|
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 ... |
3-304 |
1.06e-110 |
|
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: 324.14 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 3 HMQIETVNLPLARPMAAENGTRHAVTVIRVALEEKGFIGQGECTPAAH-YGESADSVCRQLSAIREAIENG-----LTIE 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGdprleKLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 77 QLQQNLSP-GAARNALDCALWRLNTALEKQTLWQRVGIHPPTSVVCAQTLALDSVEKMATAASNAVSHGALLLKIKL--D 153
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLggD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 154 RELILEKVAAIRAAAPNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRF--AHPIPICADESCRHS 231
Cdd:cd03319 161 LEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLrdKSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1850706165 232 GDIVGLR--RRYDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVA-ADAEHVDLDGPIWL 304
Cdd:cd03319 241 ADAARLAggGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAaAKADFVDLDGPLLL 316
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
1-321 |
3.01e-110 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 323.24 E-value: 3.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 1 MRHMQIETVNLPLARPMAAENGTRHAVTVIRVALEEKGFIGQGECTPAAHYGESADSVCRQLSAIREAIENGLTIEQLQQ 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 81 NLSPGAARNALDCALWRLNTALEKQTLWQRVGIHPPTSVVCAQTLALDSVEKMATAASNAVSHGALLLKIKLDRELILEK 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 161 VAAIRAAAPNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAHPIPICADESCRHSGDIVGLRRR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 241 YDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAADAEHVDLDGPIWLAADSSPYLTYNLGRIW 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 1850706165 321 L 321
Cdd:PRK15129 321 L 321
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-307 |
2.94e-55 |
|
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: 183.48 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 1 MRHMQIET--VNLPLARPMAAENGTRHAVTVIRVALE-EKGFIGQGECTPaahYGESADSVCRQLS-AIREAI--ENGLT 74
Cdd:COG4948 1 MKITDIEVypVRLPLKRPFTISRGTRTERDVVLVRVEtDDGITGWGEAVP---GGTGAEAVAAALEeALAPLLigRDPLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 75 IEQLQQNLS-----PGAARNALDCALW-----RLNtalekQTLWQRVGIHPPTSVVCAQTLALDSVEKMATAASNAVSHG 144
Cdd:COG4948 78 IEALWQRLYralpgNPAAKAAVDMALWdllgkALG-----VPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 145 ALLLKIKL---DRELILEKVAA-IRAAAPNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAH-- 218
Cdd:COG4948 153 FRALKLKVggpDPEEDVERVRAvREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRat 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 219 PIPICADESCRHSGDIVGL--RRRYDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAA---DA 293
Cdd:COG4948 233 PVPIAADESLTSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAalpNF 312
|
330
....*....|....
gi 1850706165 294 EHVDLDGPIWLAAD 307
Cdd:COG4948 313 DIVELDGPLLLADD 326
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
172-291 |
2.88e-14 |
|
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: 70.67 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 172 RLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAH--PIPICADESCRHSGDIvglrRRY------DM 243
Cdd:pfam13378 46 DLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRatPVPIATGESLYSREDF----RRLleagavDI 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1850706165 244 INIKLDKCGGLTEALAMVREAHFHGLRIMVGCtLGSSMAMEAALPVAA 291
Cdd:pfam13378 122 VQPDVTRVGGITEALKIAALAEAFGVPVAPHS-GGGPIGLAASLHLAA 168
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
12-306 |
3.94e-09 |
|
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: 56.74 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 12 PLARPMAAENGTRHAVTVIR----VALEEKGFIGQGECTPAAHYG----ESADSVCRQLsaireaIENgltIEQLQQNLS 83
Cdd:TIGR01927 2 RYQMPFDAPVVTRHGLLARRegliVRLTDEGRTGWGEIAPLPGFGtetlAEALDFCRAL------IEE---ITRGDIEAI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 84 PG---AARNALDCALWRLNTALEkqtlwqrvgiHPPTSVVCAQTLALDSVEKMATAASNAVSHGALLLKIKL---DREL- 156
Cdd:TIGR01927 73 DDqlpSVAFGFESALIELESGDE----------LPPASNYYVALLPAGDPALLLLRSAKAEGFRTFKWKVGVgelAREGm 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 157 ILEKVAAIRAAAPNARLiiDARASWSGLDLHSLSTAL---LPYQVAMIEQPLPVGKDE-DLQRfAHPIPICADESCRHSG 232
Cdd:TIGR01927 143 LVNLLLEALPDKAELRL--DANGGLSPDEAQQFLKALdpnLRGRIAFLEEPLPDADEMsAFSE-ATGTAIALDESLWELP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 233 DIV-----GLRrryDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAAD---AEHVDLDGPIWL 304
Cdd:TIGR01927 220 QLAdeygpGWR---GALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKlspDPAAVGFTTALL 296
|
..
gi 1850706165 305 AA 306
Cdd:TIGR01927 297 RA 298
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
172-222 |
1.81e-05 |
|
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: 42.65 E-value: 1.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1850706165 172 RLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAHPIPI 222
Cdd:smart00922 47 DLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| |
|
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 ... |
3-304 |
1.06e-110 |
|
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: 324.14 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 3 HMQIETVNLPLARPMAAENGTRHAVTVIRVALEEKGFIGQGECTPAAH-YGESADSVCRQLSAIREAIENG-----LTIE 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGdprleKLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 77 QLQQNLSP-GAARNALDCALWRLNTALEKQTLWQRVGIHPPTSVVCAQTLALDSVEKMATAASNAVSHGALLLKIKL--D 153
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLggD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 154 RELILEKVAAIRAAAPNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRF--AHPIPICADESCRHS 231
Cdd:cd03319 161 LEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLrdKSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1850706165 232 GDIVGLR--RRYDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVA-ADAEHVDLDGPIWL 304
Cdd:cd03319 241 ADAARLAggGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAaAKADFVDLDGPLLL 316
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
1-321 |
3.01e-110 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 323.24 E-value: 3.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 1 MRHMQIETVNLPLARPMAAENGTRHAVTVIRVALEEKGFIGQGECTPAAHYGESADSVCRQLSAIREAIENGLTIEQLQQ 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 81 NLSPGAARNALDCALWRLNTALEKQTLWQRVGIHPPTSVVCAQTLALDSVEKMATAASNAVSHGALLLKIKLDRELILEK 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 161 VAAIRAAAPNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAHPIPICADESCRHSGDIVGLRRR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 241 YDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAADAEHVDLDGPIWLAADSSPYLTYNLGRIW 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 1850706165 321 L 321
Cdd:PRK15129 321 L 321
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-307 |
2.94e-55 |
|
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: 183.48 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 1 MRHMQIET--VNLPLARPMAAENGTRHAVTVIRVALE-EKGFIGQGECTPaahYGESADSVCRQLS-AIREAI--ENGLT 74
Cdd:COG4948 1 MKITDIEVypVRLPLKRPFTISRGTRTERDVVLVRVEtDDGITGWGEAVP---GGTGAEAVAAALEeALAPLLigRDPLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 75 IEQLQQNLS-----PGAARNALDCALW-----RLNtalekQTLWQRVGIHPPTSVVCAQTLALDSVEKMATAASNAVSHG 144
Cdd:COG4948 78 IEALWQRLYralpgNPAAKAAVDMALWdllgkALG-----VPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 145 ALLLKIKL---DRELILEKVAA-IRAAAPNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAH-- 218
Cdd:COG4948 153 FRALKLKVggpDPEEDVERVRAvREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRat 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 219 PIPICADESCRHSGDIVGL--RRRYDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAA---DA 293
Cdd:COG4948 233 PVPIAADESLTSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAalpNF 312
|
330
....*....|....
gi 1850706165 294 EHVDLDGPIWLAAD 307
Cdd:COG4948 313 DIVELDGPLLLADD 326
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
86-298 |
6.07e-21 |
|
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: 90.09 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 86 AARNALDCALWRLNTALEKQTLwQRVGIHPPTSVVCAQTLALDSVEKMATAASNAVSHG--ALLLKIKLDRELILEKVAA 163
Cdd:cd03315 43 ATKAAVDMALWDLWGKRLGVPV-YLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGfrTFKLKVGRDPARDVAVVAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 164 IRAAA-PNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAH--PIPICADESCRHSGDIVGL--R 238
Cdd:cd03315 122 LREAVgDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARatDTPIMADESAFTPHDAFRElaL 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 239 RRYDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAADAEHVDL 298
Cdd:cd03315 202 GAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTL 261
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
85-291 |
2.01e-19 |
|
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: 85.07 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 85 GAARNALDCALWRLntalekqtlwqrvgihpptsvvCAQTLALDSVEKMATAASNAVSHGALLLKIKLDRELILEKVaai 164
Cdd:cd00308 41 GEVISGIDMALWDL----------------------AAKALGVPLAELLGGGSRDRVPAYGSIERVRAVREAFGPDA--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 165 raaapnaRLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFA--HPIPICADESCRHSGDI--VGLRRR 240
Cdd:cd00308 96 -------RLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRrrTGIPIAADESVTTVDDAleALELGA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1850706165 241 YDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAA 291
Cdd:cd00308 169 VDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAA 219
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
9-274 |
1.49e-14 |
|
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: 73.42 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 9 VNLPLARPMAAENGT---RHaVTVIRVALEEkGFIGQGECT--PAAHYGESADSVCRqlsairEAIENGLTIEQLQQNLS 83
Cdd:cd03317 6 VRMPLKFPFETSFGTlneRE-FLIVELTDEE-GITGYGEVVafEGPFYTEETNATAW------HILKDYLLPLLLGREFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 84 ------------PGA--ARNALDCALWRLNTALEKQTLWQRVGiHPPTSVVCAQTLAL-DSVEKMATAASNAVSHGALLL 148
Cdd:cd03317 78 hpeevserlapiKGNnmAKAGLEMAVWDLYAKAQGQSLAQYLG-GTRDSIPVGVSIGIqDDVEQLLKQIERYLEEGYKRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 149 KIKLDRELILEKVAAIRAAAPNARLIIDARASWSGLDLHSLStALLPYQVAMIEQPLPVGKDEDLQRFAHPI--PICADE 226
Cdd:cd03317 157 KLKIKPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLK-RLDEYGLLMIEQPLAADDLIDHAELQKLLktPICLDE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1850706165 227 SCRHSGDivgLRRRYDM-----INIKLDKCGGLTEALAMVREAHFHGLRIMVG 274
Cdd:cd03317 236 SIQSAED---ARKAIELgackiINIKPGRVGGLTEALKIHDLCQEHGIPVWCG 285
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
172-291 |
2.88e-14 |
|
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: 70.67 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 172 RLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAH--PIPICADESCRHSGDIvglrRRY------DM 243
Cdd:pfam13378 46 DLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRatPVPIATGESLYSREDF----RRLleagavDI 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1850706165 244 INIKLDKCGGLTEALAMVREAHFHGLRIMVGCtLGSSMAMEAALPVAA 291
Cdd:pfam13378 122 VQPDVTRVGGITEALKIAALAEAFGVPVAPHS-GGGPIGLAASLHLAA 168
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
83-291 |
4.41e-13 |
|
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: 68.06 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 83 SPGAARNALDCALWRLNTALEKQTLWQRvgihpptSVVCAQTLALDSVEKMATAASnAVSHGALLLKIK-----LDREL- 156
Cdd:cd03320 44 APLPLAFGIESALANLEALLVGFTRPRN-------RIPVNALLPAGDAAALGEAKA-AYGGGYRTVKLKvgatsFEEDLa 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 157 ILEKVAAIRAAAPNARLiiDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAHPIPICADESCRHSGDIVG 236
Cdd:cd03320 116 RLRALREALPADAKLRL--DANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAAGVPIALDESLRRLDDPLA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1850706165 237 LRRRY--DMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAA 291
Cdd:cd03320 194 LAAAGalGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAA 250
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
9-307 |
1.24e-11 |
|
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: 64.65 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 9 VNLPLARPMAAENGTRHAVTVIRVAL-EEKGFIGQGECTP---AAHYGESADSVCRQLS------AIREAIENGLTIEQL 78
Cdd:cd03318 10 VDLPTRRPHQFAGTTMHTQSLVLVRLtTSDGVVGIGEATTpggPAWGGESPETIKAIIDrylaplLIGRDATNIGAAMAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 79 QQNLSPGA--ARNALDCALWRLNTALEKQTLWQRVGIHPPTSVVCAQTLA-------LDSVEKMATAASnavsHGALLLK 149
Cdd:cd03318 90 LDRAVAGNlfAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLAsgdterdIAEAEEMLEAGR----HRRFKLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 150 I-KLDRELILEKVAA-IRAAAPNARLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAH--PIPICAD 225
Cdd:cd03318 166 MgARPPADDLAHVEAiAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSrnRVPIMAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 226 ESCRHSGDIVGLRRR--YDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAADAEHVD----LD 299
Cdd:cd03318 246 ESVSGPADAFELARRgaADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPfgceLF 325
|
....*...
gi 1850706165 300 GPIWLAAD 307
Cdd:cd03318 326 GPLLLAED 333
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
12-306 |
3.94e-09 |
|
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: 56.74 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 12 PLARPMAAENGTRHAVTVIR----VALEEKGFIGQGECTPAAHYG----ESADSVCRQLsaireaIENgltIEQLQQNLS 83
Cdd:TIGR01927 2 RYQMPFDAPVVTRHGLLARRegliVRLTDEGRTGWGEIAPLPGFGtetlAEALDFCRAL------IEE---ITRGDIEAI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 84 PG---AARNALDCALWRLNTALEkqtlwqrvgiHPPTSVVCAQTLALDSVEKMATAASNAVSHGALLLKIKL---DREL- 156
Cdd:TIGR01927 73 DDqlpSVAFGFESALIELESGDE----------LPPASNYYVALLPAGDPALLLLRSAKAEGFRTFKWKVGVgelAREGm 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 157 ILEKVAAIRAAAPNARLiiDARASWSGLDLHSLSTAL---LPYQVAMIEQPLPVGKDE-DLQRfAHPIPICADESCRHSG 232
Cdd:TIGR01927 143 LVNLLLEALPDKAELRL--DANGGLSPDEAQQFLKALdpnLRGRIAFLEEPLPDADEMsAFSE-ATGTAIALDESLWELP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 233 DIV-----GLRrryDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGSSMAMEAALPVAAD---AEHVDLDGPIWL 304
Cdd:TIGR01927 220 QLAdeygpGWR---GALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKlspDPAAVGFTTALL 296
|
..
gi 1850706165 305 AA 306
Cdd:TIGR01927 297 RA 298
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
6-311 |
4.12e-09 |
|
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: 56.85 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 6 IETVNLPLARPMAAENGTRHAVTVIRVALEEkGFIGQGECTPAAHYGESADSVCRQLSAI---REAIENGLTIEQLQQNL 82
Cdd:cd03316 5 VETFVLRVPLPEPGGAVTWRNLVLVRVTTDD-GITGWGEAYPGGRPSAVAAAIEDLLAPLligRDPLDIERLWEKLYRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 83 SPGAARN-------ALDCALWRLNTALEKQTLWQRVG--IHPPTSVVCAQTLALDSVEKMATAASNAVSHGALLLKIKLD 153
Cdd:cd03316 84 FWRGRGGvamaaisAVDIALWDIKGKAAGVPVYKLLGgkVRDRVRVYASGGGYDDSPEELAEEAKRAVAEGFTAVKLKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 154 RELILEKVAAIRAAAPNA---------RLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAH--PIPI 222
Cdd:cd03316 164 GPDSGGEDLREDLARVRAvreavgpdvDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQatSVPI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 223 CADEscrHSGDIVGLR-----RRYDMINIKLDKCGGLTEALAMVREAHFHGLRIMVGCTLGS-----SMAMEAALPVAAD 292
Cdd:cd03316 244 AAGE---NLYTRWEFRdlleaGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPiglaaSLHLAAALPNFGI 320
|
330
....*....|....*....
gi 1850706165 293 AEHVDLDGPIWLAADSSPY 311
Cdd:cd03316 321 LEYHLDDLPLREDLFKNPP 339
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
6-112 |
1.18e-05 |
|
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: 44.00 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 6 IETVNLPLARPMAAENGTRHAVT-----VIRVALEEkGFIGQGECTP-----AAHYGESADSVCRQLSAIREAIENGLTI 75
Cdd:pfam02746 2 IEVFVVDVGWPLRPIQMAFGTVQqqslvIVRIETSE-GVVGIGEATSyggraETIKAILDDHLAPLLIGRDAANISDLWQ 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1850706165 76 EQLQQNLSPGAARNALDCALWRLNTALEKQTLWQRVG 112
Cdd:pfam02746 81 LMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
172-222 |
1.81e-05 |
|
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: 42.65 E-value: 1.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1850706165 172 RLIIDARASWSGLDLHSLSTALLPYQVAMIEQPLPVGKDEDLQRFAHPIPI 222
Cdd:smart00922 47 DLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
12-227 |
2.16e-04 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 42.31 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 12 PLARPMAaengTRHAVTVIR----VALE-EKGFIGQGECTPAAHYG----ESADSVCRQLsaireaiENGLTIEQLQQ-- 80
Cdd:PRK02714 13 PFRQPLQ----TAHGLWRIRegiiLRLTdETGKIGWGEIAPLPWFGsetlEEALAFCQQL-------PGEITPEQIFSip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 81 -NLsPgAARNALDCAL-WRLNTalekqtlWQRVGIHPPTSvvCAqtlALDSVEKMATAASNAVSHGALLLKIK-----LD 153
Cdd:PRK02714 82 dAL-P-ACQFGFESALeNESGS-------RSNVTLNPLSY--SA---LLPAGEAALQQWQTLWQQGYRTFKWKigvdpLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850706165 154 REL-ILEKVAAIRAAAPNARLiiDARASWSGLDLH---SLSTALLPYQVAMIEQPLPVGKDEDLQRF--AHPIPICADES 227
Cdd:PRK02714 148 QELkIFEQLLERLPAGAKLRL--DANGGLSLEEAKrwlQLCDRRLSGKIEFIEQPLPPDQFDEMLQLsqDYQTPIALDES 225
|
|
| |
