|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
1-321 |
0e+00 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 631.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 1 MRNLRVYEEAWPLHTPFVIARGSRSEAKVVVVEIEEDGVKGVGECTPYPRYGESIASVMAQILTIGEQLESGITREQLQH 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 81 LLPAGAARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDNHLISER 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 161 LIAIRNVVPEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIHPLPVCADESCHTRDSLPQLRGR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 241 YEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLAPLARFADLDGPTWLAVDVEPALHFSTGVLH 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 695765033 321 L 321
Cdd:PRK15129 321 L 321
|
|
| 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 |
1.36e-130 |
|
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: 374.60 E-value: 1.36e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 3 NLRVYEEAWPLHTPFVIARGSRSEAKVVVVEIEEDGVKGVGECTPYPR-YGESIASVMAQILTIGEQLESGI-----TRE 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGDprlekLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 77 QLQHLLPA-GAARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDNH 155
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 156 LIS--ERLIAIRNVVPEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFI--HPLPVCADESCHTR 231
Cdd:cd03319 161 LEDdiERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRdkSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765033 232 DSLPQLRG--RYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLAPL-ARFADLDGPTWL 304
Cdd:cd03319 241 ADAARLAGggAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAAkADFVDLDGPLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-321 |
2.73e-82 |
|
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: 253.21 E-value: 2.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 1 MRNLRVYEEAWPLHTPFVIARGSRSEAKVVVVEIE-EDGVKGVGECTPYPRYGESIASVMAQILT---IGEQLES--GIT 74
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVEtDDGITGWGEAVPGGTGAEAVAAALEEALApllIGRDPLDieALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 75 REQLQHLLPAGAARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDN 154
Cdd:COG4948 83 QRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLKVGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 155 HLIS---ERLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIH--PLPVCADESC 228
Cdd:COG4948 163 PDPEedvERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatPVPIAADESL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 229 HTRDSLPQL--RGRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLA---PLARFADLDGPTW 303
Cdd:COG4948 243 TSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAaalPNFDIVELDGPLL 322
|
330
....*....|....*....
gi 695765033 304 LAVD-VEPALHFSTGVLHL 321
Cdd:COG4948 323 LADDlVEDPLRIEDGYLTV 341
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
1-112 |
9.52e-27 |
|
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: 101.78 E-value: 9.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 1 MRNLRVYEEAWPLHtPFVIARGSRSEAKVVVVEIE-EDGVKGVGECTPYP-----RYGESIASVMAQILTIGEQLESGIT 74
Cdd:pfam02746 1 AIEVFVVDVGWPLR-PIQMAFGTVQQQSLVIVRIEtSEGVVGIGEATSYGgraetIKAILDDHLAPLLIGRDAANISDLW 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 695765033 75 REQLQHLLPAGAARNAVDCALWDLQARRVGKTIPQLLG 112
Cdd:pfam02746 80 QLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
130-213 |
4.79e-15 |
|
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: 69.62 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 130 PEQMAASAA-ALWEKGARLLKVKLDNHLIS--ERLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPL 205
Cdd:smart00922 1 PEELAEAARrAVAEAGFRAVKVKVGGGPLEdlARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
....*...
gi 695765033 206 PADADDAL 213
Cdd:smart00922 81 PPDDLEGL 88
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-296 |
4.69e-10 |
|
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: 59.44 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 7 YEEAWPLHTPFVIARGSRSEAKVVVVEIEEDGVKGVGECTPYPRYG-ESIASVMAQILTIGEQLESGITrEQLQHLLPAG 85
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDEGRTGWGEIAPLPGFGtETLAEALDFCRALIEEITRGDI-EAIDDQLPSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 86 AArnAVDCALWDLQArrvGKTIPqllgiglPNRVVTAQTVVIGTPEqmAASAAALWEKGARLLKVKLD-NHLISERLI-- 162
Cdd:TIGR01927 80 AF--GFESALIELES---GDELP-------PASNYYVALLPAGDPA--LLLLRSAKAEGFRTFKWKVGvGELAREGMLvn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 163 AIRNVVPE-ATLIVDANESWSGDGLAARCQLLA-DIG--VAMLEQPLPaDADDALENFI-HPLPVCADESCHTRDSLPQL 237
Cdd:TIGR01927 146 LLLEALPDkAELRLDANGGLSPDEAQQFLKALDpNLRgrIAFLEEPLP-DADEMSAFSEaTGTAIALDESLWELPQLADE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765033 238 --RGRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLgcmlctSRAISAALPLAPLARFA 296
Cdd:TIGR01927 225 ygPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVF------SSVFESSIALGQLARLA 279
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
1-321 |
0e+00 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 631.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 1 MRNLRVYEEAWPLHTPFVIARGSRSEAKVVVVEIEEDGVKGVGECTPYPRYGESIASVMAQILTIGEQLESGITREQLQH 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 81 LLPAGAARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDNHLISER 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 161 LIAIRNVVPEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIHPLPVCADESCHTRDSLPQLRGR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 241 YEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLAPLARFADLDGPTWLAVDVEPALHFSTGVLH 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 695765033 321 L 321
Cdd:PRK15129 321 L 321
|
|
| 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 |
1.36e-130 |
|
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: 374.60 E-value: 1.36e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 3 NLRVYEEAWPLHTPFVIARGSRSEAKVVVVEIEEDGVKGVGECTPYPR-YGESIASVMAQILTIGEQLESGI-----TRE 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGDprlekLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 77 QLQHLLPA-GAARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDNH 155
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 156 LIS--ERLIAIRNVVPEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFI--HPLPVCADESCHTR 231
Cdd:cd03319 161 LEDdiERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRdkSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765033 232 DSLPQLRG--RYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLAPL-ARFADLDGPTWL 304
Cdd:cd03319 241 ADAARLAGggAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAAkADFVDLDGPLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-321 |
2.73e-82 |
|
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: 253.21 E-value: 2.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 1 MRNLRVYEEAWPLHTPFVIARGSRSEAKVVVVEIE-EDGVKGVGECTPYPRYGESIASVMAQILT---IGEQLES--GIT 74
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVEtDDGITGWGEAVPGGTGAEAVAAALEEALApllIGRDPLDieALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 75 REQLQHLLPAGAARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDN 154
Cdd:COG4948 83 QRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLKVGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 155 HLIS---ERLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIH--PLPVCADESC 228
Cdd:COG4948 163 PDPEedvERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatPVPIAADESL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 229 HTRDSLPQL--RGRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLA---PLARFADLDGPTW 303
Cdd:COG4948 243 TSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAaalPNFDIVELDGPLL 322
|
330
....*....|....*....
gi 695765033 304 LAVD-VEPALHFSTGVLHL 321
Cdd:COG4948 323 LADDlVEDPLRIEDGYLTV 341
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
12-298 |
7.51e-30 |
|
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: 114.36 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 12 PLHTPFVIARGSRSEAKVVVVEI-EEDGVKGVGEctpyprygesiasvmaqiltigeqlesgitreqlqhllpagAARNA 90
Cdd:cd03315 9 PLKRPLKWASGTLTTADHVLLRLhTDDGLVGWAE-----------------------------------------ATKAA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 91 VDCALWDLQARRVGKTIPQLLGiGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDNHLIS--ERLIAIRNVV 168
Cdd:cd03315 48 VDMALWDLWGKRLGVPVYLLLG-GYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRDPARdvAVVAALREAV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 169 P-EATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIH--PLPVCADESCHTRDSLPQL--RGRYEM 243
Cdd:cd03315 127 GdDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARatDTPIMADESAFTPHDAFRElaLGAADA 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 695765033 244 VNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLAPLARFADL 298
Cdd:cd03315 207 VNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTL 261
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
1-112 |
9.52e-27 |
|
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: 101.78 E-value: 9.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 1 MRNLRVYEEAWPLHtPFVIARGSRSEAKVVVVEIE-EDGVKGVGECTPYP-----RYGESIASVMAQILTIGEQLESGIT 74
Cdd:pfam02746 1 AIEVFVVDVGWPLR-PIQMAFGTVQQQSLVIVRIEtSEGVVGIGEATSYGgraetIKAILDDHLAPLLIGRDAANISDLW 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 695765033 75 REQLQHLLPAGAARNAVDCALWDLQARRVGKTIPQLLG 112
Cdd:pfam02746 80 QLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
12-296 |
6.65e-26 |
|
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: 105.39 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 12 PLHTPFVIARGSRSEAKVVVVEIE-EDGVKGVGECT--PYPRYG-ESIAS---VMAQILtIGEQLESGITR-----EQLQ 79
Cdd:cd03317 9 PLKFPFETSFGTLNEREFLIVELTdEEGITGYGEVVafEGPFYTeETNATawhILKDYL-LPLLLGREFSHpeevsERLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 80 HLLPAGAARNAVDCALWDLQARRVGKTIPQLLGiGLPNRVVTAqtVVIG---TPEQMAASAAALWEKGARLLKVKLDNHL 156
Cdd:cd03317 88 PIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLG-GTRDSIPVG--VSIGiqdDVEQLLKQIERYLEEGYKRIKLKIKPGW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 157 ISERLIAIRNVVPEATLIVDANESWSgDGLAARCQLLADIGVAMLEQPLPadADDALEnfiHPL-------PVCADESCH 229
Cdd:cd03317 165 DVEPLKAVRERFPDIPLMADANSAYT-LADIPLLKRLDEYGLLMIEQPLA--ADDLID---HAElqkllktPICLDESIQ 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765033 230 TRDSLPQLR--GRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCT--SRAISAAlpLAPLARFA 296
Cdd:cd03317 239 SAEDARKAIelGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESgiGRAHNVA--LASLPNFT 307
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
9-321 |
4.75e-24 |
|
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: 100.38 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 9 EAWPLHTPFVIARGSRSEAKVVVVEIE-EDGVKGVGECTPYPRyGESIASVMAQILT---IGEQ-LESGITREQLQHLL- 82
Cdd:cd03316 6 ETFVLRVPLPEPGGAVTWRNLVLVRVTtDDGITGWGEAYPGGR-PSAVAAAIEDLLApllIGRDpLDIERLWEKLYRRLf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 83 ------PAGAARNAVDCALWDLQARRVGKTIPQLLGiGLPNRVVTAQTVVIG---TPEQMAASAAALWEKGARLLKVKLD 153
Cdd:cd03316 85 wrgrggVAMAAISAVDIALWDIKGKAAGVPVYKLLG-GKVRDRVRVYASGGGyddSPEELAEEAKRAVAEGFTAVKLKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 154 NHLIS--------ERLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIH--PLPV 222
Cdd:cd03316 164 GPDSGgedlredlARVRAVREAVgPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQatSVPI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 223 CADESCHTRDSLPQL--RGRYEMVNIKLDKTGGLTEALFLAQEAGELG-------FERMLGCMLCTSraISAALPLAPLA 293
Cdd:cd03316 244 AAGENLYTRWEFRDLleAGAVDIIQPDVTKVGGITEAKKIAALAEAHGvrvaphgAGGPIGLAASLH--LAAALPNFGIL 321
|
330 340
....*....|....*....|....*...
gi 695765033 294 RFADLDGPTWLAVDVEPaLHFSTGVLHL 321
Cdd:cd03316 322 EYHLDDLPLREDLFKNP-PEIEDGYVTV 348
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
4-298 |
8.10e-23 |
|
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: 94.32 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 4 LRVYEEAWPLHTPFVIARGSRSEAKVVVVEIE-EDGVKGVGECtpyprygesiasvmaqiltigeqlesgitreqlqhll 82
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTtDSGVVGWGEV------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 83 pagaaRNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVvigtpeqmaasaaalwekgarllkvkldnhlisERLI 162
Cdd:cd00308 44 -----ISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSI---------------------------------ERVR 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 163 AIRNVVPEATLI-VDANESWSGDGLAARCQLLADIGVAMLEQPLPAD--ADDALENFIHPLPVCADESCHTRDSLPQL-- 237
Cdd:cd00308 86 AVREAFGPDARLaVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDdlEGYAALRRRTGIPIAADESVTTVDDALEAle 165
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765033 238 RGRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLA---PLARFADL 298
Cdd:cd00308 166 LGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAaalPNDRAIET 229
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
12-321 |
1.02e-22 |
|
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: 97.00 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 12 PLHTPFVIARGSRSEAKVVVVEI-EEDGVKGVGECTPY--PRYG-ESIASVMAQI------LTIGEQ-LESGITREQLQH 80
Cdd:cd03318 13 PTRRPHQFAGTTMHTQSLVLVRLtTSDGVVGIGEATTPggPAWGgESPETIKAIIdrylapLLIGRDaTNIGAAMALLDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 81 LLPAGA-ARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKG-ARLLKVKL---DNH 155
Cdd:cd03318 93 AVAGNLfAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGrHRRFKLKMgarPPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 156 LISERLIAIRNVVP-EATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALE--NFIHPLPVCADESCHTRD 232
Cdd:cd03318 173 DDLAHVEAIAKALGdRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLArlRSRNRVPIMADESVSGPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 233 SLPQL--RGRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLAplARFADLD------GPTWL 304
Cdd:cd03318 253 DAFELarRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLF--ATLPSLPfgcelfGPLLL 330
|
330
....*....|....*...
gi 695765033 305 AVDV-EPALHFSTGVLHL 321
Cdd:cd03318 331 AEDLlEEPLAYRDGELHV 348
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
132-321 |
1.95e-17 |
|
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: 79.53 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 132 QMAASAAALW-EKGARLLKVKLDNHLIS---ERLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLP 206
Cdd:pfam13378 1 ELAAEARRAVeARGFRAFKLKVGGPDPEedvERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 207 ADADDALENF--IHPLPVCADESCHTRDSLPQL--RGRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLcTSRA 282
Cdd:pfam13378 81 PDDLEGLARLrrATPVPIATGESLYSREDFRRLleAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG-GPIG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695765033 283 ISAALPLA---PLARFAD--LDGPTWLAVDVEPALHFSTGVLHL 321
Cdd:pfam13378 160 LAASLHLAaavPNLLIQEyfLDPLLLEDDLLTEPLEVEDGRVAV 203
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
3-305 |
3.91e-17 |
|
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: 79.61 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 3 NLRVYEEawPLHTPFVIARGSRSEAKVVVVEIE-EDGVKGVGECTPYPrygesiasvmaqiltigeqlesgitreqlqhl 81
Cdd:cd03320 2 RLYPYSL--PLSRPLGTSRGRLTRRRGLLLRLEdLTGPVGWGEIAPLP-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 82 lpagaARNAVDCALWDLQARRVGKTIPQllgiglpNRVVTAQTVVIGTPEQMAAsAAALWEKGARLLKVKLDNHLISE-- 159
Cdd:cd03320 48 -----LAFGIESALANLEALLVGFTRPR-------NRIPVNALLPAGDAAALGE-AKAAYGGGYRTVKLKVGATSFEEdl 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 160 -RLIAIRNVVPE-ATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIHPLPVCADESCHTRDSLPQL 237
Cdd:cd03320 115 aRLRALREALPAdAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAAGVPIALDESLRRLDDPLAL 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 238 R--GRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLGCMLCTSRAISAALPLAplARFADLDGPTWLA 305
Cdd:cd03320 195 AaaGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLA--AALPPLPAACGLG 262
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
130-213 |
4.79e-15 |
|
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: 69.62 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 130 PEQMAASAA-ALWEKGARLLKVKLDNHLIS--ERLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPL 205
Cdd:smart00922 1 PEELAEAARrAVAEAGFRAVKVKVGGGPLEdlARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
....*...
gi 695765033 206 PADADDAL 213
Cdd:smart00922 81 PPDDLEGL 88
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-296 |
4.69e-10 |
|
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: 59.44 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 7 YEEAWPLHTPFVIARGSRSEAKVVVVEIEEDGVKGVGECTPYPRYG-ESIASVMAQILTIGEQLESGITrEQLQHLLPAG 85
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDEGRTGWGEIAPLPGFGtETLAEALDFCRALIEEITRGDI-EAIDDQLPSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 86 AArnAVDCALWDLQArrvGKTIPqllgiglPNRVVTAQTVVIGTPEqmAASAAALWEKGARLLKVKLD-NHLISERLI-- 162
Cdd:TIGR01927 80 AF--GFESALIELES---GDELP-------PASNYYVALLPAGDPA--LLLLRSAKAEGFRTFKWKVGvGELAREGMLvn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 163 AIRNVVPE-ATLIVDANESWSGDGLAARCQLLA-DIG--VAMLEQPLPaDADDALENFI-HPLPVCADESCHTRDSLPQL 237
Cdd:TIGR01927 146 LLLEALPDkAELRLDANGGLSPDEAQQFLKALDpNLRgrIAFLEEPLP-DADEMSAFSEaTGTAIALDESLWELPQLADE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765033 238 --RGRYEMVNIKLDKTGGLTEALFLAQEAGELGFERMLgcmlctSRAISAALPLAPLARFA 296
Cdd:TIGR01927 225 ygPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVF------SSVFESSIALGQLARLA 279
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
24-258 |
5.47e-07 |
|
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: 50.41 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 24 RSEAKVVVVEIE-EDGVKGVGECTPYPRYGESIASVMAQILTIGEQLESGITREQLQHL-LPAG------AARNAVDCAL 95
Cdd:cd03327 6 RTRVGWLFVEIEtDDGTVGYANTTGGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRAtLAYGrkgiamAAISAVDLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 96 WDLQARRVGKTIPQLLGIGLPNRVVT-AQTVVIGTPEQMAASAAALWEKGARLLKVKL-----DNHL----ISERLIAIR 165
Cdd:cd03327 86 WDLLGKIRGEPVYKLLGGRTRDKIPAyASGLYPTDLDELPDEAKEYLKEGYRGMKMRFgygpsDGHAglrkNVELVRAIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 166 NVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDALENFIHP--LPVCADESCHTRDSLPQLrgrYE 242
Cdd:cd03327 166 EAVgYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKAtgIPISTGEHEYTVYGFKRL---LE 242
|
250 260
....*....|....*....|.
gi 695765033 243 MVNIKL-----DKTGGLTEAL 258
Cdd:cd03327 243 GRAVDIlqpdvNWVGGITELK 263
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
25-208 |
5.20e-06 |
|
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: 47.41 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 25 SEAKVVVVEIEEDGVKGVGECTPYPRYGESIASVMAQILTIGEQLESGITREQLQHLLP-------AGAARNAVDCALWD 97
Cdd:cd03328 26 DATTLVLVEVRAGGRTGLGYTYADAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRAVRnagrpgvAAMAISAVDIALWD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 98 LQARRVGKTIPQLLGiglpnrVVTAQTVVIG-------TPEQMAASAAALWEKGARLLKVKLDNHLIS--ERLIAIRNVV 168
Cdd:cd03328 106 LKARLLGLPLARLLG------RAHDSVPVYGsggftsyDDDRLREQLSGWVAQGIPRVKMKIGRDPRRdpDRVAAARRAI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695765033 169 -PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPAD 208
Cdd:cd03328 180 gPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSD 220
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
12-208 |
6.24e-06 |
|
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: 47.09 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 12 PLHTPFVIARGSRSEAKVVVVEIEED-GVKGVGECTPY-PRYGESIASVMAQI--LTIGEQLESGITREQLQH---LLPA 84
Cdd:cd03321 14 PMQYPVHTSVGTVATAPLVLIDLATDeGVTGHSYLFTYtPAALKSLKQLLDDMaaLLVGEPLAPAELERALAKrfrLLGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 85 ----GAARNAVDCALWDLQARRVGKTIPQLLGiGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDNHLISER 160
Cdd:cd03321 94 tglvRMAAAGIDMAAWDALAKVHGLPLAKLLG-GNPRPVQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKIGYPTADED 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695765033 161 LIAIRNVV----PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPAD 208
Cdd:cd03321 173 LAVVRSIRqavgDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQH 224
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
5-227 |
6.96e-06 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 46.93 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 5 RVYEEawPLHTPFVIARGSRSEAKVVVVEIE-EDGVKGVGECTPYPRYGesiASVMAQILTIGEQLESGITREQLQHL-- 81
Cdd:PRK02714 8 RPYQR--PFRQPLQTAHGLWRIREGIILRLTdETGKIGWGEIAPLPWFG---SETLEEALAFCQQLPGEITPEQIFSIpd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 82 -LPAgaARNAVDCALWDLQARR-----VGKTIPQLLGIGLpnrvvtaqtvvigTPEQMAASaaaLWEKGARLLKVK--LD 153
Cdd:PRK02714 83 aLPA--CQFGFESALENESGSRsnvtlNPLSYSALLPAGE-------------AALQQWQT---LWQQGYRTFKWKigVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 154 NhLISERLI---AIRNVVPEATLIVDANESWSgdgLAARCQLLA-----DIG-VAMLEQPLPADADDAL----ENFihPL 220
Cdd:PRK02714 145 P-LEQELKIfeqLLERLPAGAKLRLDANGGLS---LEEAKRWLQlcdrrLSGkIEFIEQPLPPDQFDEMlqlsQDY--QT 218
|
....*..
gi 695765033 221 PVCADES 227
Cdd:PRK02714 219 PIALDES 225
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
11-150 |
1.94e-05 |
|
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: 45.85 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 11 WPLHTPfviarGSRSEAKVVVVEIE-EDGVKGVGECTPYPRYGESIASVMAQILtIGEqleSGITREQLQHLLpAGAAR- 88
Cdd:cd03329 21 GGHHHP-----GPAGTRKLALLTIEtDEGAKGHAFGGRPVTDPALVDRFLKKVL-IGQ---DPLDRERLWQDL-WRLQRg 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765033 89 ------NAVDCALWDLQARRVGKTIPQLLGiGLPNRVVT-AQTVV------IGTPEQMAASAAALWEKGARLLKV 150
Cdd:cd03329 91 ltdrglGLVDIALWDLAGKYLGLPVHRLLG-GYREKIPAyASTMVgddlegLESPEAYADFAEECKALGYRAIKL 164
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
1-312 |
5.31e-04 |
|
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: 41.02 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 1 MRNLRVYEEAWPLHTPfVIARGSR-SEAKVVVVEIEEDGVKGVGECTPYPRY-GESIAsvMAQiltigEQLESGITREQL 78
Cdd:COG1441 1 MRHATLYRYSIPMDAG-VILRNQRlKTRDGLLVRLQEGGREGWGEIAPLPGFsQETLE--QAE-----QQALAWLQRWLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 79 QHLLPAGAA----RNAVDCALWDLQArrvgktipqllgiGLPnrvvTAQTVVI-----GTPEQ-MAASAAALWEKGARLl 148
Cdd:COG1441 73 GDLLDEKSLlpsvAFGLSCALAELEG-------------ELP----EAANYRAaplcsGDPDElIARLNQMPGEKVAKV- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 149 KVKLDNhliSERLIAIRNV----VPEATLIVDANESWS---GDGLAARCQLLADIGVAMLEQPLpADADDALENFIHP-L 220
Cdd:COG1441 135 KVGLYE---AVRDGMVVNLlleaIPDLRLRLDANRSWTldkAVQFAKYVNPEHRSRIAFLEEPC-KTPEESREFARETgI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 221 PVCADESchTRDslPQLRGRYE----MVNIKLDKTGGLTEALFLAQEAGELGFERMLgcmlctSRAISAALPLAPLARFA 296
Cdd:COG1441 211 AIAWDES--VRE--PDFRVEAEpgvaAIVIKPTLVGSLQRCRQLIEQAHQLGLQAVI------SSSIESSLGLTQLARLA 280
|
330
....*....|....*.
gi 695765033 297 dldgpTWLAVDVEPAL 312
Cdd:COG1441 281 -----AWLTPDTAPGL 291
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
27-258 |
9.76e-04 |
|
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: 40.40 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 27 AKVVVVEIEEDGVKGVGECTPYPRYGESIASVMAQI--LTIGEQLESgITRE------------QLQHLLP-AGA---AR 88
Cdd:cd03324 33 AAYVVLRTDAAGLKGHGLTFTIGRGNEIVCAAIEALahLVVGRDLES-IVADmgkfwrrltsdsQLRWIGPeKGVihlAT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 89 NAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQ-----TVVIgTPEQM-----------AASAAAL------------ 140
Cdd:cd03324 112 AAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIdfryiTDAL-TPEEAleilrrgqpgkAAREADLlaegypayttsa 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 141 -W-----EKGARL-----------LKVKLDNHLISE--RLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAM 200
Cdd:cd03324 191 gWlgysdEKLRRLckealaqgfthFKLKVGADLEDDirRCRLAREVIgPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWW 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695765033 201 LEQPLPAD-----ADDALENFIHPLPVCADESCHTRDSLPQL--RGRYEMVNIKLDKTGGLTEAL 258
Cdd:cd03324 271 IEEPTSPDdilghAAIRKALAPLPIGVATGEHCQNRVVFKQLlqAGAIDVVQIDSCRLGGVNENL 335
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
124-290 |
2.64e-03 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 39.18 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 124 TVVIGTPEQMAASAAALweKGARLLKVKLDNHLIS-----ERLIAIRNVV-PEATLIVDANESWSGD-GLAARCQLLADI 196
Cdd:PRK02901 84 TVPAVDAAQVPEVLARF--PGCRTAKVKVAEPGQTladdvARVNAVRDALgPDGRVRVDANGGWSVDeAVAAARALDADG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 197 GVAMLEQPLPADADDALENFIHPLPVCADESchTRDSLPQLR----GRYEMVNIKLDKTGGLTEALFLAQEAGelgferm 272
Cdd:PRK02901 162 PLEYVEQPCATVEELAELRRRVGVPIAADES--IRRAEDPLRvaraGAADVAVLKVAPLGGVRAALDIAEQIG------- 232
|
170 180
....*....|....*....|..
gi 695765033 273 LGCM----LCTSRAISAALPLA 290
Cdd:PRK02901 233 LPVVvssaLDTSVGIAAGLALA 254
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
85-213 |
4.31e-03 |
|
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: 38.46 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765033 85 GAARNAVDCALWDLQARRVGKTIPQLLGIGLPNRVVTAQTVVIGTPEQMAASAAALWEKGARLLKVKLDNHL-------- 156
Cdd:cd03325 79 MSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNATEELqwidtskk 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765033 157 ---ISERLIAIRNVV-PEATLIVDANESWSGDGLAARCQLLADIGVAMLEQPLPADADDAL 213
Cdd:cd03325 159 vdaAVERVAALREAVgPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEAL 219
|
|
| |
