|
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: 640.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 1 MRTVKVYPESWPLHSAFIIARGARHEAGVVVVELEENGTKGIGECTPYARYGETEASVLAQIALLLPEIEQGLTRHALQQ 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 81 RLPAGAARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVCVDVPEMMASSALALWENGAKLIKIKLDDHMIAER 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 161 LVAIRSAVPQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFVHPLPICADESCHSVDSLAALRGR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 241 YEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLAPKARFVDLDGPTWLAIDAEPALAFDCGRIL 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 490273803 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 |
1.40e-113 |
|
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: 332.23 E-value: 1.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 3 TVKVYPESWPLHSAFIIARGARHEAGVVVVELEENGTKGIGECTPYAR-YGETEASVLAQIALLLPEIEQG-----LTRH 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGdprleKLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 77 ALQQRLPA-GAARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVCVDVPEMMASSALALWENGAKLIKIKLDDH 155
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 156 MIA--ERLVAIRSAVPQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFV--HPLPICADESCHSV 231
Cdd:cd03319 161 LEDdiERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRdkSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490273803 232 DSLAALRG--RYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLAP-KARFVDLDGPTWL 304
Cdd:cd03319 241 ADAARLAGggAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAaKADFVDLDGPLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-322 |
9.05e-68 |
|
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: 216.61 E-value: 9.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 1 MRTVKVYPESWPLHSAFIIARGARHEAGVVVVELE-ENGTKGIGECTPYARYGET-EASVLAQIALLL-----PEIEQgl 73
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVEtDDGITGWGEAVPGGTGAEAvAAALEEALAPLLigrdpLDIEA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 74 TRHALQQRLP-AGAARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVCVDVPEMMASSALALWENGAKLIKIKL 152
Cdd:COG4948 81 LWQRLYRALPgNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 153 DDHMIA---ERLVAIRSAV-PQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFVH--PLPICADE 226
Cdd:COG4948 161 GGPDPEedvERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatPVPIAADE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 227 SCHSVDSLAAL--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLA---PKARFVDLDGP 301
Cdd:COG4948 241 SLTSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAaalPNFDIVELDGP 320
|
330 340
....*....|....*....|..
gi 490273803 302 TWLAID-AEPALAFDCGRILLS 322
Cdd:COG4948 321 LLLADDlVEDPLRIEDGYLTVP 342
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-299 |
7.58e-27 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 108.00 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 7 YPESWPLHSAFIIARGARHEAGVVVVELEE-NGTKGIGEC----TPYARYgETEASVLAQIA-LLLPEIEQGLTRHALQQ 80
Cdd:TIGR01928 1 YHVSEPFKSPFKTSKGTLNHRDCLIIELIDdKGNAGFGEVvafqTPWYTH-ETIATVKHIIEdFFEPNINKEFEHPSEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 81 RLPAG-----AARNAIDSALWDLQVHSGSQNLWQLTGTT---APVQIETAQTVCVDVPEMMASsalaLWENGAKLIKIKL 152
Cdd:TIGR01928 80 ELVRSlkgtpMAKAGLEMALWDMYHKLPSFSLAYGQGKLrdkAPAGAVSGLANDEQMLKQIES----LKATGYKRIKLKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 153 DDHMIAERLVAIRSAVPQAMLIVDANESWHSEGLAaRCQLLADLNISMLEQPLPAADDVALENFVHPL--PICADESCHS 230
Cdd:TIGR01928 156 TPQIMHQLVKLRRLRFPQIPLVIDANESYDLQDFP-RLKELDRYQLLYIEEPFKIDDISMLDELAKGTitPICLDESITS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 231 VDSLAAL--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCT--SRAIRAALP----------LAPKARFV 296
Cdd:TIGR01928 235 LDDARNLieLGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETgiSRAFNVALAslggndypgdVSPSGYYF 314
|
...
gi 490273803 297 DLD 299
Cdd:TIGR01928 315 DQD 317
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
1-112 |
7.59e-20 |
|
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: 83.67 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 1 MRTVKVYPESWPLHSaFIIARGARHEAGVVVVELE-ENGTKGIGECTPY-----ARYGETEASVLAQIALLLPEIEQGLT 74
Cdd:pfam02746 1 AIEVFVVDVGWPLRP-IQMAFGTVQQQSLVIVRIEtSEGVVGIGEATSYggraeTIKAILDDHLAPLLIGRDAANISDLW 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 490273803 75 RHALQQRLPAGAARNAIDSALWDLQVHSGSQNLWQLTG 112
Cdd:pfam02746 80 QLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
130-222 |
1.08e-13 |
|
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: 66.15 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 130 PEMMASSAL-ALWENGAKLIKIKL--DDHMIAERLVAIRSAV-PQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPL 205
Cdd:smart00922 1 PEELAEAARrAVAEAGFRAVKVKVggGPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
90
....*....|....*..
gi 490273803 206 PAADDVALENFVHPLPI 222
Cdd:smart00922 81 PPDDLEGLAELRRATPI 97
|
|
| |
|
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: 640.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 1 MRTVKVYPESWPLHSAFIIARGARHEAGVVVVELEENGTKGIGECTPYARYGETEASVLAQIALLLPEIEQGLTRHALQQ 80
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREALQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 81 RLPAGAARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVCVDVPEMMASSALALWENGAKLIKIKLDDHMIAER 160
Cdd:PRK15129 81 LLPAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 161 LVAIRSAVPQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFVHPLPICADESCHSVDSLAALRGR 240
Cdd:PRK15129 161 MVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSSLKALKGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 241 YEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLAPKARFVDLDGPTWLAIDAEPALAFDCGRIL 320
Cdd:PRK15129 241 YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQVRFADLDGPTWLAVDVEPALQFTTGELH 320
|
.
gi 490273803 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 |
1.40e-113 |
|
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: 332.23 E-value: 1.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 3 TVKVYPESWPLHSAFIIARGARHEAGVVVVELEENGTKGIGECTPYAR-YGETEASVLAQIALLLPEIEQG-----LTRH 76
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRvTGETVESVLAALKSVRPALIGGdprleKLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 77 ALQQRLPA-GAARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVCVDVPEMMASSALALWENGAKLIKIKLDDH 155
Cdd:cd03319 81 ALQELLPGnGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 156 MIA--ERLVAIRSAVPQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFV--HPLPICADESCHSV 231
Cdd:cd03319 161 LEDdiERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRdkSPLPIMADESCFSA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490273803 232 DSLAALRG--RYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLAP-KARFVDLDGPTWL 304
Cdd:cd03319 241 ADAARLAGggAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAaKADFVDLDGPLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-322 |
9.05e-68 |
|
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: 216.61 E-value: 9.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 1 MRTVKVYPESWPLHSAFIIARGARHEAGVVVVELE-ENGTKGIGECTPYARYGET-EASVLAQIALLL-----PEIEQgl 73
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVEtDDGITGWGEAVPGGTGAEAvAAALEEALAPLLigrdpLDIEA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 74 TRHALQQRLP-AGAARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVCVDVPEMMASSALALWENGAKLIKIKL 152
Cdd:COG4948 81 LWQRLYRALPgNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 153 DDHMIA---ERLVAIRSAV-PQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFVH--PLPICADE 226
Cdd:COG4948 161 GGPDPEedvERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatPVPIAADE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 227 SCHSVDSLAAL--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLA---PKARFVDLDGP 301
Cdd:COG4948 241 SLTSRADFRRLieAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAaalPNFDIVELDGP 320
|
330 340
....*....|....*....|..
gi 490273803 302 TWLAID-AEPALAFDCGRILLS 322
Cdd:COG4948 321 LLLADDlVEDPLRIEDGYLTVP 342
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
84-298 |
4.09e-28 |
|
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: 110.12 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 84 AGAARNAIDSALWDLQVHSGSQNLWQLTGTTAPvQIETAQTVCVDVPEMMASSALALWENGAKLIKIK--LDDHMIAERL 161
Cdd:cd03315 41 AEATKAAVDMALWDLWGKRLGVPVYLLLGGYRD-RVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKvgRDPARDVAVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 162 VAIRSAVPQ-AMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFVH--PLPICADESCHSVDSL--AA 236
Cdd:cd03315 120 AALREAVGDdAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARatDTPIMADESAFTPHDAfrEL 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490273803 237 LRGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLAPKARFVDL 298
Cdd:cd03315 200 ALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTL 261
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-299 |
7.58e-27 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 108.00 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 7 YPESWPLHSAFIIARGARHEAGVVVVELEE-NGTKGIGEC----TPYARYgETEASVLAQIA-LLLPEIEQGLTRHALQQ 80
Cdd:TIGR01928 1 YHVSEPFKSPFKTSKGTLNHRDCLIIELIDdKGNAGFGEVvafqTPWYTH-ETIATVKHIIEdFFEPNINKEFEHPSEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 81 RLPAG-----AARNAIDSALWDLQVHSGSQNLWQLTGTT---APVQIETAQTVCVDVPEMMASsalaLWENGAKLIKIKL 152
Cdd:TIGR01928 80 ELVRSlkgtpMAKAGLEMALWDMYHKLPSFSLAYGQGKLrdkAPAGAVSGLANDEQMLKQIES----LKATGYKRIKLKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 153 DDHMIAERLVAIRSAVPQAMLIVDANESWHSEGLAaRCQLLADLNISMLEQPLPAADDVALENFVHPL--PICADESCHS 230
Cdd:TIGR01928 156 TPQIMHQLVKLRRLRFPQIPLVIDANESYDLQDFP-RLKELDRYQLLYIEEPFKIDDISMLDELAKGTitPICLDESITS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 231 VDSLAAL--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCT--SRAIRAALP----------LAPKARFV 296
Cdd:TIGR01928 235 LDDARNLieLGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETgiSRAFNVALAslggndypgdVSPSGYYF 314
|
...
gi 490273803 297 DLD 299
Cdd:TIGR01928 315 DQD 317
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
12-287 |
9.51e-25 |
|
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: 102.70 E-value: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 12 PLHSAFIIARGARHEAGVVVVELE-ENGTKGIGECTPYAR--YG-ETEAS---VLAQiaLLLPEIEQGLTRHA------L 78
Cdd:cd03317 9 PLKFPFETSFGTLNEREFLIVELTdEEGITGYGEVVAFEGpfYTeETNATawhILKD--YLLPLLLGREFSHPeevserL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 79 QQRLPAGAARNAIDSALWDLQVHSGSQNLWQLTGTT---APVQIETAQTVcvDVPEMMASSALALwENGAKLIKIKLDDH 155
Cdd:cd03317 87 APIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGTrdsIPVGVSIGIQD--DVEQLLKQIERYL-EEGYKRIKLKIKPG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 156 MIAERLVAIRSAVPQAMLIVDANESWhSEGLAARCQLLADLNISMLEQPLPAADDVALENFVHPL--PICADESCHSVDS 233
Cdd:cd03317 164 WDVEPLKAVRERFPDIPLMADANSAY-TLADIPLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLktPICLDESIQSAED 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490273803 234 LAALR--GRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCT--SRAIRAAL 287
Cdd:cd03317 243 ARKAIelGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESgiGRAHNVAL 300
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
1-112 |
7.59e-20 |
|
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: 83.67 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 1 MRTVKVYPESWPLHSaFIIARGARHEAGVVVVELE-ENGTKGIGECTPY-----ARYGETEASVLAQIALLLPEIEQGLT 74
Cdd:pfam02746 1 AIEVFVVDVGWPLRP-IQMAFGTVQQQSLVIVRIEtSEGVVGIGEATSYggraeTIKAILDDHLAPLLIGRDAANISDLW 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 490273803 75 RHALQQRLPAGAARNAIDSALWDLQVHSGSQNLWQLTG 112
Cdd:pfam02746 80 QLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
133-322 |
1.76e-19 |
|
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: 85.31 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 133 MASSALALW-ENGAKLIKIKLDDHMIA---ERLVAIRSAV-PQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPA 207
Cdd:pfam13378 2 LAAEARRAVeARGFRAFKLKVGGPDPEedvERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 208 ADDVALENFVH--PLPICADESCHSVDSLAAL--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLcTSRAI 283
Cdd:pfam13378 82 DDLEGLARLRRatPVPIATGESLYSREDFRRLleAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG-GPIGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490273803 284 RAALPLA---PKARFVD--LDGPTWLAIDAEPALAFDCGRILLS 322
Cdd:pfam13378 161 AASLHLAaavPNLLIQEyfLDPLLLEDDLLTEPLEVEDGRVAVP 204
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
85-298 |
1.11e-18 |
|
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: 83.53 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 85 GAARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVcvdvpemmassalalwengaklikiklddhmiaERLVAI 164
Cdd:cd00308 41 GEVISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSI---------------------------------ERVRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 165 RSAVPQAMLI-VDANESWHSEGLAARCQLLADLNISMLEQPLPAAD--DVALENFVHPLPICADESCHSVDSL--AALRG 239
Cdd:cd00308 88 REAFGPDARLaVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDleGYAALRRRTGIPIAADESVTTVDDAleALELG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490273803 240 RYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLA---PKARFVDL 298
Cdd:cd00308 168 AVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAaalPNDRAIET 229
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
12-290 |
2.47e-17 |
|
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: 81.98 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 12 PLHSAFIIARGARHEAGVVVVEL-EENGTKGIGECTP---YARYGET-EAS------VLAQIALLLPEIEQGLTRHALQQ 80
Cdd:cd03318 13 PTRRPHQFAGTTMHTQSLVLVRLtTSDGVVGIGEATTpggPAWGGESpETIkaiidrYLAPLLIGRDATNIGAAMALLDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 81 RLPAGA-ARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIETAQTVCV-DVPEMMASSALALWENGAKLIKIKLDDHMIA 158
Cdd:cd03318 93 AVAGNLfAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASgDTERDIAEAEEMLEAGRHRRFKLKMGARPPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 159 E---RLVAIRSAVP-QAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAA--DDVALENFVHPLPICADESCHSVD 232
Cdd:cd03318 173 DdlaHVEAIAKALGdRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPREnlDGLARLRSRNRVPIMADESVSGPA 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 233 SLAAL--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLA 290
Cdd:cd03318 253 DAFELarRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLF 312
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
87-305 |
1.89e-15 |
|
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: 74.99 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 87 ARNAIDSALWDLQVHSGSQNLWQLTgttapvqIETAQTVCvDVPEMMASSALALWENGAKLIKIKLDDHMIAE---RLVA 163
Cdd:cd03320 48 LAFGIESALANLEALLVGFTRPRNR-------IPVNALLP-AGDAAALGEAKAAYGGGYRTVKLKVGATSFEEdlaRLRA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 164 IRSAVP-QAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFVHPLPICADESCHSVDSLAALR--GR 240
Cdd:cd03320 120 LREALPaDAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAAGVPIALDESLRRLDDPLALAaaGA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490273803 241 YEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLApkARFVDLDGPTWLA 305
Cdd:cd03320 200 LGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLA--AALPPLPAACGLG 262
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
9-322 |
3.13e-14 |
|
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: 72.64 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 9 ESWPLHSAFIIARGARHEAGVVVVELE-ENGTKGIGECTPYARYGETEASVLAQIALLL-------PE-IEQGLTR--HA 77
Cdd:cd03316 6 ETFVLRVPLPEPGGAVTWRNLVLVRVTtDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLigrdpldIErLWEKLYRrlFW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 78 LQQRLPAGAARNAIDSALWDLQVHSGSQNLWQLTG----TTAPV---QIETAQTvcvdvPEMMASSALALWENGAKLIKI 150
Cdd:cd03316 86 RGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGgkvrDRVRVyasGGGYDDS-----PEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 151 KLDDHMI--------AERLVAIRSAV-PQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAADDVALENFVH--P 219
Cdd:cd03316 161 KVGGPDSggedlredLARVRAVREAVgPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQatS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 220 LPICADESCHSVDSLAAL--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIM-------LGCMLCTSRAirAALPLA 290
Cdd:cd03316 241 VPIAAGENLYTRWEFRDLleAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAphgaggpIGLAASLHLA--AALPNF 318
|
330 340 350
....*....|....*....|....*....|..
gi 490273803 291 PKARFVDLDGPTWLAIDAEPALAFDcGRILLS 322
Cdd:cd03316 319 GILEYHLDDLPLREDLFKNPPEIED-GYVTVP 349
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
130-222 |
1.08e-13 |
|
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: 66.15 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 130 PEMMASSAL-ALWENGAKLIKIKL--DDHMIAERLVAIRSAV-PQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPL 205
Cdd:smart00922 1 PEELAEAARrAVAEAGFRAVKVKVggGPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
90
....*....|....*..
gi 490273803 206 PAADDVALENFVHPLPI 222
Cdd:smart00922 81 PPDDLEGLAELRRATPI 97
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-292 |
1.76e-07 |
|
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: 52.12 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 7 YPESWPLHSAFIIARG--ARHEAgvVVVELEENGTKGIGECTPYARYG-ETEASVLAQIALLLPEIEQGLTrHALQQRLP 83
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGllARREG--LIVRLTDEGRTGWGEIAPLPGFGtETLAEALDFCRALIEEITRGDI-EAIDDQLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 84 AGAArnAIDSALWDLQvhSGSQNlwqltgttAPVQIETAQTVCVDVPEMMASSALalWENGAKLIKIKLDDHMIAERLVA 163
Cdd:TIGR01927 78 SVAF--GFESALIELE--SGDEL--------PPASNYYVALLPAGDPALLLLRSA--KAEGFRTFKWKVGVGELAREGML 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 164 IRS---AVP-QAMLIVDANESWHSEGLAARCQLLA---DLNISMLEQPLPAADDVALENFVHPLPICADESCHSVDSLAA 236
Cdd:TIGR01927 144 VNLlleALPdKAELRLDANGGLSPDEAQQFLKALDpnlRGRIAFLEEPLPDADEMSAFSEATGTAIALDESLWELPQLAD 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490273803 237 L--RGRYEMVNIKLDKTGGLTAALELARCAQDQGFAIMLGCMLCTSRAIRAALPLAPK 292
Cdd:TIGR01927 224 EygPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAK 281
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
30-213 |
3.43e-05 |
|
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: 45.01 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 30 VVVELEEN-GTKGIGECTPYARYGETEASVLAQIALLLPE----IE---QGLTRHALQQRLPA-GAARNAIDSALWDLQV 100
Cdd:cd03325 15 LFVKIETDeGVVGWGEPTVEGKARTVEAAVQELEDYLIGKdpmnIEhhwQVMYRGGFYRGGPVlMSAISGIDQALWDIKG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 101 HSGSQNLWQLTGTTAPVQIETAQTVCVDVPEMMASSALALWENGAKLIKIKLDDHM-----------IAERLVAIRSAV- 168
Cdd:cd03325 95 KVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNATEELqwidtskkvdaAVERVAALREAVg 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490273803 169 PQAMLIVDAneswH---SEGLAAR-CQLLADLNISMLEQPLPAADDVAL 213
Cdd:cd03325 175 PDIDIGVDF----HgrvSKPMAKDlAKELEPYRLLFIEEPVLPENVEAL 219
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
56-209 |
1.81e-04 |
|
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: 42.85 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 56 ASVLAQIALLLPEIEQGLTRH--ALQQRLPAGAARNAIDSALWDLQVHSGSQNLWQLTGTtAPVQIETAQTVCVDVPEMM 133
Cdd:cd03321 67 AALLVGEPLAPAELERALAKRfrLLGYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGG-NPRPVQAYDSHGLDGAKLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 134 ASSALALWENGAKLIKIKLDDHMIAERLVAIRS---AVPQAM-LIVDANESWHSEGLAARCQLLADLNISMLEQPLPAAD 209
Cdd:cd03321 146 TERAVTAAEEGFHAVKTKIGYPTADEDLAVVRSirqAVGDGVgLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHD 225
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
28-209 |
8.01e-04 |
|
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: 40.78 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 28 GVVVVELE-ENGTKGIGECTpyarygetEASVLAQIalllpeIEQGLTR---------------HALQQRLPAG------ 85
Cdd:cd03327 10 GWLFVEIEtDDGTVGYANTT--------GGPVACWI------VDQHLARfligkdpsdieklwdQMYRATLAYGrkgiam 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 86 AARNAIDSALWDLQVHSGSQNLWQLTGTTAPVQIET-AQTVCVDVPEMMASSALALWENGAKLIKIKL----DDHMIA-- 158
Cdd:cd03327 76 AAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAyASGLYPTDLDELPDEAKEYLKEGYRGMKMRFgygpSDGHAGlr 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490273803 159 ---ERLVAIRSAV-PQAMLIVDANESWHSEGLAARCQLLADLNISMLEQPLPAAD 209
Cdd:cd03327 156 knvELVRAIREAVgYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDD 210
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
128-240 |
1.03e-03 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 40.34 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273803 128 DVPEMMASSAlalwenGAKLIKIKLDDH--MIAE---RLVAIRSAV-PQAMLIVDANESWH-SEGLAARCQLLADLNISM 200
Cdd:PRK02901 92 QVPEVLARFP------GCRTAKVKVAEPgqTLADdvaRVNAVRDALgPDGRVRVDANGGWSvDEAVAAARALDADGPLEY 165
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 490273803 201 LEQPlpaaddvalenfvhplpicadesCHSVDSLAALRGR 240
Cdd:PRK02901 166 VEQP-----------------------CATVEELAELRRR 182
|
|
| |
