|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
1-320 |
0e+00 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 618.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 1 MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDC--ELP 78
Cdd:PRK05105 1 MRSAQLYRYQIPMDAGVPLRKQRLKTRDGLVVQLREGEREGWGEIAPLPGFSQETLEEAQEALLAWLNNWLAGDCddELS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 79 QMPSVAFGVSCALAELADTLPQAANYRAAPLCNGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLHL 158
Cdd:PRK05105 81 QYPSVAFGLSCALAELAGTLPQAANYRTAPLCYGDPDELILKLADMPGEKVAKVKVGLYEAVRDGMLVNLLLEAIPDLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 159 RLDANRAWTPLKGQQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLREPDFAFVAEEGVRAVVIKPTL 238
Cdd:PRK05105 161 RLDANRGWTLEKAQQFAKYVPPDYRHRIAFLEEPCKTPDDSRAFARATGIAIAWDESLREPDFQFEAEPGVRAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 239 TGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQVRRWPGSTLPVVEVDALER 318
Cdd:PRK05105 241 TGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLAAWLTPDTIPGLDTLDLMQAQLVRPWPGSKLPLLTLDELEL 320
|
..
gi 1230334350 319 LL 320
Cdd:PRK05105 321 LW 322
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
1-319 |
0e+00 |
|
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: 608.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 1 MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDC--ELP 78
Cdd:COG1441 1 MRHATLYRYSIPMDAGVILRNQRLKTRDGLLVRLQEGGREGWGEIAPLPGFSQETLEQAEQQALAWLQRWLAGDLldEKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 79 QMPSVAFGVSCALAELADTLPQAANYRAAPLCNGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLHL 158
Cdd:COG1441 81 LLPSVAFGLSCALAELEGELPEAANYRAAPLCSGDPDELIARLNQMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 159 RLDANRAWTPLKGQQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLREPDFAFVAEEGVRAVVIKPTL 238
Cdd:COG1441 161 RLDANRSWTLDKAVQFAKYVNPEHRSRIAFLEEPCKTPEESREFARETGIAIAWDESVREPDFRVEAEPGVAAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 239 TGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQVRRWPGSTLPVVEVDALER 318
Cdd:COG1441 241 VGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTQLARLAAWLTPDTAPGLDTLDLMQAQLLRPWPGSDLPLVALDSLEI 320
|
.
gi 1230334350 319 L 319
Cdd:COG1441 321 V 321
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-306 |
1.65e-156 |
|
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: 440.01 E-value: 1.65e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 7 YRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDCELP--QMPSVA 84
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDEGRTGWGEIAPLPGFGTETLAEALDFCRALIEEITRGDIEAIddQLPSVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 85 FGVSCALAELADT--LPQAANYRAAPLCNGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPD-LHLRLD 161
Cdd:TIGR01927 81 FGFESALIELESGdeLPPASNYYVALLPAGDPALLLLRSAKAEGFRTFKWKVGVGELAREGMLVNLLLEALPDkAELRLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 162 ANRAWTPLKGQQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLRE-PDFAFVAEEGVR-AVVIKPTLT 239
Cdd:TIGR01927 161 ANGGLSPDEAQQFLKALDPNLRGRIAFLEEPLPDADEMSAFSEATGTAIALDESLWElPQLADEYGPGWRgALVIKPAII 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1230334350 240 GSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQVRRWPGS 306
Cdd:TIGR01927 241 GSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLSPDPAAVGFTTALLRAQDLEAWPFS 307
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
4-291 |
3.60e-78 |
|
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: 239.08 E-value: 3.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 4 AQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREG-EREGWGEISPLPgfsqetweeaqsvllawvnnwlagdcelpqmps 82
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLtGPVGWGEIAPLP--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 83 VAFGVSCALAELADTL-----PQAANYRAAPLCNGDPDDLI-LKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIP-D 155
Cdd:cd03320 48 LAFGIESALANLEALLvgftrPRNRIPVNALLPAGDAAALGeAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPaD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 156 LHLRLDANRAWTPLKGQQFAKYVNPDyrhRIAFLEEPCKTRDDSRAFARETGIAIAWDESLR--EPDFAFVAEEGVRAVV 233
Cdd:cd03320 128 AKLRLDANGGWSLEEALAFLEALAAG---RIEYIEQPLPPDDLAELRRLAAGVPIALDESLRrlDDPLALAAAGALGALV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1230334350 234 IKPTLTGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTP-DTIPGLDT 291
Cdd:cd03320 205 LKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPlPAACGLGT 263
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
116-271 |
1.85e-13 |
|
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: 68.36 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 116 DLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAI-PDLHLRLDANRAWTPLKGQQFAKYVNPdyrHRIAFLEEPCK 194
Cdd:pfam13378 4 AEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEE---LGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 195 TRDDS--RAFARETGIAIAWDESLREP-DFA-FVAEEGVRAVVIKPTLTGSLEKVREQVQAAHALGLtAVISSSIESSLG 270
Cdd:pfam13378 81 PDDLEglARLRRATPVPIATGESLYSReDFRrLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGV-PVAPHSGGGPIG 159
|
.
gi 1230334350 271 L 271
Cdd:pfam13378 160 L 160
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
116-208 |
4.85e-10 |
|
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: 55.75 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 116 DLILKLADMPGEKVAKVKVGLYEAvRDGMVVNLLLEAI-PDLHLRLDANRAWTPLKGQQFAKYVNPdyrHRIAFLEEPCK 194
Cdd:smart00922 6 EAARRAVAEAGFRAVKVKVGGGPL-EDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDE---LGLEWIEEPVP 81
|
90
....*....|....*.
gi 1230334350 195 TRDDS--RAFARETGI 208
Cdd:smart00922 82 PDDLEglAELRRATPI 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
1-320 |
0e+00 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 618.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 1 MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDC--ELP 78
Cdd:PRK05105 1 MRSAQLYRYQIPMDAGVPLRKQRLKTRDGLVVQLREGEREGWGEIAPLPGFSQETLEEAQEALLAWLNNWLAGDCddELS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 79 QMPSVAFGVSCALAELADTLPQAANYRAAPLCNGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLHL 158
Cdd:PRK05105 81 QYPSVAFGLSCALAELAGTLPQAANYRTAPLCYGDPDELILKLADMPGEKVAKVKVGLYEAVRDGMLVNLLLEAIPDLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 159 RLDANRAWTPLKGQQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLREPDFAFVAEEGVRAVVIKPTL 238
Cdd:PRK05105 161 RLDANRGWTLEKAQQFAKYVPPDYRHRIAFLEEPCKTPDDSRAFARATGIAIAWDESLREPDFQFEAEPGVRAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 239 TGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQVRRWPGSTLPVVEVDALER 318
Cdd:PRK05105 241 TGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLAAWLTPDTIPGLDTLDLMQAQLVRPWPGSKLPLLTLDELEL 320
|
..
gi 1230334350 319 LL 320
Cdd:PRK05105 321 LW 322
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
1-319 |
0e+00 |
|
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: 608.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 1 MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDC--ELP 78
Cdd:COG1441 1 MRHATLYRYSIPMDAGVILRNQRLKTRDGLLVRLQEGGREGWGEIAPLPGFSQETLEQAEQQALAWLQRWLAGDLldEKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 79 QMPSVAFGVSCALAELADTLPQAANYRAAPLCNGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLHL 158
Cdd:COG1441 81 LLPSVAFGLSCALAELEGELPEAANYRAAPLCSGDPDELIARLNQMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 159 RLDANRAWTPLKGQQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLREPDFAFVAEEGVRAVVIKPTL 238
Cdd:COG1441 161 RLDANRSWTLDKAVQFAKYVNPEHRSRIAFLEEPCKTPEESREFARETGIAIAWDESVREPDFRVEAEPGVAAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 239 TGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQVRRWPGSTLPVVEVDALER 318
Cdd:COG1441 241 VGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTQLARLAAWLTPDTAPGLDTLDLMQAQLLRPWPGSDLPLVALDSLEI 320
|
.
gi 1230334350 319 L 319
Cdd:COG1441 321 V 321
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-306 |
1.65e-156 |
|
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: 440.01 E-value: 1.65e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 7 YRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDCELP--QMPSVA 84
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDEGRTGWGEIAPLPGFGTETLAEALDFCRALIEEITRGDIEAIddQLPSVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 85 FGVSCALAELADT--LPQAANYRAAPLCNGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPD-LHLRLD 161
Cdd:TIGR01927 81 FGFESALIELESGdeLPPASNYYVALLPAGDPALLLLRSAKAEGFRTFKWKVGVGELAREGMLVNLLLEALPDkAELRLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 162 ANRAWTPLKGQQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLRE-PDFAFVAEEGVR-AVVIKPTLT 239
Cdd:TIGR01927 161 ANGGLSPDEAQQFLKALDPNLRGRIAFLEEPLPDADEMSAFSEATGTAIALDESLWElPQLADEYGPGWRgALVIKPAII 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1230334350 240 GSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQVRRWPGS 306
Cdd:TIGR01927 241 GSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLSPDPAAVGFTTALLRAQDLEAWPFS 307
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
4-291 |
3.60e-78 |
|
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: 239.08 E-value: 3.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 4 AQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREG-EREGWGEISPLPgfsqetweeaqsvllawvnnwlagdcelpqmps 82
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLtGPVGWGEIAPLP--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 83 VAFGVSCALAELADTL-----PQAANYRAAPLCNGDPDDLI-LKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIP-D 155
Cdd:cd03320 48 LAFGIESALANLEALLvgftrPRNRIPVNALLPAGDAAALGeAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPaD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 156 LHLRLDANRAWTPLKGQQFAKYVNPDyrhRIAFLEEPCKTRDDSRAFARETGIAIAWDESLR--EPDFAFVAEEGVRAVV 233
Cdd:cd03320 128 AKLRLDANGGWSLEEALAFLEALAAG---RIEYIEQPLPPDDLAELRRLAAGVPIALDESLRrlDDPLALAAAGALGALV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1230334350 234 IKPTLTGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTP-DTIPGLDT 291
Cdd:cd03320 205 LKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPlPAACGLGT 263
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
4-288 |
3.50e-70 |
|
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: 218.75 E-value: 3.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 4 AQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGE-REGWGEISplpgfsqetweeaqsvllawvnnwlagdcelpqmps 82
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDgLVGWAEAT------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 83 vAFGVSCALAELADTL----------PQAANYRAAPLCNG----DPDDLILKLADMpGEKVAKVKVGLYEAvRDGMVVNL 148
Cdd:cd03315 45 -KAAVDMALWDLWGKRlgvpvylllgGYRDRVRVAHMLGLgepaEVAEEARRALEA-GFRTFKLKVGRDPA-RDVAVVAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 149 LLEAIP-DLHLRLDANRAWTPLKGQQFAKYVNPDyrhRIAFLEEPCKTRD--DSRAFARETGIAIAWDESLREPDFAF-- 223
Cdd:cd03315 122 LREAVGdDAELRVDANRGWTPKQAIRALRALEDL---GLDYVEQPLPADDleGRAALARATDTPIMADESAFTPHDAFre 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1230334350 224 VAEEGVRAVVIKPTLTGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPG 288
Cdd:cd03315 199 LALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPG 263
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
4-289 |
2.74e-42 |
|
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: 145.93 E-value: 2.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 4 AQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLR-EGEREGWGEisplpgfsqetweeaqsvllawvnnwlagdcelpqmps 82
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTtDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 83 VAFGVSCALAELADtlpQAANyraaplcngdpddliLKLADMPGEKVAKvkvgLYEAVRDGMVVNLLLEAIP-DLHLRLD 161
Cdd:cd00308 43 VISGIDMALWDLAA---KALG---------------VPLAELLGGGSRD----RVPAYGSIERVRAVREAFGpDARLAVD 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 162 ANRAWTPLKGQQFAKYVNPDyrhRIAFLEEPCKT--RDDSRAFARETGIAIAWDESLREPDFA--FVAEEGVRAVVIKPT 237
Cdd:cd00308 101 ANGAWTPKEAIRLIRALEKY---GLAWIEEPCAPddLEGYAALRRRTGIPIAADESVTTVDDAleALELGAVDILQIKPT 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1230334350 238 LTGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGL 289
Cdd:cd00308 178 RVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPNDRAIET 229
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-294 |
6.42e-23 |
|
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: 97.20 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 1 MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLR-EGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDCE--L 77
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVEtDDGITGWGEAVPGGTGAEAVAAALEEALAPLLIGRDPLDIEalW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 78 PQMPSVAFGVSCALA--ELA--DTLPQAAN----------YRAAPLCN-----GDPDDLILKLADM--PGEKVAKVKVGL 136
Cdd:COG4948 83 QRLYRALPGNPAAKAavDMAlwDLLGKALGvpvyqllggkVRDRVPVYatlgiDTPEEMAEEAREAvaRGFRALKLKVGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 137 YEAVRDGMVVNLLLEAI-PDLHLRLDANRAWTPLKGQQFAKYVNPdyrHRIAFLEEPCKTRDDS--RAFARETGIAIAWD 213
Cdd:COG4948 163 PDPEEDVERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALED---LGLEWIEQPLPAEDLEglAELRRATPVPIAAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 214 ESLREP-DFA-FVAEEGVRAVVIKPTLTGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAwltpdTIPGLDT 291
Cdd:COG4948 240 ESLTSRaDFRrLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAA-----ALPNFDI 314
|
...
gi 1230334350 292 LDL 294
Cdd:COG4948 315 VEL 317
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
110-281 |
1.05e-19 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 89.92 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 110 CNGDPDDLILKLADMPGEKVA--KVKVGLYEA-VRDGMVVNLLLEAIP-DLHLRLDANRAWTPLKGQQFAKYVNpdyRHR 185
Cdd:PLN02980 1087 SNGSPLEVAYVARKLVEEGFSaiKLKVGRRVSpIQDAAVIQEVRKAVGyQIELRADANRNWTYEEAIEFGSLVK---SCN 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 186 IAFLEEPCKTRDDSRAFARETGIAIAWDESLRE------PDFAFVAEEGVRAVVIKPTLTGSLEKVREQVQAAHALGLTA 259
Cdd:PLN02980 1164 LKYIEEPVQDEDDLIKFCEETGLPVALDETIDKfeecplRMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGKMA 1243
|
170 180
....*....|....*....|..
gi 1230334350 260 VISSSIESSLGLTQLARIAAWL 281
Cdd:PLN02980 1244 VISAAYESGLGLSAYIQFASYL 1265
|
|
| 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 ... |
22-294 |
1.82e-18 |
|
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: 84.16 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 22 RRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQSVLLAWVNNWLAGDCE-----------LPQMPSVAFGVSCA 90
Cdd:cd03319 20 GSRTEAENVIVEIELDGITGYGEAAPTPRVTGETVESVLAALKSVRPALIGGDPRlekllealqelLPGNGAARAAVDIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 91 LAELAdtlpqaANYRAAPLCN------------------GDPDDLILKLADMP--GEKVAKVKVGLY--------EAVRd 142
Cdd:cd03319 100 LWDLE------AKLLGLPLYQlwgggaprpletdytisiDTPEAMAAAAKKAAkrGFPLLKIKLGGDleddieriRAIR- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 143 gmvvnlllEAIPDLHLRLDANRAWTPlkgQQFAKYVNPDYRHRIAFLEEPCKTRDDS--RAFARETGIAIAWDESLREP- 219
Cdd:cd03319 173 --------EAAPDARLRVDANQGWTP---EEAVELLRELAELGVELIEQPVPAGDDDglAYLRDKSPLPIMADESCFSAa 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1230334350 220 DFAFVAEEG-VRAVVIKPTLTGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQlariAAWLTPDTIpglDTLDL 294
Cdd:cd03319 242 DAARLAGGGaYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAA----AAHLAAAKA---DFVDL 310
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
25-281 |
2.84e-16 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 78.13 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 25 KTRDGLYVCLR-EGEREGWGEISPLPGFSQETWEEAQSV------LLAWVNNWLAGDcelpQMPSVAFGVSCALaELADT 97
Cdd:PRK02714 26 RIREGIILRLTdETGKIGWGEIAPLPWFGSETLEEALAFcqqlpgEITPEQIFSIPD----ALPACQFGFESAL-ENESG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 98 LPQAANYRAAPLC----NGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIP-DLHLRLDANRAWTPLKGQ 172
Cdd:PRK02714 101 SRSNVTLNPLSYSallpAGEAALQQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQLLERLPaGAKLRLDANGGLSLEEAK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 173 QFAKYVNPDYRHRIAFLEEPCKTR--DDSRAFARETGIAIAWDES---LREpdFAFVAEEGVRAV-VIKPTLTGSLEKVR 246
Cdd:PRK02714 181 RWLQLCDRRLSGKIEFIEQPLPPDqfDEMLQLSQDYQTPIALDESvanLAQ--LQQCYQQGWRGIfVIKPAIAGSPSRLR 258
|
250 260 270
....*....|....*....|....*....|....*
gi 1230334350 247 EQVQAAHalgLTAVISSSIESSLGLTQLARIAAWL 281
Cdd:PRK02714 259 QFCQQHP---LDAVFSSVFETAIGRKAALALAAEL 290
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
116-271 |
1.85e-13 |
|
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: 68.36 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 116 DLILKLADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAI-PDLHLRLDANRAWTPLKGQQFAKYVNPdyrHRIAFLEEPCK 194
Cdd:pfam13378 4 AEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEE---LGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 195 TRDDS--RAFARETGIAIAWDESLREP-DFA-FVAEEGVRAVVIKPTLTGSLEKVREQVQAAHALGLtAVISSSIESSLG 270
Cdd:pfam13378 81 PDDLEglARLRRATPVPIATGESLYSReDFRrLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGV-PVAPHSGGGPIG 159
|
.
gi 1230334350 271 L 271
Cdd:pfam13378 160 L 160
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
9-297 |
1.89e-12 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 66.92 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 9 WQIPMDagvvLRDRRLKTRDGLyvcLREGErEGWGEISPLPGFSQEtwEEAQsvllawvnnWLAgdcelpqmpsvafgvs 88
Cdd:PRK02901 17 VALPMR----VRFRGITVREAV---LIEGP-AGWGEFSPFLEYDPA--EAAA---------WLA---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 89 CALaELADTLPQAANYRAAPLcNG-----DPDDLILKLADMPGEKVAKVKVG-----------LYEAVRDGMVvnlllea 152
Cdd:PRK02901 62 SAI-EAAYGGPPPPVRDRVPV-NAtvpavDAAQVPEVLARFPGCRTAKVKVAepgqtladdvaRVNAVRDALG------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 153 iPDLHLRLDANRAWTplKGQQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLREPD--FAFVAEEGVR 230
Cdd:PRK02901 133 -PDGRVRVDANGGWS--VDEAVAAARALDADGPLEYVEQPCATVEELAELRRRVGVPIAADESIRRAEdpLRVARAGAAD 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1230334350 231 AVVIKPTLTGSlekVREQVQAAHALGLTAVISSSIESSLGLT-QLARIAAWLTPDTIPGLDTLDLMQA 297
Cdd:PRK02901 210 VAVLKVAPLGG---VRAALDIAEQIGLPVVVSSALDTSVGIAaGLALAAALPELDHACGLATGGLFEE 274
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
116-208 |
4.85e-10 |
|
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: 55.75 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 116 DLILKLADMPGEKVAKVKVGLYEAvRDGMVVNLLLEAI-PDLHLRLDANRAWTPLKGQQFAKYVNPdyrHRIAFLEEPCK 194
Cdd:smart00922 6 EAARRAVAEAGFRAVKVKVGGGPL-EDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDE---LGLEWIEEPVP 81
|
90
....*....|....*.
gi 1230334350 195 TRDDS--RAFARETGI 208
Cdd:smart00922 82 PDDLEglAELRRATPI 97
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
149-291 |
1.89e-08 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 55.02 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 149 LLEAIPDLHLRLDANRAWTPlkgqQFAKYVNPDYRHRIAFLEEPCKTRDDSRAFARETG-------IAIAWDEsLREPdf 221
Cdd:cd03323 207 LAEAFPGARLRLDPNGAWSL----ETAIRLAKELEGVLAYLEDPCGGREGMAEFRRATGlplatnmIVTDFRQ-LGHA-- 279
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 222 afVAEEGVRAVVIKPTLTGSLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAwltpdTIPGLDT 291
Cdd:cd03323 280 --IQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNNHLGISLAMMTHVAA-----AAPGLIT 342
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
108-290 |
2.03e-08 |
|
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: 55.02 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 108 PLCNGDPDDLILKLADMPGEK---VAKVKVGLYEAVRDGMVVNLLLEAIPD-LHLRLDANRAWTPlkgQQFAKYVNPDYR 183
Cdd:cd03318 137 TLASGDTERDIAEAEEMLEAGrhrRFKLKMGARPPADDLAHVEAIAKALGDrASVRVDVNQAWDE---STAIRALPRLEA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 184 HRIAFLEEPCkTRDDSRAFAR---ETGIAIAWDESLREPD--FAFVAEEGVRAVVIKPTLTGSLEKVREQVQAAHALGLT 258
Cdd:cd03318 214 AGVELIEQPV-PRENLDGLARlrsRNRVPIMADESVSGPAdaFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIA 292
|
170 180 190
....*....|....*....|....*....|..
gi 1230334350 259 AVISSSIESSLGLTQLARIAAwltpdTIPGLD 290
Cdd:cd03318 293 LYGGTMLESSIGTAASAHLFA-----TLPSLP 319
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
131-216 |
4.62e-05 |
|
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: 44.52 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 131 KVKVGLYEAV-----RDGMVVNLLLEAI-PDLHLRLDANRAWTPLKGQQFAKYVNPdyrHRIAFLEEPCKT--RDDSRAF 202
Cdd:cd03316 159 KLKVGGPDSGgedlrEDLARVRAVREAVgPDVDLMVDANGRWDLAEAIRLARALEE---YDLFWFEEPVPPddLEGLARL 235
|
90
....*....|....
gi 1230334350 203 ARETGIAIAWDESL 216
Cdd:cd03316 236 RQATSVPIAAGENL 249
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
91-260 |
8.50e-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: 37.69 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 91 LAELADTLpQAANYRAAPLcNGDPDDLILKLADMPGEKVAKVkvglyEAVRDGmvVNLLLEAIPDLHLRLDANRAwtplk 170
Cdd:cd03325 127 VAEAARAR-REAGFTAVKM-NATEELQWIDTSKKVDAAVERV-----AALREA--VGPDIDIGVDFHGRVSKPMA----- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230334350 171 gQQFAKYVNPdyrHRIAFLEEPCKTRDDS--RAFARETGIAIAWDESL-REPDFAFVAEEGVRAVVikptltgslekvre 247
Cdd:cd03325 193 -KDLAKELEP---YRLLFIEEPVLPENVEalAEIAARTTIPIATGERLfSRWDFKELLEDGAVDII-------------- 254
|
170
....*....|...
gi 1230334350 248 QVQAAHALGLTAV 260
Cdd:cd03325 255 QPDISHAGGITEL 267
|
|
| |
