFIAGFL 233
|
....*.
gi 513175214 264 FYLAHY 269
Cdd:cd01940 234 LSLLAG 239
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
62-299 |
2.71e-13 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 69.29 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 62 VGKDSFGNDYVANLKKNGVSTAFvGQTADAVTGT-ASIIVNSEGQNVIVIvpGANLLLSSEDLKRASDIIC--KAKVAVC 138
Cdd:PTZ00247 89 VGDDRFAEILKEAAEKDGVEMLF-EYTTKAPTGTcAVLVCGKERSLVANL--GAANHLSAEHMQSHAVQEAikTAQLYYL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 139 Q---LEITPAVSLEALKMARASGVKTLFN-PAP-ALADLDPEFYT---HSDIFCCNETEAEILTGIPVGNLEDTEKVGR- 209
Cdd:PTZ00247 166 EgffLTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFFFERLLQvlpYVDILFGNEEEAKTFAKAMKWDTEDLKEIAAr 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 210 ---LLLERGCK--LVIVTLGAE----GCMMISVEEPIPKhVPAEKVraVDTTGAGDSFVGA-LAFYLAHYPElpvEEMVR 279
Cdd:PTZ00247 246 iamLPKYSGTRprLVVFTQGPEptliATKDGVTSVPVPP-LDQEKI--VDTNGAGDAFVGGfLAQYANGKDI---DRCVE 319
|
250 260
....*....|....*....|
gi 513175214 280 KCNYIASVSVQASGtqSSYP 299
Cdd:PTZ00247 320 AGHYSAQVIIQHNG--CTYP 337
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
181-294 |
2.14e-12 |
|
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: 65.95 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 181 DIFCCNETEAEILTGIPvgNLEdteKVGRLLLERGCKLVIVTLGAEGCMMISVEE--PIPKHvPAEKVraVDTTGAGDSF 258
Cdd:cd01946 165 DVVIINDGEARQLTGAA--NLV---KAARLILAMGPKALIIKRGEYGALLFTDDGyfAAPAY-PLESV--FDPTGAGDTF 236
|
90 100 110
....*....|....*....|....*....|....*....
gi 513175214 259 VGALAFYLAHYPELPVEEMVRKCNY---IASVSVQASGT 294
Cdd:cd01946 237 AGGFIGYLASQKDTSEANMRRAIIYgsaMASFCVEDFGT 275
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
39-293 |
1.37e-10 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 60.52 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVgQTADAVTgtASIIVNSEGQNVIV--IVPG--A 114
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV-HTKHGVT--AQTQVELHDNDRVFgdYTEGvmA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 115 NLLLSSEDLKRAS--DIICKAKVAVCQleitpavslEALKMARASGVKTLFNPA---------PALADLDPEFYTHSDif 183
Cdd:PRK09813 100 DFALSEEDYAWLAqyDIVHAAIWGHAE---------DAFPQLHAAGKLTAFDFSdkwdsplwqTLVPHLDYAFASAPQ-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 184 ccnETEAeiltgipvgnLEDTEKVgrlLLERGCKLVIVTLGAEGCmmISVEEPIPKHVPAEKVRAVDTTGAGDSFV-GAL 262
Cdd:PRK09813 169 ---EDEF----------LRLKMKA---IVARGAGVVIVTLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIaGFL 230
|
250 260 270
....*....|....*....|....*....|.
gi 513175214 263 AFYLAHypeLPVEEMVRKCNYIASVSVQASG 293
Cdd:PRK09813 231 CGWLAG---MTLPQAMAQGTACAAKTIQYHG 258
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
39-263 |
8.72e-10 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 58.85 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQTADAVTGTASIIVNSEGQnVIVIVPGANL-- 116
Cdd:PRK09850 40 GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGE-MLVAINDMNIsn 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 117 LLSSEDLKRASDIICKAKVAVCQLEItpavSLEALK--MARASGVKTLFNPAPALADLD-PEFYTHSDIFCCNETEAEIL 193
Cdd:PRK09850 119 AITAEYLAQHREFIQRAKVIVADCNI----SEEALAwiLDNAANVPVFVDPVSAWKCVKvRDRLNQIHTLKPNRLEAETL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 194 TGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPIPKHVPAeKVRAVDTTGAGDSFVGALA 263
Cdd:PRK09850 195 SGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGWSAPI-KTNVINVTGAGDAMMAGLA 263
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
39-272 |
2.32e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 57.90 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTS--------LICKVGKDSFGNDYVANLKKNGVStaFVGQ-TADAVTGTASIIVNSEGQNVIV 109
Cdd:PLN02813 126 GGSLSNTLVALARLGSQSAagpalnvaMAGSVGSDPLGDFYRTKLRRANVH--FLSQpVKDGTTGTVIVLTTPDAQRTML 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 110 IVPGANLLLS-SEDLkraSDIICKAKVAVCQ-----LEITPAVSLEALKMARASGVKTlfnpapALADLDP--------E 175
Cdd:PLN02813 204 SYQGTSSTVNyDSCL---ASAISKSRVLVVEgylweLPQTIEAIAQACEEAHRAGALV------AVTASDVscierhrdD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 176 FY----THSDIFCCNETEAEILTGIpvGNLEDTEKVGRLLLERgCKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDT 251
Cdd:PLN02813 275 FWdvmgNYADILFANSDEARALCGL--GSEESPESATRYLSHF-CPLVSVTDGARGSYIGVKGEAV--YIPPSPCVPVDT 349
|
250 260
....*....|....*....|..
gi 513175214 252 TGAGDSFV-GALAFYLAHYPEL 272
Cdd:PLN02813 350 CGAGDAYAaGILYGLLRGVSDL 371
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
39-279 |
2.13e-08 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 54.40 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGkDSFGNDYVANLKKNGVSTAFVgQTADAVTGTASIIVNSEGQNVIVIVPGANLll 118
Cdd:PRK10294 38 GGGGINVARAIAHLGGSATAIFPAG-GATGEHLVSLLADENVPVATV-EAKDWTRQNLHVHVEASGEQYRFVMPGAAL-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 119 sSED----LKRASDIICKAKVAVCQLEITPAVSLEAL----KMARASGVKTLFNP-----APALADLDPEFYTHsdifcc 185
Cdd:PRK10294 114 -NEDefrqLEEQVLEIESGAILVISGSLPPGVKLEKLtqliSAAQKQGIRCIIDSsgdalSAALAIGNIELVKP------ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 186 NETEAEILTGIPVGNLEDTEKVGRLLLERG-CKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDTTGAGDSFVGALAF 264
Cdd:PRK10294 187 NQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCI--QVVPPPVKSQSTVGAGDSMVGAMTL 264
|
250
....*....|....*
gi 513175214 265 YLAHypELPVEEMVR 279
Cdd:PRK10294 265 KLAE--NASLEEMVR 277
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
179-282 |
2.68e-08 |
|
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: 53.74 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 179 HSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVT----LGAEGCMMISVEEPIPKHVPAEKV-RAVDTTG 253
Cdd:cd01173 136 LADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelADDDRIEMLGSTATEAWLVQRPKIpFPAYFNG 215
|
90 100
....*....|....*....|....*....
gi 513175214 254 AGDSFVGALAFYLAHYPELPveEMVRKCN 282
Cdd:cd01173 216 TGDLFAALLLARLLKGKSLA--EALEKAL 242
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
39-288 |
3.05e-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: 50.48 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFgnDYVANLKKNGVSTAFVGqtaDAVTGTASIIVNSEGQNVIVIVPGANLL- 117
Cdd:cd01937 24 GGPATYASLTLSRLGLTVKLVTKVGRDYP--DKWSDLFDNGIEVISLL---STETTTFELNYTNEGRTRTLLAKCAAIPd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 118 LSSEDLKRASDIICKAKVAvcqLEITPAVSLE-ALKMARASGVKTLFNP-----APALADLDPEFYTHSDIFCCNeTEAE 191
Cdd:cd01937 99 TESPLSTITAEIVILGPVP---EEISPSLFRKfAFISLDAQGFLRRANQeklikCVILKLHDVLKLSRVEAEVIS-TPTE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 192 ILtgipvgnledtekvgRLLLERGCKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDTTGAGDSFVGALAFYLAHYPE 271
Cdd:cd01937 175 LA---------------RLIKETGVKEIIVTDGEEGGYIFDGNGKY--TIPASKKDVVDPTGAGDVFLAAFLYSRLSGKD 237
|
250
....*....|....*..
gi 513175214 272 LpveemVRKCNYIASVS 288
Cdd:cd01937 238 I-----KEAAEFAAAAA 249
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
49-260 |
3.05e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 51.33 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 49 SARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVgQTADAVTGTASIIVNSEGQNVI-------VIVPGANLllSSE 121
Cdd:PLN02379 97 SAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRL-RAKKGPTAQCVCLVDALGNRTMrpclssaVKLQADEL--TKE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 122 DLKRASDIIckAKVAVCQLEitpaVSLEALKMARASGVKTLFNPA---------PALADLdpefYTHSDIFCC--NETEA 190
Cdd:PLN02379 174 DFKGSKWLV--LRYGFYNLE----VIEAAIRLAKQEGLSVSLDLAsfemvrnfrSPLLQL----LESGKIDLCfaNEDEA 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 513175214 191 EILTGipvGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPIpkHVPA-EKVRAVDTTGAGDSFVG 260
Cdd:PLN02379 244 RELLR---GEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGKEVV--RVPAiGETNAVDATGAGDLFAS 309
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
186-266 |
3.74e-07 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 50.85 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 186 NETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEGCMMISVEEPIPKHVPAEKVraVDTTGAGDSFVGALAFY 265
Cdd:PRK09513 187 NRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDV--VSTVGAGDSMVGGLIYG 264
|
.
gi 513175214 266 L 266
Cdd:PRK09513 265 L 265
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
167-268 |
4.21e-07 |
|
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: 50.15 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 167 PALADLDPEFYTHSDIFCC--------------NETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVT-LGAEGCM-- 229
Cdd:COG2240 112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsVPLDDTPad 191
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 513175214 230 ---MISVEEPIPKHVPAEKVrAVDTTGAGDSFVGALAFYLAH 268
Cdd:COG2240 192 kigNLAVTADGAWLVETPLL-PFSPNGTGDLFAALLLAHLLR 232
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
181-268 |
6.04e-07 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 50.03 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 181 DIFCCNETEAEILTGIPV---GNLEDTEKVGRLLLE-----RGCKLVIVTLGAEGCMMISVEEPIPKHVPA-----EKVr 247
Cdd:cd01943 182 DVFSPNLEEAARLLGLPTsepSSDEEKEAVLQALLFsgilqDPGGGVVLRCGKLGCYVGSADSGPELWLPAyhtksTKV- 260
|
90 100
....*....|....*....|.
gi 513175214 248 aVDTTGAGDSFVGALAFYLAH 268
Cdd:cd01943 261 -VDPTGGGNSFLGGFAAGLAL 280
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
189-280 |
8.34e-07 |
|
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: 49.02 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 189 EAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLG-AEGCMMISV-----EEPIpKHVPAEKVRAVDTTGAGDSFVGAL 262
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGhLEGEEAVVTdvlydGGGF-YTLEAPRIPTKNTHGTGCTLSAAI 207
|
90
....*....|....*...
gi 513175214 263 AFYLAHYpeLPVEEMVRK 280
Cdd:pfam08543 208 AANLAKG--LSLPEAVRE 223
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
39-264 |
9.01e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 49.93 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 39 GGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVGQTADAVTGTASIIVNSEGQNVIVIvPGANLL- 117
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDETVLAI-NDTHILq 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 118 -LSSEDLKRASDIICKAKVAVCQLEITPavslEALKMarasgVKTLFNPAPALADLDPEF--------YTHSDIFCCNET 188
Cdd:PRK09954 172 qLTPQLLNGSRDLIRHAGVVLADCNLTA----EALEW-----VFTLADEIPVFVDTVSEFkagkikhwLAHIHTLKPTQP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 189 EAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLGAEG--CMMISVEEPI---PKHVpaekvrAVDTTGAGDSFVGALA 263
Cdd:PRK09954 243 ELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESvfCSEKDGEQFLltaPAHT------TVDSFGADDGFMAGLV 316
|
.
gi 513175214 264 F 264
Cdd:PRK09954 317 Y 317
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
203-293 |
1.82e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 48.65 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 203 DTEKVgrllleRGCKLVIVTLGAEGCMMISVEEPIpkHVPAEKVRAVDTTGAGDSFVGalAFYLAHYPELPVEEMVRKCN 282
Cdd:PLN02630 196 DVEEV------RQKCCVIVTNGKKGCRIYWKDGEM--RVPPFPAIQVDPTGAGDSFLG--GFVAGLVQGLAVPDAALLGN 265
|
90
....*....|.
gi 513175214 283 YIASVSVQASG 293
Cdd:PLN02630 266 YFGSLAVEQVG 276
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
189-280 |
2.20e-06 |
|
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: 48.11 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 189 EAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVTLG-AEGCMMISV----EEPIpkHVPAEKVRAVDTTGAGDSFVGALA 263
Cdd:COG0351 136 EAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGhLPGDEAVDVlydgDGVR--EFSAPRIDTGNTHGTGCTLSSAIA 213
|
90
....*....|....*..
gi 513175214 264 FYLAHypELPVEEMVRK 280
Cdd:COG0351 214 ALLAK--GLDLEEAVRE 228
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
189-273 |
2.84e-06 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 47.81 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 189 EAEILTGIPVGNLEDT-EKVGRLLLERGCKLVIVTLGAEGcmmisvEEPIPKHV----------PAEKVRAVDTTGAGDS 257
Cdd:PRK06427 143 EAEALTGLPIADTEDEmKAAARALHALGCKAVLIKGGHLL------DGEESVDWlfdgegeerfSAPRIPTKNTHGTGCT 216
|
90
....*....|....*.
gi 513175214 258 FVGALAFYLAHYPELP 273
Cdd:PRK06427 217 LSAAIAAELAKGASLL 232
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-294 |
2.12e-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: 45.09 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 5 VAVVGSCMTDLVSFTTRLPRAGETILGQKFFIGFGGKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAF 84
Cdd:cd01939 2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 85 VGQTADAVTGTASIIVNSEGQNVIVIVPGANLLLSSEDLKRASD-----IICKAKVAVCQL--------------EITPA 145
Cdd:cd01939 82 CYRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLtqygwIHFEGRNPDETLrmmqhieehnnrrpEIRIT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 146 VSLEalkmarasgvktLFNPAPALADLDPE----FYTHSdifccneteaeILTGIPVGNLEDTeKVGRLLLERGCKLVIV 221
Cdd:cd01939 162 ISVE------------VEKPREELLELAAYcdvvFVSKD-----------WAQSRGYKSPEEC-LRGEGPRAKKAALLVC 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 513175214 222 TLGAEG--CMMIsveEPIPKHVPAEK-VRAVDTTGAGDSFVGALAFYLAHYPElPVEEMVRKCNYIASVSVQASGT 294
Cdd:cd01939 218 TWGDQGagALGP---DGEYVHSPAHKpIRVVDTLGAGDTFNAAVIYALNKGPD-DLSEALDFGNRVASQKCTGVGF 289
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
180-227 |
5.38e-05 |
|
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: 44.05 E-value: 5.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 513175214 180 SDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVT-LGAEG 227
Cdd:TIGR00687 139 ADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAG 187
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
40-294 |
1.55e-04 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 42.89 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 40 GKGANQCVQSARLGAKTSLICKVGKDSFGNDYVANLKKNGVSTAFVgqtadAVTGTASII---VNSEGQNVIVI------ 110
Cdd:PRK11316 51 GGAANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFV-----SVPTHPTITklrVLSRNQQLIRLdfeegf 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 111 --VPGANLLLSSED-LKRASDIICK--AKVAVCQLEitpavslEALKMARASGVKTLFNPAPAladlDPEFYTHSDIFCC 185
Cdd:PRK11316 126 egVDPQPLLERIEQaLPSIGALVLSdyAKGALASVQ-------AMIQLARKAGVPVLIDPKGT----DFERYRGATLLTP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 186 NETEAEILTGiPVGNLEDtekvgrlLLERGCKLV--------IVTLGAEGCMMISVEEPiPKHVPAEKVRAVDTTGAGDS 257
Cdd:PRK11316 195 NLSEFEAVVG-KCKDEAE-------LVEKGMKLIadydlsalLVTRSEQGMTLLQPGKA-PLHLPTQAREVYDVTGAGDT 265
|
250 260 270
....*....|....*....|....*....|....*..
gi 513175214 258 FVGALAFYLAHYPELPveEMVRKCNYIASVSVQASGT 294
Cdd:PRK11316 266 VISVLAAALAAGNSLE--EACALANAAAGVVVGKLGT 300
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
179-222 |
5.49e-04 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 41.01 E-value: 5.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 513175214 179 HSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVT 222
Cdd:PRK05756 138 AADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
186-271 |
1.50e-03 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 39.72 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 186 NETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVT-LGAEGCMMISVEEPIPKHVPAEKVR-AVDT-----TGAGDSF 258
Cdd:PLN02978 156 NQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITsIDIDGKLLLVGSHRKEKGARPEQFKiVIPKipayfTGTGDLM 235
|
90
....*....|...
gi 513175214 259 VGALAFYLAHYPE 271
Cdd:PLN02978 236 AALLLGWSHKYPD 248
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
186-279 |
4.13e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 38.56 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 186 NETEAEILTGIPVGNLEDTEKVGRLLLER-GCKLVIVTLGaegcmMISVEEPIP--------KHVPAEKVRAVDTTGAGD 256
Cdd:PRK08573 137 NRPEAEKLTGMKIRSVEDARKAAKYIVEElGAEAVVVKGG-----HLEGEEAVDvlyhngtfREFRAPRVESGCTHGTGC 211
|
90 100
....*....|....*....|...
gi 513175214 257 SFVGALAFYLAHypELPVEEMVR 279
Cdd:PRK08573 212 SFSAAIAAGLAK--GLDPEEAIK 232
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
168-267 |
9.84e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 36.96 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513175214 168 ALADLDPEFYTHSDIFCCNETEAEILTGIPVGNLEDTEKVGRLLLERGCKLVIVtlgaEGCMMISVEEPIPKHVPAEKVR 247
Cdd:PRK12413 118 ELRQELIQFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI----KGGNRLSQKKAIDLFYDGKEFV 193
|
90 100
....*....|....*....|....*..
gi 513175214 248 AVDT-------TGAGDSFVGALAFYLA 267
Cdd:PRK12413 194 ILESpvleknnIGAGCTFASSIASQLV 220
|
|
| |
