|
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: 647.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 1 MRTVKVFEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREELQK 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 81 ILPAGAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNHLISER 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 161 MVAIRTAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKALKGR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 241 YEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQVSFADLDGPTWLAVDVEPALQFTTGELH 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 90111249 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 |
4.80e-127 |
|
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: 365.36 E-value: 4.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 3 TVKVFEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPR-YGESDASVMAQIMSVVPQLEKG-----LTRE 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGdprleKLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 77 ELQKILPA-GAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNH 155
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 156 LIS--ERMVAIRTAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFI--HPLPICADESCHTR 231
Cdd:cd03319 161 LEDdiERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRdkSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111249 232 SNLKALKG--RYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQ-VSFADLDGPTWL 304
Cdd:cd03319 241 ADAARLAGggAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAAkADFVDLDGPLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-321 |
2.26e-75 |
|
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: 235.49 E-value: 2.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 1 MRTVKVFEEAWPLHTPFVIARGSRSEARVVV-VELEEEGIKGTGECTPYPRYGESDASVMAQIMSvvPQLEkGLT----- 74
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLvRVETDDGITGWGEAVPGGTGAEAVAAALEEALA--PLLI-GRDpldie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 75 --REELQKILP-AGAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVK 151
Cdd:COG4948 80 alWQRLYRALPgNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 152 LDNHLIS---ERMVAIRTAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIH--PLPICAD 225
Cdd:COG4948 160 VGGPDPEedvERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatPVPIAAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 226 ESCHTRSNLKAL--KGRYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAAL---PLVPQVSFADLDG 300
Cdd:COG4948 240 ESLTSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALhlaAALPNFDIVELDG 319
|
330 340
....*....|....*....|..
gi 90111249 301 PTWLAVD-VEPALQFTTGELHL 321
Cdd:COG4948 320 PLLLADDlVEDPLRIEDGYLTV 341
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
1-112 |
6.82e-31 |
|
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: 112.56 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 1 MRTVKVFEEAWPLHtPFVIARGSRSEARVVVVE-LEEEGIKGTGECTPYP-----RYGESDASVMAQIMSVVPQLEKGLT 74
Cdd:pfam02746 1 AIEVFVVDVGWPLR-PIQMAFGTVQQQSLVIVRiETSEGVVGIGEATSYGgraetIKAILDDHLAPLLIGRDAANISDLW 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 90111249 75 REELQKILPAGAARNALDCALWDLAARRQQQSLADLIG 112
Cdd:pfam02746 80 QLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
130-213 |
5.04e-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: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 130 PDQMANSA-STLWQAGAKLLKVKLDNHLIS--ERMVAIRTAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPL 205
Cdd:smart00922 1 PEELAEAArRAVAEAGFRAVKVKVGGGPLEdlARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
....*...
gi 90111249 206 PAQDDAAL 213
Cdd:smart00922 81 PPDDLEGL 88
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
38-313 |
1.09e-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: 58.66 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 38 GIKGTGECTPYPRYG-ESDASVMAQIMSVVPQLEKGLTrEELQKILPAGAArnALDCALWDLAArrqqqsladliGITLP 116
Cdd:TIGR01927 32 GRTGWGEIAPLPGFGtETLAEALDFCRALIEEITRGDI-EAIDDQLPSVAF--GFESALIELES-----------GDELP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 117 ET-VITAQTVVIGTPDQMANSAstLWQAGAKLLKVKLD-NHLISERMV--AIRTAVPD-ATLIVDANESWR-AEGLAARC 190
Cdd:TIGR01927 98 PAsNYYVALLPAGDPALLLLRS--AKAEGFRTFKWKVGvGELAREGMLvnLLLEALPDkAELRLDANGGLSpDEAQQFLK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 191 QLLADLG--VAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKAL--KGRYEMVNIKLDKTGGLTEALALATEARA 266
Cdd:TIGR01927 176 ALDPNLRgrIAFLEEPLPDADEMSAFSEATGTAIALDESLWELPQLADEygPGWRGALVIKPAIIGSPAKLRDLAQKAHR 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 90111249 267 QGFSLMLGCMLCTSRAISAALPLVPQVSFAD---LDGPTWL-AVDVEPALQ 313
Cdd:TIGR01927 256 LGLQAVFSSVFESSIALGQLARLAAKLSPDPaavGFTTALLrAQDLEAWPF 306
|
|
| |
|
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: 647.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 1 MRTVKVFEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREELQK 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 81 ILPAGAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNHLISER 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 161 MVAIRTAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKALKGR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 241 YEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQVSFADLDGPTWLAVDVEPALQFTTGELH 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 90111249 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 |
4.80e-127 |
|
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: 365.36 E-value: 4.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 3 TVKVFEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPR-YGESDASVMAQIMSVVPQLEKG-----LTRE 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGdprleKLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 77 ELQKILPA-GAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNH 155
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 156 LIS--ERMVAIRTAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFI--HPLPICADESCHTR 231
Cdd:cd03319 161 LEDdiERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRdkSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111249 232 SNLKALKG--RYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQ-VSFADLDGPTWL 304
Cdd:cd03319 241 ADAARLAGggAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAAkADFVDLDGPLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-321 |
2.26e-75 |
|
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: 235.49 E-value: 2.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 1 MRTVKVFEEAWPLHTPFVIARGSRSEARVVV-VELEEEGIKGTGECTPYPRYGESDASVMAQIMSvvPQLEkGLT----- 74
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLvRVETDDGITGWGEAVPGGTGAEAVAAALEEALA--PLLI-GRDpldie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 75 --REELQKILP-AGAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVK 151
Cdd:COG4948 80 alWQRLYRALPgNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 152 LDNHLIS---ERMVAIRTAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIH--PLPICAD 225
Cdd:COG4948 160 VGGPDPEedvERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatPVPIAAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 226 ESCHTRSNLKAL--KGRYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAAL---PLVPQVSFADLDG 300
Cdd:COG4948 240 ESLTSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALhlaAALPNFDIVELDG 319
|
330 340
....*....|....*....|..
gi 90111249 301 PTWLAVD-VEPALQFTTGELHL 321
Cdd:COG4948 320 PLLLADDlVEDPLRIEDGYLTV 341
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
1-112 |
6.82e-31 |
|
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: 112.56 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 1 MRTVKVFEEAWPLHtPFVIARGSRSEARVVVVE-LEEEGIKGTGECTPYP-----RYGESDASVMAQIMSVVPQLEKGLT 74
Cdd:pfam02746 1 AIEVFVVDVGWPLR-PIQMAFGTVQQQSLVIVRiETSEGVVGIGEATSYGgraetIKAILDDHLAPLLIGRDAANISDLW 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 90111249 75 REELQKILPAGAARNALDCALWDLAARRQQQSLADLIG 112
Cdd:pfam02746 80 QLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
12-296 |
1.28e-29 |
|
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: 115.79 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 12 PLHTPFVIARGSRSEARVV-VVELEEEGIKGTGECT--PYPRYGESDASVMAQIMS--VVPQLeKGLT-------REELQ 79
Cdd:cd03317 9 PLKFPFETSFGTLNEREFLiVELTDEEGITGYGEVVafEGPFYTEETNATAWHILKdyLLPLL-LGREfshpeevSERLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 80 KILPAGAARNALDCALWDLAARRQQQSLADLIGITlPETVITAqtVVIG---TPDQMANSASTLWQAGAKLLKVKLDNHL 156
Cdd:cd03317 88 PIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGT-RDSIPVG--VSIGiqdDVEQLLKQIERYLEEGYKRIKLKIKPGW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 157 ISERMVAIRTAVPDATLIVDANESWRAEGlAARCQLLADLGVAMLEQPLPAQD---DAALENFIHPlPICADESCHT-RS 232
Cdd:cd03317 165 DVEPLKAVRERFPDIPLMADANSAYTLAD-IPLLKRLDEYGLLMIEQPLAADDlidHAELQKLLKT-PICLDESIQSaED 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111249 233 NLKALK-GRYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCT--SRAISAALPLVPQVSFA 296
Cdd:cd03317 243 ARKAIElGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESgiGRAHNVALASLPNFTYP 309
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
84-286 |
1.46e-29 |
|
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: 113.59 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 84 AGAARNALDCALWDLAARRQQQSLADLIGITLpETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNHLISERMV- 162
Cdd:cd03315 41 AEATKAAVDMALWDLWGKRLGVPVYLLLGGYR-DRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRDPARDVAVv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 163 -AIRTAVP-DATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIH--PLPICADESCHTRSNLK--A 236
Cdd:cd03315 120 aALREAVGdDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARatDTPIMADESAFTPHDAFreL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90111249 237 LKGRYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAA 286
Cdd:cd03315 200 ALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLAN 249
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
38-321 |
4.15e-23 |
|
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: 97.77 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 38 GIKGTGECTPY--PRYGESDASVMAQIMSVV--------PQLEKGLTREELQKILPAGA-ARNALDCALWDLAARRQQQS 106
Cdd:cd03318 40 GVVGIGEATTPggPAWGGESPETIKAIIDRYlaplligrDATNIGAAMALLDRAVAGNLfAKAAIEMALLDAQGRRLGLP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 107 LADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAG-AKLLKVKL---DNHLISERMVAIRTAVPD-ATLIVDANESW 181
Cdd:cd03318 120 VSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGrHRRFKLKMgarPPADDLAHVEAIAKALGDrASVRVDVNQAW 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 182 RAEGLAARCQLLADLGVAMLEQPLPAQDDAALE--NFIHPLPICADESCHTRSNLKAL--KGRYEMVNIKLDKTGGLTEA 257
Cdd:cd03318 200 DESTAIRALPRLEAAGVELIEQPVPRENLDGLArlRSRNRVPIMADESVSGPADAFELarRGAADVFSLKIAKSGGLRRA 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 258 LALATEARAQGFSLMLGCMLCTSRAISAALPL---VPQVSFA-DLDGPTWLAVDV--EPaLQFTTGELHL 321
Cdd:cd03318 280 QKVAAIAEAAGIALYGGTMLESSIGTAASAHLfatLPSLPFGcELFGPLLLAEDLleEP-LAYRDGELHV 348
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
132-321 |
6.42e-21 |
|
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: 89.16 E-value: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 132 QMANSASTLW-QAGAKLLKVKLDNHLIS---ERMVAIRTAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLP 206
Cdd:pfam13378 1 ELAAEARRAVeARGFRAFKLKVGGPDPEedvERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 207 AQDDAALENF--IHPLPICADESCHTRSNLKAL--KGRYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLcTSRA 282
Cdd:pfam13378 81 PDDLEGLARLrrATPVPIATGESLYSREDFRRLleAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG-GPIG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 90111249 283 ISAALPL---VPQVSFAD--LDGPTWLAVDVEPALQFTTGELHL 321
Cdd:pfam13378 160 LAASLHLaaaVPNLLIQEyfLDPLLLEDDLLTEPLEVEDGRVAV 203
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
85-287 |
9.94e-21 |
|
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: 88.92 E-value: 9.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 85 GAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVvigtpdqmansastlwqagakllkvkldnhlisERMVAI 164
Cdd:cd00308 41 GEVISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSI---------------------------------ERVRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 165 RTAVPDATLI-VDANESWRAEGLAARCQLLADLGVAMLEQPLPAQD--DAALENFIHPLPICADESCHT---RSNLKALK 238
Cdd:cd00308 88 REAFGPDARLaVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDleGYAALRRRTGIPIAADESVTTvddALEALELG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90111249 239 GRyEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAAL 287
Cdd:cd00308 168 AV-DILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAAL 215
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
38-321 |
6.71e-19 |
|
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: 86.13 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 38 GIKGTGECTPYPRyGESDASVMAQImsVVPQL--------EKglTREELQKIL-------PAGAARNALDCALWDLAARR 102
Cdd:cd03316 36 GITGWGEAYPGGR-PSAVAAAIEDL--LAPLLigrdpldiER--LWEKLYRRLfwrgrggVAMAAISAVDIALWDIKGKA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 103 QQQSLADLIGITLPETV---ITAQTVVIgTPDQMANSASTLWQAGAKLLKVKLDNHLIS--------ERMVAIRTAV-PD 170
Cdd:cd03316 111 AGVPVYKLLGGKVRDRVrvyASGGGYDD-SPEELAEEAKRAVAEGFTAVKLKVGGPDSGgedlredlARVRAVREAVgPD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 171 ATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIH--PLPICADESCHTRSNLKAL--KGRYEMVNI 246
Cdd:cd03316 190 VDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQatSVPIAAGENLYTRWEFRDLleAGAVDIIQP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 247 KLDKTGGLTEALALATEARAQGFSLM-------LGCMLCTSraISAALPLVPQVSFADLDGPTWLAVDVEPaLQFTTGEL 319
Cdd:cd03316 270 DVTKVGGITEAKKIAALAEAHGVRVAphgaggpIGLAASLH--LAAALPNFGILEYHLDDLPLREDLFKNP-PEIEDGYV 346
|
..
gi 90111249 320 HL 321
Cdd:cd03316 347 TV 348
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
130-213 |
5.04e-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: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 130 PDQMANSA-STLWQAGAKLLKVKLDNHLIS--ERMVAIRTAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPL 205
Cdd:smart00922 1 PEELAEAArRAVAEAGFRAVKVKVGGGPLEdlARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
....*...
gi 90111249 206 PAQDDAAL 213
Cdd:smart00922 81 PPDDLEGL 88
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
87-287 |
5.87e-12 |
|
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: 64.59 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 87 ARNALDCALWDLAARRQQQSladligiTLPETVITAQTVVIGTPDQMANSASTlWQAGAKLLKVKLDNHLISE---RMVA 163
Cdd:cd03320 48 LAFGIESALANLEALLVGFT-------RPRNRIPVNALLPAGDAAALGEAKAA-YGGGYRTVKLKVGATSFEEdlaRLRA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 164 IRTAVP-DATLIVDANESW-RAEGLAArCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKALK--G 239
Cdd:cd03320 120 LREALPaDAKLRLDANGGWsLEEALAF-LEALAAGRIEYIEQPLPPDDLAELRRLAAGVPIALDESLRRLDDPLALAaaG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 90111249 240 RYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAAL 287
Cdd:cd03320 199 ALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALA 246
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
38-313 |
1.09e-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: 58.66 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 38 GIKGTGECTPYPRYG-ESDASVMAQIMSVVPQLEKGLTrEELQKILPAGAArnALDCALWDLAArrqqqsladliGITLP 116
Cdd:TIGR01927 32 GRTGWGEIAPLPGFGtETLAEALDFCRALIEEITRGDI-EAIDDQLPSVAF--GFESALIELES-----------GDELP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 117 ET-VITAQTVVIGTPDQMANSAstLWQAGAKLLKVKLD-NHLISERMV--AIRTAVPD-ATLIVDANESWR-AEGLAARC 190
Cdd:TIGR01927 98 PAsNYYVALLPAGDPALLLLRS--AKAEGFRTFKWKVGvGELAREGMLvnLLLEALPDkAELRLDANGGLSpDEAQQFLK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 191 QLLADLG--VAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKAL--KGRYEMVNIKLDKTGGLTEALALATEARA 266
Cdd:TIGR01927 176 ALDPNLRgrIAFLEEPLPDADEMSAFSEATGTAIALDESLWELPQLADEygPGWRGALVIKPAIIGSPAKLRDLAQKAHR 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 90111249 267 QGFSLMLGCMLCTSRAISAALPLVPQVSFAD---LDGPTWL-AVDVEPALQ 313
Cdd:TIGR01927 256 LGLQAVFSSVFESSIALGQLARLAAKLSPDPaavGFTTALLrAQDLEAWPF 306
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
84-288 |
1.37e-08 |
|
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: 55.50 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 84 AGAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQA-GAKLLKVKLDNHLIS--ER 160
Cdd:cd03328 92 AAMAISAVDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTSYDDDRLREQLSGWVAqGIPRVKMKIGRDPRRdpDR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 161 MVAIRTAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAAL----ENFIHPLPICADESCHTRSNLK 235
Cdd:cd03328 172 VAAARRAIgPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLrlvrERGPAGMDIAAGEYAYTLAYFR 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90111249 236 ALKGRYEMVNIKLDKT--GGLTEALALATEARAQGFSLMLGCMLCTSRAISAALP 288
Cdd:cd03328 252 RLLEAHAVDVLQADVTrcGGVTGFLQAAALAAAHHVDLSAHCAPALHAHVACAVP 306
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
78-320 |
7.32e-05 |
|
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: 44.01 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 78 LQKILPAGaarnaLDCALWDLAARRQQQSLADLIGiTLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNHLI 157
Cdd:cd03321 96 LVRMAAAG-----IDMAAWDALAKVHGLPLAKLLG-GNPRPVQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKIGYPTA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 158 SERMVAIRT---AVPDA-TLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQD---DAALENFIHPLPICADESCHT 230
Cdd:cd03321 170 DEDLAVVRSirqAVGDGvGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDyegHARIASALRTPVQMGENWLGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 231 RSNLKALKGRY-EMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQVSFADLDGPTwlavdVE 309
Cdd:cd03321 250 EEMFKALSAGAcDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEISAHLLAVTPTAHWLEYVDWAGAI-----LE 324
|
250
....*....|.
gi 90111249 310 PALQFTTGELH 320
Cdd:cd03321 325 PPLKFEDGNAV 335
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
144-296 |
5.89e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 41.11 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 144 GAKLLKVKLDNHLIS-----ERMVAIRTAV-PDATLIVDANESWR-AEGLAARCQLLADLGVAMLEQPLPAQDD-AALEN 215
Cdd:PRK02901 102 GCRTAKVKVAEPGQTladdvARVNAVRDALgPDGRVRVDANGGWSvDEAVAAARALDADGPLEYVEQPCATVEElAELRR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 216 FIHpLPICADESchTRSNLKALK----GRYEMVNIKLDKTGGLTEALALATEAraqGFSLMLGCMLCTSRAISAALPLV- 290
Cdd:PRK02901 182 RVG-VPIAADES--IRRAEDPLRvaraGAADVAVLKVAPLGGVRAALDIAEQI---GLPVVVSSALDTSVGIAAGLALAa 255
|
....*...
gi 90111249 291 --PQVSFA 296
Cdd:PRK02901 256 alPELDHA 263
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
41-237 |
8.40e-04 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 40.38 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 41 GTGECTPYPRYGESDasvMAQIMSVVPQLEKGLTREELQKI---LPAgaARNALDCALWDLAarrQQQSLADLIGITLPE 117
Cdd:PRK02714 43 GWGEIAPLPWFGSET---LEEALAFCQQLPGEITPEQIFSIpdaLPA--CQFGFESALENES---GSRSNVTLNPLSYSA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 118 TVITAQTVVigtpdqmaNSASTLWQAGAKLLKVK--LDNhLISERMV---AIRTAVPDATLIVDANESWRAEGlAAR--- 189
Cdd:PRK02714 115 LLPAGEAAL--------QQWQTLWQQGYRTFKWKigVDP-LEQELKIfeqLLERLPAGAKLRLDANGGLSLEE-AKRwlq 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90111249 190 -CQLLADLGVAMLEQPLP-AQDDAALE-NFIHPLPICADESChtrSNLKAL 237
Cdd:PRK02714 185 lCDRRLSGKIEFIEQPLPpDQFDEMLQlSQDYQTPIALDESV---ANLAQL 232
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
86-268 |
1.54e-03 |
|
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: 39.62 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 86 AARNALDCALWDLAARRQQQSLADLI-GITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKL-----DNHLISE 159
Cdd:cd03327 76 AAISAVDLALWDLLGKIRGEPVYKLLgGRTRDKIPAYASGLYPTDLDELPDEAKEYLKEGYRGMKMRFgygpsDGHAGLR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 160 RMV----AIRTAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDdaaLENFIH-----PLPICADESCH 229
Cdd:cd03327 156 KNVelvrAIREAVgYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDD---IEGYAElkkatGIPISTGEHEY 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 90111249 230 TRSNLKALkgrYEMVNIKL-----DKTGGLTEALALATEARAQG 268
Cdd:cd03327 233 TVYGFKRL---LEGRAVDIlqpdvNWVGGITELKKIAALAEAYG 273
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
77-268 |
2.61e-03 |
|
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: 39.30 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 77 ELQKILPAgAARNALDCALWDLAARRQQQSLADLIG------ITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLK- 149
Cdd:cd03329 86 RLQRGLTD-RGLGLVDIALWDLAGKYLGLPVHRLLGgyrekiPAYASTMVGDDLEGLESPEAYADFAEECKALGYRAIKl 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 150 -------VKLDNHLISermvAIRTAV-PDATLIVDANESW-RAEGLAARcQLLADLGVAMLEQPLPAQDDAALENFIHPL 220
Cdd:cd03329 165 hpwgpgvVRRDLKACL----AVREAVgPDMRLMHDGAHWYsRADALRLG-RALEELGFFWYEDPLREASISSYRWLAEKL 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90111249 221 --PICADESC----HTRSNLkALKGRYEMVNIKLDKTGGLTEALALATEARAQG 268
Cdd:cd03329 240 diPILGTEHSrgalESRADW-VLAGATDFLRADVNLVGGITGAMKTAHLAEAFG 292
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
70-259 |
6.65e-03 |
|
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: 38.09 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 70 EKGLTReelqkiLPAGAARNALdcalWDLAARRQQQSLADLIGITLPET------------VITAQTVVI----GTPDQM 133
Cdd:cd03324 103 EKGVIH------LATAAVVNAV----WDLWAKAEGKPLWKLLVDMTPEElvscidfryitdALTPEEALEilrrGQPGKA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 134 ANSASTL------------W----------------QAGAKLLKVKLDNHLISE--RMVAIRTAV-PDATLIVDANESWR 182
Cdd:cd03324 173 AREADLLaegypayttsagWlgysdeklrrlckealAQGFTHFKLKVGADLEDDirRCRLAREVIgPDNKLMIDANQRWD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111249 183 AEGLAARCQLLADLGVAMLEQPlPAQDD----AALENFIHPLPI--CADESCHTRSNLKAL--KGRYEMVNIKLDKTGGL 254
Cdd:cd03324 253 VPEAIEWVKQLAEFKPWWIEEP-TSPDDilghAAIRKALAPLPIgvATGEHCQNRVVFKQLlqAGAIDVVQIDSCRLGGV 331
|
....*
gi 90111249 255 TEALA 259
Cdd:cd03324 332 NENLA 336
|
|
| |
