|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
5-326 |
2.15e-131 |
|
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239435 [Multi-domain] Cd Length: 316 Bit Score: 378.07 E-value: 2.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 5 DVQVHYRNIPLLVPFKTALRQANEIDSIEVEITLDnGIKGTGAAAPTVVITGDSTESIMSVAAGpVKEALSGHDLRdFQG 84
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGETVESVLAALKS-VRPALIGGDPR-LEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 85 ALKKVQRCCTGNTSAKAAADIALYDAYSKWLNIPLYAYLGG--QKNLRTSMTIGVDTPEKMAWDAEKSVEAGFHLLKIKV 162
Cdd:cd03319 78 LLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGgaPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 163 GTYPEIDLERIEVVRRAVPpDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKLPVMAD 242
Cdd:cd03319 158 GGDLEDDIERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELA--ELGVELIEQPVPAGDDDGLAYLRDKSPLPIMAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 243 ESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLSVAAAAHFAAAhpNVAYMDLDA 322
Cdd:cd03319 235 ESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAA--KADFVDLDG 312
|
....
gi 518550582 323 PLWL 326
Cdd:cd03319 313 PLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-350 |
4.71e-116 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 340.65 E-value: 4.71e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 1 MIIKDVQVHYRNIPLLVPFKTALRQANEIDSIEVEITLDNGIKGTGAAAPTvvitGDSTESIMSVAAGPVKEALSGHDLR 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPG----GTGAEAVAAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 81 DFQGALKKVQRCCTGNTSAKAAADIALYDAYSKWLNIPLYAYLGGQKN--LRTSMTIGVDTPEKMAWDAEKSVEAGFHLL 158
Cdd:COG4948 77 DIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRdrVPVYATLGIDTPEEMAEEAREAVARGFRAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 159 KIKVGT-YPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKL 237
Cdd:COG4948 157 KLKVGGpDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALE--DLGLEWIEQPLPAEDLEGLAELRRATPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 238 PVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLSVAAAAHFAAAHPNVAY 317
Cdd:COG4948 235 PIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFDI 314
|
330 340 350
....*....|....*....|....*....|....*
gi 518550582 318 MDLDAPLWLSEEP--DHLTYDGEDVLLSDQPGIGI 350
Cdd:COG4948 315 VELDGPLLLADDLveDPLRIEDGYLTVPDGPGLGV 349
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
13-300 |
2.37e-69 |
|
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.
Pssm-ID: 239431 [Multi-domain] Cd Length: 265 Bit Score: 217.98 E-value: 2.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 13 IPLLVPFKTALRQANEIDSIEVEITLDNGIKGTGAAAptvvitgdstesimsvaagpvkealsghdlrdfqgalkkvqrc 92
Cdd:cd03315 8 LPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEAT------------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 93 ctgntsaKAAADIALYDAYSKWLNIPLYAYLGGQK-NLRTSMTIGVDTPEKMAWDAEKSVEAGFHLLKIKVGTYPEIDLE 171
Cdd:cd03315 45 -------KAAVDMALWDLWGKRLGVPVYLLLGGYRdRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRDPARDVA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 172 RIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESLFSAKDA 251
Cdd:cd03315 118 VVAALREAVGDDAELRVDANRGWTPKQAIRALRALE--DLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHDA 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518550582 252 LKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSL 300
Cdd:cd03315 196 FRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGL 244
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
14-350 |
2.03e-63 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 206.01 E-value: 2.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 14 PLLVPFKTALRQANEIDSIEVEITLDNGIKGTGAAAP--TVVITGDSTESIMSVAAGPVKEALSGHDLRDFQGALKKVQR 91
Cdd:cd03318 13 PTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTpgGPAWGGESPETIKAIIDRYLAPLLIGRDATNIGAAMALLDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 92 CCTGNTSAKAAADIALYDAYSKWLNIPLYAYLGG--QKNLRTSMTIGV-DTPEKMAwDAEKSVEAGFH-LLKIKVGTYP- 166
Cdd:cd03318 93 AVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGrvRDSLPVAWTLASgDTERDIA-EAEEMLEAGRHrRFKLKMGARPp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 167 EIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESLF 246
Cdd:cd03318 172 ADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLE--AAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 247 SAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLSVAAAAHFAAAHPNVAY-MDLDAPLW 325
Cdd:cd03318 250 GPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPFgCELFGPLL 329
|
330 340
....*....|....*....|....*..
gi 518550582 326 LSEEPDH--LTYDGEDVLLSDQPGIGI 350
Cdd:cd03318 330 LAEDLLEepLAYRDGELHVPTGPGLGV 356
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
3-350 |
1.03e-55 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 185.89 E-value: 1.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 3 IKDVQVHYRNIPLLVPFKTALRQaneiDSIEVEITLDNGIKGTGAAAPtvvitGDSTESIMSVAAGPVKEALSGHDLRDF 82
Cdd:cd03316 2 ITDVETFVLRVPLPEPGGAVTWR----NLVLVRVTTDDGITGWGEAYP-----GGRPSAVAAAIEDLLAPLLIGRDPLDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 83 QGALKKVQRC------CTGNTSAKAAADIALYDAYSKWLNIPLYAYLGGQKNLR-----TSMTIGvDTPEKMAWDAEKSV 151
Cdd:cd03316 73 ERLWEKLYRRlfwrgrGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRvrvyaSGGGYD-DSPEELAEEAKRAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 152 EAGFHLLKIKVG------TYPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDW 225
Cdd:cd03316 152 AEGFTAVKLKVGgpdsggEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALE--EYDLFWFEEPVPPDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 226 EGLKFVTERTKLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCM-------VGSMMep 298
Cdd:cd03316 230 EGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAphgaggpIGLAA-- 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 518550582 299 SLSVaaaahfAAAHPNVAYM-----DLDAPLWLSEEPDHLTyDGEdVLLSDQPGIGI 350
Cdd:cd03316 308 SLHL------AAALPNFGILeyhldDLPLREDLFKNPPEIE-DGY-VTVPDRPGLGV 356
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
3-350 |
2.85e-55 |
|
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2).
Pssm-ID: 162905 [Multi-domain] Cd Length: 368 Bit Score: 185.00 E-value: 2.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 3 IKDVQVHYRNIPLLVPFKTALRQANEIDSIEVEITLDNGIKGTGAAaptVVITG-----DSTESIMSVAAGPVKEALSGH 77
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEG---TTIGGlwwggESPETIKANIDTYLAPVLVGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 78 DLRDFQGALKKVQRCCTGNTSAKAAADIALYDAYSKWLNIPLYAYLGG--QKNLRTSMTIGVDTPEKMAWDAEKSVEA-G 154
Cdd:TIGR02534 78 DATEIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGrvRDSVDVTWTLASGDTDRDIAEAEERIEEkR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 155 FHLLKIKVGTY-PEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTE 233
Cdd:TIGR02534 158 HRSFKLKIGARdPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLA--DAGVELIEQPTPAENREALARLTR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 234 RTKLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLSVAAAAHFAAAHP 313
Cdd:TIGR02534 236 RFNVPIMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFP 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 518550582 314 NVAY-MDLDAPLWLSEE--PDHLTYDGEDVLLSDQPGIGI 350
Cdd:TIGR02534 316 ALSFgTELFGPLLLKDEilTEPLQYEDFQLHLPQGPGLGV 355
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
142-350 |
8.10e-54 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 176.22 E-value: 8.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 142 KMAWDAEKSVEA-GFHLLKIKVGTY-PEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQP 219
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGGPdPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALE--ELGLLWIEEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 220 VRADDWEGLKFVTERTKLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEP- 298
Cdd:pfam13378 79 VPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPi 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 299 ----SLSVaaaahfAAAHPNVAYMDLDAPLWLSEEpDHLTYDGED----VLLSDQPGIGI 350
Cdd:pfam13378 159 glaaSLHL------AAAVPNLLIQEYFLDPLLLED-DLLTEPLEVedgrVAVPDGPGLGV 211
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
94-301 |
4.36e-46 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 156.72 E-value: 4.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 94 TGNTSAKAAADIALYDAYSKWLNIPLYAYLGGQknlrtsmtigvdtpekmawdAEKSVEAGFHLlkikvgtypeidlERI 173
Cdd:cd00308 38 VGWGEVISGIDMALWDLAAKALGVPLAELLGGG--------------------SRDRVPAYGSI-------------ERV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 174 EVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESLFSAKDALK 253
Cdd:cd00308 85 RAVREAFGPDARLAVDANGAWTPKEAIRLIRALE--KYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDDALE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518550582 254 LIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLS 301
Cdd:cd00308 163 ALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIG 210
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-301 |
2.30e-44 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 155.86 E-value: 2.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 6 VQVHYRNIPLLVPFKTALRQANEIDSIEVEITLDNGIKGTGAAapTVVITGDSTESIMSVAAGPVKE----ALSGHDLR- 80
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEV--VAFEGPFYTEETNATAWHILKDyllpLLLGREFSh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 81 --DFQGALKKVQrcctGNTSAKAAADIALYDAYSKWLNIPLYAYLGGQknlRTSMTIGV-----DTPEKMAWDAEKSVEA 153
Cdd:cd03317 79 peEVSERLAPIK----GNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGT---RDSIPVGVsigiqDDVEQLLKQIERYLEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 154 GFHLLKIKVGtyPEIDLERIEVVRRAVPpDVKLRLDANQAWEPKQAVQiLQELEkkDFGIEFVEQPVRADDWEGLKFVTE 233
Cdd:cd03317 152 GYKRIKLKIK--PGWDVEPLKAVRERFP-DIPLMADANSAYTLADIPL-LKRLD--EYGLLMIEQPLAADDLIDHAELQK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518550582 234 RTKLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLS 301
Cdd:cd03317 226 LLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIG 293
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-301 |
1.80e-40 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 144.98 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 9 HYRnIPLLVPFKTALRQANEIDSIEVEITLDNGIKGTG--AAAPTVVITGDSTESIMSVAAGPVKEALSGhDLRDFQGAL 86
Cdd:TIGR01928 2 HVS-EPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGevVAFQTPWYTHETIATVKHIIEDFFEPNINK-EFEHPSEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 87 KKVQRCcTGNTSAKAAADIALYDAYSKWLNIPLYAYLGGQKNLRTS-MTIGVDTPEKMAWDAEKSVEAGFHLLKIKVGty 165
Cdd:TIGR01928 80 ELVRSL-KGTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAgAVSGLANDEQMLKQIESLKATGYKRIKLKIT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 166 PEIDLERIEVVRRAVPpDVKLRLDANQAWEPKQAVQiLQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESL 245
Cdd:TIGR01928 157 PQIMHQLVKLRRLRFP-QIPLVIDANESYDLQDFPR-LKELD--RYQLLYIEEPFKIDDISMLDELAKGTITPICLDESI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 518550582 246 FSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLS 301
Cdd:TIGR01928 233 TSLDDARNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGIS 288
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
3-327 |
1.10e-35 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 132.18 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 3 IKDVQVHYRNIPLLVPFKTALRQANEIDSIEVEITlDNGIKGTGAAAPTVVItGDSTESIMSVAAGPVKEALSGHDLRDF 82
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELE-EEGIKGTGECTPYPRY-GESDASVMAQIMSVVPQLEKGLTREAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 83 QgalkkvQRCCTGntSAKAAADIALYDAYSKWLNIPLYAYLGGQKNLR--TSMTIGVDTPEKMAWDAEKSVEAGFHLLKI 160
Cdd:PRK15129 79 Q------KLLPAG--AARNAVDCALWDLAARQQQQSLAQLIGITLPETvtTAQTVVIGTPEQMANSASALWQAGAKLLKV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 161 KVGTYpeIDLERIEVVRRAVPpDVKLRLDANQAWEPKQAVQILQELekKDFGIEFVEQPVRADDWEGLK-FVTertKLPV 239
Cdd:PRK15129 151 KLDNH--LISERMVAIRSAVP-DATLIVDANESWRAEGLAARCQLL--ADLGVAMLEQPLPAQDDAALEnFIH---PLPI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 240 MADESLFSaKDALKLIAGRFaDLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLSVaaaAHFAAAHPNVAYMD 319
Cdd:PRK15129 223 CADESCHT-RSSLKALKGRY-EMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAI---SAALPLVPQVRFAD 297
|
....*...
gi 518550582 320 LDAPLWLS 327
Cdd:PRK15129 298 LDGPTWLA 305
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
3-351 |
1.37e-31 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 121.82 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 3 IKDVQVHYRNIPLLVPFKTALRQANEIDSIEVEITLDNGIKGTgaaAPTVVITGDSTESIMSVAAGpVKEALSGHDLRDF 82
Cdd:cd03321 3 ITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGH---SYLFTYTPAALKSLKQLLDD-MAALLVGEPLAPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 83 QGALKKVQR-CCTGNTS----AKAAADIALYDAYSKWLNIPLYAYLGGQ-KNLRTSMTIGVDTPEKMAWDAEKSVEAGFH 156
Cdd:cd03321 79 ELERALAKRfRLLGYTGlvrmAAAGIDMAAWDALAKVHGLPLAKLLGGNpRPVQAYDSHGLDGAKLATERAVTAAEEGFH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 157 LLKIKVGtYP--EIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTER 234
Cdd:cd03321 159 AVKTKIG-YPtaDEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALD--QEGLTWIEEPTLQHDYEGHARIASA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 235 TKLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKcmVGSMMEPSLSVaaaaHFAAAHPN 314
Cdd:cd03321 236 LRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIP--MSSHLFQEISA----HLLAVTPT 309
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 518550582 315 ---VAYMDLDAPLWlsEEPdhLTYDGEDVLLSDQPGIGII 351
Cdd:cd03321 310 ahwLEYVDWAGAIL--EPP--LKFEDGNAVIPDEPGNGII 345
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
136-308 |
2.84e-31 |
|
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239436 [Multi-domain] Cd Length: 263 Bit Score: 118.90 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 136 GVDTPEKMAWDAEKsvEAGFHLLKIKVGTYP-EIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELekKDFGIE 214
Cdd:cd03320 81 AGDAAALGEAKAAY--GGGYRTVKLKVGATSfEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEAL--AAGRIE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 215 FVEQPVRADDWEGLKfvtERTK-LPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVG 293
Cdd:cd03320 157 YIEQPLPPDDLAELR---RLAAgVPIALDESLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVS 233
|
170
....*....|....*
gi 518550582 294 SMMEPSLSVAAAAHF 308
Cdd:cd03320 234 SALESSIGLGALAHL 248
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
98-288 |
3.33e-29 |
|
D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239441 [Multi-domain] Cd Length: 352 Bit Score: 115.12 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 98 SAKAAADIALYDAYSKWLNIPLYAYLGGQ--KNLRTSMTIGVDTPEKMAWDAEKSVEAGFHLLK---------IKVGTYP 166
Cdd:cd03325 80 SAISGIDQALWDIKGKVLGVPVHQLLGGQvrDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 167 EIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESLF 246
Cdd:cd03325 160 DAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELE--PYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLF 237
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518550582 247 SAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGV 288
Cdd:cd03325 238 SRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDV 279
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
61-302 |
4.00e-29 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239444 [Multi-domain] Cd Length: 352 Bit Score: 115.20 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 61 SIMSVAAGPVKEALSGHDLRDFQGALKKVQRCCTGN------TSAKAAADIALYDAYSKWLNIPLYAYLGGQknlRTSMT 134
Cdd:cd03328 51 AAAALVDGLLAPVVEGRDALDPPAAWEAMQRAVRNAgrpgvaAMAISAVDIALWDLKARLLGLPLARLLGRA---HDSVP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 135 I----GVDT--PEKMAWDAEKSVEAGFHLLKIKVGTYPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEk 208
Cdd:cd03328 128 VygsgGFTSydDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFA- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 209 kDFGIEFVEQPVRADDWEGLKFVTERT--KLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEAN 286
Cdd:cd03328 207 -DEGVTWFEEPVSSDDLAGLRLVRERGpaGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAH 285
|
250
....*....|....*.
gi 518550582 287 GVKcmVGSMMEPSLSV 302
Cdd:cd03328 286 HVD--LSAHCAPALHA 299
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
140-235 |
4.31e-29 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 107.75 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 140 PEKMAWDAEKSVEA-GFHLLKIKVGTYPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQ 218
Cdd:smart00922 1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALD--ELGLEWIEE 78
|
90
....*....|....*..
gi 518550582 219 PVRADDWEGLKFVTERT 235
Cdd:smart00922 79 PVPPDDLEGLAELRRAT 95
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
99-288 |
2.53e-26 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239443 [Multi-domain] Cd Length: 341 Bit Score: 107.03 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 99 AKAAADIALYDAYSKWLNIPLYAYLGG--QKNLRTSMT-IGVDTPEKMAWDAEKSVEAGFHLLKIKVGTYP-------EI 168
Cdd:cd03327 77 AISAVDLALWDLLGKIRGEPVYKLLGGrtRDKIPAYASgLYPTDLDELPDEAKEYLKEGYRGMKMRFGYGPsdghaglRK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 169 DLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEKkdFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESLFSA 248
Cdd:cd03327 157 NVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEK--YELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTV 234
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518550582 249 KDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGV 288
Cdd:cd03327 235 YGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGV 274
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
96-288 |
2.58e-25 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 104.98 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 96 NTSAKAAADIALYDAYSKWLNIPLYAYLGGQ--KNLRTSMTIGVDTPEKMAWDAEKSVEAGFHLLKIK-------VGTYP 166
Cdd:PRK14017 79 LMSAIAGIDQALWDIKGKALGVPVHELLGGLvrDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMNgteelqyIDSPR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 167 EID--LERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVEQPVRADDWEGLKFVTERTKLPVMADES 244
Cdd:PRK14017 159 KVDaaVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELE--PYRPMFIEEPVLPENAEALPEIAAQTSIPIATGER 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518550582 245 LFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGV 288
Cdd:PRK14017 237 LFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDV 280
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
159-300 |
6.26e-20 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 88.87 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 159 KIKV---GTYPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkKDFGIEFVEQPVRAddWEGLKFVTERT 235
Cdd:PRK02901 107 KVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALD-ADGPLEYVEQPCAT--VEELAELRRRV 183
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518550582 236 KLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGIseaWKIADIAEANGVKCMVGSMMEPSL 300
Cdd:PRK02901 184 GVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGV---RAALDIAEQIGLPVVVSSALDTSV 245
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
2-290 |
1.20e-18 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 85.91 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 2 IIKDVQVH---YRNIPllVPFK---TALRQANEIDSIEVEITLDNGIKGTGAAAPTVvITGDSTESImsvaagpVKEALS 75
Cdd:cd03329 1 KITDVEVTvfeYPTQP--VSFDgghHHPGPAGTRKLALLTIETDEGAKGHAFGGRPV-TDPALVDRF-------LKKVLI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 76 GHDLRD---FQGALKKVQRCCTgnTSAKAAADIALYDAYSKWLNIPLYAYLGGQKN----LRTSMT----IGVDTPEKMA 144
Cdd:cd03329 71 GQDPLDrerLWQDLWRLQRGLT--DRGLGLVDIALWDLAGKYLGLPVHRLLGGYREkipaYASTMVgddlEGLESPEAYA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 145 WDAEKSVEAGFHLLKIK--VGTYPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEKKDFgiEFVEQPVRA 222
Cdd:cd03329 149 DFAEECKALGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGF--FWYEDPLRE 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518550582 223 DDWEGLKFVTERTKLPVMADESLFSAKDAL-KLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKC 290
Cdd:cd03329 227 ASISSYRWLAEKLDIPILGTEHSRGALESRaDWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDV 295
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
98-289 |
4.62e-16 |
|
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.
Pssm-ID: 239438 [Multi-domain] Cd Length: 361 Bit Score: 78.25 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 98 SAKAAADIALYDAYSKWLNIPLYAYLGGQKN---LRTSMTIGVDTPEKMAwDAEKSVEAGFHLLKIKVGTYpeidlerIE 174
Cdd:cd03322 83 NAIAAVDMALWDIKGKAAGMPLYQLLGGKSRdgiMVYSHASGRDIPELLE-AVERHLAQGYRAIRVQLPKL-------FE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 175 VVRRAVPPDVKLRLDANQAWEPKQAVQILQELEKkdFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESLFSAKDALKL 254
Cdd:cd03322 155 AVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEP--YRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNL 232
|
170 180 190
....*....|....*....|....*....|....*
gi 518550582 255 IAGRFADLINIKLMKCGGISEAWKIADIAEANGVK 289
Cdd:cd03322 233 IQERLIDYIRTTVSHAGGITPARKIADLASLYGVR 267
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
154-301 |
1.14e-14 |
|
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441050 [Multi-domain] Cd Length: 325 Bit Score: 73.76 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 154 GFHLLKIKVGTY-PEIDLERIEVVRRAVPpDVKLRLDANQAWEPKQAVQILQELEKKDFG-IEFVEQPVRADDwEGLKFv 231
Cdd:COG1441 128 GEKVAKVKVGLYeAVRDGMVVNLLLEAIP-DLRLRLDANRSWTLDKAVQFAKYVNPEHRSrIAFLEEPCKTPE-ESREF- 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 232 TERTKLPVMADESLFSAKDALKLIAGRFAdlINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLS 301
Cdd:COG1441 205 ARETGIAIAWDESVREPDFRVEAEPGVAA--IVIKPTLVGSLQRCRQLIEQAHQLGLQAVISSSIESSLG 272
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
154-301 |
2.91e-14 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 72.53 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 154 GFHLLKIKVGTY-PEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEKKDFG-IEFVEQPVRADDwEGLKFv 231
Cdd:TIGR01927 124 GFRTFKWKVGVGeLAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDPNLRGrIAFLEEPLPDAD-EMSAF- 201
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 232 TERTKLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSLS 301
Cdd:TIGR01927 202 SEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIA 271
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
141-227 |
1.04e-13 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239440 [Multi-domain] Cd Length: 415 Bit Score: 71.60 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 141 EKMAWDAEKSVEAGFHLLKIKVGTYPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEKkdFGIEFVEQPV 220
Cdd:cd03324 198 EKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAE--FKPWWIEEPT 275
|
....*..
gi 518550582 221 RADDWEG 227
Cdd:cd03324 276 SPDDILG 282
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
154-300 |
9.62e-13 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 67.94 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 154 GFHLLKIKVGTY-PEIDLERIEVVRRAVPpDVKLRLDANQAWEPKQAVQILQELEKKDFG-IEFVEQPVRADDwEGLKFV 231
Cdd:PRK05105 128 GEKVAKVKVGLYeAVRDGMLVNLLLEAIP-DLKLRLDANRGWTLEKAQQFAKYVPPDYRHrIAFLEEPCKTPD-DSRAFA 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518550582 232 TErTKLPVMADESLFSAKDALKLIAGRFAdlINIKLMKCGGISEAWKIADIAEANGVKCMVGSMMEPSL 300
Cdd:PRK05105 206 RA-TGIAIAWDESLREPDFQFEAEPGVRA--IVIKPTLTGSLEKCQELIEQAHALGLRAVISSSIESSL 271
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
139-302 |
3.27e-12 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 67.96 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 139 TPEKMAWDAEKSVEAGFHLLKIKVG--TYPEIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQIlqELEKKDFGIEFV 216
Cdd:PLN02980 1090 SPLEVAYVARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEF--GSLVKSCNLKYI 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 217 EQPVRADDwEGLKFvTERTKLPVMADESLFSAKDALKLIAGRFAD----LINIKLMKCGGISEAWKIADIAEANGVKCMV 292
Cdd:PLN02980 1168 EEPVQDED-DLIKF-CEETGLPVALDETIDKFEECPLRMLTKYTHpgivAVVIKPSVVGGFENAALIARWAQQHGKMAVI 1245
|
170
....*....|
gi 518550582 293 GSMMEPSLSV 302
Cdd:PLN02980 1246 SAAYESGLGL 1255
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
14-124 |
1.87e-10 |
|
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold similarity with enolase N-terminal domain.
Pssm-ID: 397046 [Multi-domain] Cd Length: 117 Bit Score: 57.87 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 14 PLLVPFKTALRQANEIDSIEVEITLDNGIKGTGAAaptvVITGDSTESIMSVAAGPVKEALSGHDLRDFQGALKKVQRCC 93
Cdd:pfam02746 11 WPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEA----TSYGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAA 86
|
90 100 110
....*....|....*....|....*....|.
gi 518550582 94 TGNTSAKAAADIALYDAYSKWLNIPLYAYLG 124
Cdd:pfam02746 87 LGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
98-289 |
1.35e-09 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 59.15 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 98 SAKAAADIALYDAYSKWLNIPLYAYLGGQKnlRTSMTI-----GVDTPEKMAwDAEKSVEAGFHLLKIKVG------TY- 165
Cdd:PRK15072 84 SAIAAVDMALWDIKAKAAGMPLYQLLGGAS--REGVMVyghanGRDIDELLD-DVARHLELGYKAIRVQCGvpglktTYg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 166 -----------------PEIDL-----------ERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEkkDFGIEFVE 217
Cdd:PRK15072 161 vskgkglayepatkgllPEEELwstekylrfvpKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLE--PYRLFWLE 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518550582 218 QPVRADDWEGLKFVTERTKLPVMADESLFSAKDALKLIAGRFADLINIKLMKCGGISEAWKIADIAEANGVK 289
Cdd:PRK15072 239 DPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVR 310
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
146-249 |
1.47e-09 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 58.49 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 146 DAEKSVEAGFHLLKIKVGTYP-EIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELEKKDFG-IEFVEQPVRAD 223
Cdd:PRK02714 125 QWQTLWQQGYRTFKWKIGVDPlEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDRRLSGkIEFIEQPLPPD 204
|
90 100
....*....|....*....|....*.
gi 518550582 224 DWEGLKFVTERTKLPVMADESLFSAK 249
Cdd:PRK02714 205 QFDEMLQLSQDYQTPIALDESVANLA 230
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
99-287 |
2.08e-09 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239442 [Multi-domain] Cd Length: 385 Bit Score: 58.56 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 99 AKAAADIALYDAYSKWLNIPLYAYLG-----GQKNLRTSMTIG------VDTPEKMAWDAEKSVEAGFHLLKIKVGTYP- 166
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAAggyyypGDDLGRLRDEMRRYLDRGYTVVKIKIGGAPl 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 167 EIDLERIEVVRRAVPPDVKLRLDANQAWEPKQAVQILQELekKDFGIEFVEQPVRADDWEGLKFVTERTKLPVMADESLF 246
Cdd:cd03326 189 DEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKAL--APYGLRWYEEPGDPLDYALQAELADHYDGPIATGENLF 266
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518550582 247 SAKDALKLI--AGRFADLiNIKLMKCG---GISEAWKIADIAEANG 287
Cdd:cd03326 267 SLQDARNLLryGGMRPDR-DVLQFDPGlsyGLPEYLRMLDVLEAHG 311
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
97-239 |
7.84e-08 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 53.48 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 97 TSAKAAADIALYDAYSKWLNIPLYAYLGGQknLRTSMTIG-------------------------VDTPEKMAWDAEKSV 151
Cdd:cd03323 103 VHVVTAFEVALLDLLGQALGVPVADLLGGG--QRDSVPFLaylfykgdrhktdlpypwfrdrwgeALTPEGVVRLARAAI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518550582 152 EA-GFHLLKIKVGTY-PEIDLERIEVVRRAVPpDVKLRLDANQAWEPKQAVQILQELEKKdfgIEFVEQPVRADdwEGLK 229
Cdd:cd03323 181 DRyGFKSFKLKGGVLpGEEEIEAVKALAEAFP-GARLRLDPNGAWSLETAIRLAKELEGV---LAYLEDPCGGR--EGMA 254
|
170
....*....|
gi 518550582 230 FVTERTKLPV 239
Cdd:cd03323 255 EFRRATGLPL 264
|
|
| |
