|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
1-321 |
0e+00 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 567.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 1 MRAAQLYRYQVPMDAGVVLRERRLKTRDGLLVRLSDNGREGWGDIAPLPGFSDETLDAALSAARDWLRAWQRGDAQPL-P 79
Cdd:PRK05105 1 MRSAQLYRYQIPMDAGVPLRKQRLKTRDGLVVQLREGEREGWGEIAPLPGFSQETLEEAQEALLAWLNNWLAGDCDDElS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 80 EVASVAFGLSMAQAELHGTLPVAANYHTAPLCTGDPDELFARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIPDLTL 159
Cdd:PRK05105 81 QYPSVAFGLSCALAELAGTLPQAANYRTAPLCYGDPDELILKLADMPGEKVAKVKVGLYEAVRDGMLVNLLLEAIPDLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 160 RLDANRAWTPLKAQQFAKYVNPAYRSRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRERDFSITAEPGLRAVIIKPTL 239
Cdd:PRK05105 161 RLDANRGWTLEKAQQFAKYVPPDYRHRIAFLEEPCKTPDDSRAFARATGIAIAWDESLREPDFQFEAEPGVRAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 240 TGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPGLDTLALMQAQLVRPWPGSPLPCWPVDALEP 319
Cdd:PRK05105 241 TGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLAAWLTPDTIPGLDTLDLMQAQLVRPWPGSKLPLLTLDELEL 320
|
..
gi 1355064373 320 LL 321
Cdd:PRK05105 321 LW 322
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
1-320 |
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: 558.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 1 MRAAQLYRYQVPMDAGVVLRERRLKTRDGLLVRLSDNGREGWGDIAPLPGFSDETLDAALSAARDWLRAWQRGDAQPL-P 79
Cdd:COG1441 1 MRHATLYRYSIPMDAGVILRNQRLKTRDGLLVRLQEGGREGWGEIAPLPGFSQETLEQAEQQALAWLQRWLAGDLLDEkS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 80 EVASVAFGLSMAQAELHGTLPVAANYHTAPLCTGDPDELFARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIPDLTL 159
Cdd:COG1441 81 LLPSVAFGLSCALAELEGELPEAANYRAAPLCSGDPDELIARLNQMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 160 RLDANRAWTPLKAQQFAKYVNPAYRSRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRERDFSITAEPGLRAVIIKPTL 239
Cdd:COG1441 161 RLDANRSWTLDKAVQFAKYVNPEHRSRIAFLEEPCKTPEESREFARETGIAIAWDESVREPDFRVEAEPGVAAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 240 TGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPGLDTLALMQAQLVRPWPGSPLPCWPVDALEP 319
Cdd:COG1441 241 VGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTQLARLAAWLTPDTAPGLDTLDLMQAQLLRPWPGSDLPLVALDSLEI 320
|
.
gi 1355064373 320 L 320
Cdd:COG1441 321 V 321
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-307 |
8.83e-123 |
|
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: 354.50 E-value: 8.83e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 7 YRYQVPMDAGVVLRERRLKTRDGLLVRLSDNGREGWGDIAPLPGFSDETLDAALSAARDWLRAWQRGDAQPLP-EVASVA 85
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDEGRTGWGEIAPLPGFGTETLAEALDFCRALIEEITRGDIEAIDdQLPSVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 86 FGLSMAQAELHGT--LPVAANYHTAPLCTGDPDELFARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIPD-LTLRLD 162
Cdd:TIGR01927 81 FGFESALIELESGdeLPPASNYYVALLPAGDPALLLLRSAKAEGFRTFKWKVGVGELAREGMLVNLLLEALPDkAELRLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 163 ANRAWTPLKAQQFAKYVNPAYRSRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRER-DFSITAEPGLR-AVIIKPTLT 240
Cdd:TIGR01927 161 ANGGLSPDEAQQFLKALDPNLRGRIAFLEEPLPDADEMSAFSEATGTAIALDESLWELpQLADEYGPGWRgALVIKPAII 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355064373 241 GSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPGLDTLALMQAQLVRPWPGS 307
Cdd:TIGR01927 241 GSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLSPDPAAVGFTTALLRAQDLEAWPFS 307
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
4-292 |
4.46e-66 |
|
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: 208.27 E-value: 4.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 4 AQLYRYQVPMDAGVVLRERRLKTRDGLLVRL-SDNGREGWGDIAPLPgfsdetldaalsaardwlrawqrgdaqplpeva 82
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLeDLTGPVGWGEIAPLP--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 83 sVAFGLSMAQAEL-----HGTLPVAANYHTAPLCTGDPDELF-ARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIP- 155
Cdd:cd03320 48 -LAFGIESALANLeallvGFTRPRNRIPVNALLPAGDAAALGeAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPa 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 156 DLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLR--ERDFSITAEPGLRAV 233
Cdd:cd03320 127 DAKLRLDANGGWSLEEALAFLEALAAG---RIEYIEQPLPPDDLAELRRLAAGVPIALDESLRrlDDPLALAAAGALGAL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 234 IIKPTLTGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTP-GLDT 292
Cdd:cd03320 204 VLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPLPAAcGLGT 263
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
117-209 |
8.74e-11 |
|
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: 57.68 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 117 ELFARLAGLTGKKVAKVKVGLYEAvRDGMVVNLLLEAI-PDLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCK 195
Cdd:smart00922 6 EAARRAVAEAGFRAVKVKVGGGPL-EDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDEL---GLEWIEEPVP 81
|
90
....*....|....*.
gi 1355064373 196 TPDDS--RAFAAETGI 209
Cdd:smart00922 82 PDDLEglAELRRATPI 97
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
129-220 |
5.98e-10 |
|
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: 58.35 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 129 KVAKVKVGLYEAVRDGMVVNLLLEAI-PDLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPDDS--RAFAA 205
Cdd:pfam13378 16 RAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEEL---GLLWIEEPVPPDDLEglARLRR 92
|
90
....*....|....*
gi 1355064373 206 ETGIAIAWDESLRER 220
Cdd:pfam13378 93 ATPVPIATGESLYSR 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
1-321 |
0e+00 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 567.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 1 MRAAQLYRYQVPMDAGVVLRERRLKTRDGLLVRLSDNGREGWGDIAPLPGFSDETLDAALSAARDWLRAWQRGDAQPL-P 79
Cdd:PRK05105 1 MRSAQLYRYQIPMDAGVPLRKQRLKTRDGLVVQLREGEREGWGEIAPLPGFSQETLEEAQEALLAWLNNWLAGDCDDElS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 80 EVASVAFGLSMAQAELHGTLPVAANYHTAPLCTGDPDELFARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIPDLTL 159
Cdd:PRK05105 81 QYPSVAFGLSCALAELAGTLPQAANYRTAPLCYGDPDELILKLADMPGEKVAKVKVGLYEAVRDGMLVNLLLEAIPDLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 160 RLDANRAWTPLKAQQFAKYVNPAYRSRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRERDFSITAEPGLRAVIIKPTL 239
Cdd:PRK05105 161 RLDANRGWTLEKAQQFAKYVPPDYRHRIAFLEEPCKTPDDSRAFARATGIAIAWDESLREPDFQFEAEPGVRAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 240 TGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPGLDTLALMQAQLVRPWPGSPLPCWPVDALEP 319
Cdd:PRK05105 241 TGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLAAWLTPDTIPGLDTLDLMQAQLVRPWPGSKLPLLTLDELEL 320
|
..
gi 1355064373 320 LL 321
Cdd:PRK05105 321 LW 322
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
1-320 |
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: 558.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 1 MRAAQLYRYQVPMDAGVVLRERRLKTRDGLLVRLSDNGREGWGDIAPLPGFSDETLDAALSAARDWLRAWQRGDAQPL-P 79
Cdd:COG1441 1 MRHATLYRYSIPMDAGVILRNQRLKTRDGLLVRLQEGGREGWGEIAPLPGFSQETLEQAEQQALAWLQRWLAGDLLDEkS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 80 EVASVAFGLSMAQAELHGTLPVAANYHTAPLCTGDPDELFARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIPDLTL 159
Cdd:COG1441 81 LLPSVAFGLSCALAELEGELPEAANYRAAPLCSGDPDELIARLNQMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 160 RLDANRAWTPLKAQQFAKYVNPAYRSRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRERDFSITAEPGLRAVIIKPTL 239
Cdd:COG1441 161 RLDANRSWTLDKAVQFAKYVNPEHRSRIAFLEEPCKTPEESREFARETGIAIAWDESVREPDFRVEAEPGVAAIVIKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 240 TGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPGLDTLALMQAQLVRPWPGSPLPCWPVDALEP 319
Cdd:COG1441 241 VGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTQLARLAAWLTPDTAPGLDTLDLMQAQLLRPWPGSDLPLVALDSLEI 320
|
.
gi 1355064373 320 L 320
Cdd:COG1441 321 V 321
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
7-307 |
8.83e-123 |
|
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: 354.50 E-value: 8.83e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 7 YRYQVPMDAGVVLRERRLKTRDGLLVRLSDNGREGWGDIAPLPGFSDETLDAALSAARDWLRAWQRGDAQPLP-EVASVA 85
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDEGRTGWGEIAPLPGFGTETLAEALDFCRALIEEITRGDIEAIDdQLPSVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 86 FGLSMAQAELHGT--LPVAANYHTAPLCTGDPDELFARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIPD-LTLRLD 162
Cdd:TIGR01927 81 FGFESALIELESGdeLPPASNYYVALLPAGDPALLLLRSAKAEGFRTFKWKVGVGELAREGMLVNLLLEALPDkAELRLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 163 ANRAWTPLKAQQFAKYVNPAYRSRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRER-DFSITAEPGLR-AVIIKPTLT 240
Cdd:TIGR01927 161 ANGGLSPDEAQQFLKALDPNLRGRIAFLEEPLPDADEMSAFSEATGTAIALDESLWELpQLADEYGPGWRgALVIKPAII 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355064373 241 GSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPGLDTLALMQAQLVRPWPGS 307
Cdd:TIGR01927 241 GSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLSPDPAAVGFTTALLRAQDLEAWPFS 307
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
4-292 |
4.46e-66 |
|
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: 208.27 E-value: 4.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 4 AQLYRYQVPMDAGVVLRERRLKTRDGLLVRL-SDNGREGWGDIAPLPgfsdetldaalsaardwlrawqrgdaqplpeva 82
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLeDLTGPVGWGEIAPLP--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 83 sVAFGLSMAQAEL-----HGTLPVAANYHTAPLCTGDPDELF-ARLAGLTGKKVAKVKVGLYEAVRDGMVVNLLLEAIP- 155
Cdd:cd03320 48 -LAFGIESALANLeallvGFTRPRNRIPVNALLPAGDAAALGeAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPa 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 156 DLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLR--ERDFSITAEPGLRAV 233
Cdd:cd03320 127 DAKLRLDANGGWSLEEALAFLEALAAG---RIEYIEQPLPPDDLAELRRLAAGVPIALDESLRrlDDPLALAAAGALGAL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 234 IIKPTLTGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTP-GLDT 292
Cdd:cd03320 204 VLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPLPAAcGLGT 263
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
4-289 |
8.46e-50 |
|
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: 166.36 E-value: 8.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 4 AQLYRYQVPMDAGVVLRERRLKTRDGLLVRL-SDNGREGWGDIAplpgfsdetldaalsaardwlrawqrgdaqplpeva 82
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLhTDDGLVGWAEAT------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 83 svAFGLSMAQAELHGTL----------PVAANYHTAPLCTGDPDELFARLAGLT---GKKVAKVKVGLYEAvRDGMVVNL 149
Cdd:cd03315 45 --KAAVDMALWDLWGKRlgvpvylllgGYRDRVRVAHMLGLGEPAEVAEEARRAleaGFRTFKLKVGRDPA-RDVAVVAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 150 LLEAIP-DLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPD--DSRAFAAETGIAIAWDESLRERD--FSI 224
Cdd:cd03315 122 LREAVGdDAELRVDANRGWTPKQAIRALRALEDL---GLDYVEQPLPADDleGRAALARATDTPIMADESAFTPHdaFRE 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355064373 225 TAEPGLRAVIIKPTLTGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPG 289
Cdd:cd03315 199 LALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPG 263
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
4-284 |
7.74e-24 |
|
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: 97.40 E-value: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 4 AQLYRYQVPMDAGVVLRERRLKTRDGLLVRLS-DNGREGWGDiaplpgfsdetldaalsaardwlrawqrgdaqplpeva 82
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTtDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 83 sVAFGLSMAQAELHGTlpvaanyhtaplctgdpdELFARLAGLTGKKVAKvkvgLYEAVRDGMVVNLLLEAIP-DLTLRL 161
Cdd:cd00308 43 -VISGIDMALWDLAAK------------------ALGVPLAELLGGGSRD----RVPAYGSIERVRAVREAFGpDARLAV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 162 DANRAWTPLKAQQFAKYVNPayrSRIEFIEEPCKTPD--DSRAFAAETGIAIAWDESLRERDF--SITAEPGLRAVIIKP 237
Cdd:cd00308 100 DANGAWTPKEAIRLIRALEK---YGLAWIEEPCAPDDleGYAALRRRTGIPIAADESVTTVDDalEALELGAVDILQIKP 176
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1355064373 238 TLTGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTP 284
Cdd:cd00308 177 TRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPN 223
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-303 |
1.73e-20 |
|
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: 90.65 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 1 MRAAQLYRYQVPMDAGVVLRERRLKTRDGLLVRL-SDNGREGWGDIAPLPGFSDETLDAALSAARDWL---------RAW 70
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVeTDDGITGWGEAVPGGTGAEAVAAALEEALAPLLigrdpldieALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 71 QRGDAQpLPEVASVAFGLSMA----QAELHGtLPVAA----NYHTAPLC-----TGDPDELFARLAGL--TGKKVAKVKV 135
Cdd:COG4948 83 QRLYRA-LPGNPAAKAAVDMAlwdlLGKALG-VPVYQllggKVRDRVPVyatlgIDTPEEMAEEAREAvaRGFRALKLKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 136 GLYEAVRDGMVVNLLLEAI-PDLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPDDS--RAFAAETGIAIA 212
Cdd:COG4948 161 GGPDPEEDVERVRAVREAVgPDARLRVDANGAWTLEEAIRLLRALEDL---GLEWIEQPLPAEDLEglAELRRATPVPIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 213 WDESLRER-DF-SITAEPGLRAVIIKPTLTGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWLTPGVTPGL 290
Cdd:COG4948 238 ADESLTSRaDFrRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFDIVEL 317
|
330
....*....|...
gi 1355064373 291 DTLALMQAQLVRP 303
Cdd:COG4948 318 DGPLLLADDLVED 330
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
27-282 |
1.16e-18 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 86.83 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 27 RDGLLVRLS-DNGREGWGDIAPLPGFSDETLD--------------AALSAARDWLRA------WQRGDAQPLPEVASVA 85
Cdd:PLN02980 961 REGFILSLSlEDGSVGFGEVAPLEIHEEDLLDveeqlrfllhvikgAKISFMLPLLKGsfsswiWSELGIPPSSIFPSVR 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 86 FGLSMA----QAELHGT--LPVAANY----------HTAPLC-----TGDPDE--LFARLAGLTGKKVAKVKVGLYEA-V 141
Cdd:PLN02980 1041 CGLEMAilnaIAVRHGSslLNILDPYqkdengseqsHSVQICalldsNGSPLEvaYVARKLVEEGFSAIKLKVGRRVSpI 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 142 RDGMVVNLLLEAIP-DLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRE- 219
Cdd:PLN02980 1121 QDAAVIQEVRKAVGyQIELRADANRNWTYEEAIEFGSLVKSC---NLKYIEEPVQDEDDLIKFCEETGLPVALDETIDKf 1197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355064373 220 -----RDFSITAEPGLRAVIIKPTLTGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAWL 282
Cdd:PLN02980 1198 eecplRMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYIQFASYL 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 ... |
3-220 |
1.80e-15 |
|
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: 75.69 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 3 AAQLYRYQVPMDAGVVLRERRLKTRDGLLVRLSDNGREGWGDIAPLPGFSDETLDAALSAARDWLRAWQRGDAQP----- 77
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGYGEAAPTPRVTGETVESVLAALKSVRPALIGGDPRLeklle 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 78 -----LPEVASVAFGLSMA----QAELHGtLPVAA---NYHTAPLCT------GDPDE--LFARLAGLTGKKVAKVKVGL 137
Cdd:cd03319 81 alqelLPGNGAARAAVDIAlwdlEAKLLG-LPLYQlwgGGAPRPLETdytisiDTPEAmaAAAKKAAKRGFPLLKIKLGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 138 Y--------EAVRdgmvvnlllEAIPDLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPDDS--RAFAAET 207
Cdd:cd03319 160 DleddieriRAIR---------EAAPDARLRVDANQGWTPEEAVELLRELAEL---GVELIEQPVPAGDDDglAYLRDKS 227
|
250
....*....|...
gi 1355064373 208 GIAIAWDESLRER 220
Cdd:cd03319 228 PLPIMADESCFSA 240
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
5-282 |
2.89e-15 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 75.05 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 5 QLYRYQVPMDAGVVLRERRLKTRDGLLVRLSD-NGREGWGDIAPLPGFSDETLDAALSAARDWlrawqrgdaQPLPEVAS 83
Cdd:PRK02714 6 AFRPYQRPFRQPLQTAHGLWRIREGIILRLTDeTGKIGWGEIAPLPWFGSETLEEALAFCQQL---------PGEITPEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 84 VA----------FGLSMAQA-ELHGTLPVAAN--YHTAPLCTGDPDELFARLAGLTGKKVAKVKVGLYEAVRDGMVVNLL 150
Cdd:PRK02714 77 IFsipdalpacqFGFESALEnESGSRSNVTLNplSYSALLPAGEAALQQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 151 LEAIP-DLTLRLDANRAWTPLKAQQFAKYVNPAYRSRIEFIEEPCkTPDD-------SRAFAAetgiAIAWDES---LRE 219
Cdd:PRK02714 157 LERLPaGAKLRLDANGGLSLEEAKRWLQLCDRRLSGKIEFIEQPL-PPDQfdemlqlSQDYQT----PIALDESvanLAQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355064373 220 RDFSITAepGLRAV-IIKPTLTGSlqtvqqqVAQAHAQCLT----AVISSSIESSLGLTQLARLAAWL 282
Cdd:PRK02714 232 LQQCYQQ--GWRGIfVIKPAIAGS-------PSRLRQFCQQhpldAVFSSVFETAIGRKAALALAAEL 290
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
9-303 |
3.02e-12 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 66.14 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 9 YQVPMDagvvLRERRLKTRDGLLVRlsdnGREGWGDIAPLPGFSDETldaalsaARDWLRAWQRGDAQPLPEVasvafgl 88
Cdd:PRK02901 17 VALPMR----VRFRGITVREAVLIE----GPAGWGEFSPFLEYDPAE-------AAAWLASAIEAAYGGPPPP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 89 smaqaeLHGTLPVAAnyhTAPLCtgDPDELFARLAGLTGKKVAKVKVG-----------LYEAVRDGMVvnllleaiPDL 157
Cdd:PRK02901 75 ------VRDRVPVNA---TVPAV--DAAQVPEVLARFPGCRTAKVKVAepgqtladdvaRVNAVRDALG--------PDG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 158 TLRLDANRAWTPLKAQQFAKYVNPAyrSRIEFIEEPCKTPDDSRAFAAETGIAIAWDESLRErdfsitAEPGLRAV---- 233
Cdd:PRK02901 136 RVRVDANGGWSVDEAVAAARALDAD--GPLEYVEQPCATVEELAELRRRVGVPIAADESIRR------AEDPLRVAraga 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355064373 234 ----IIKPTLTGSLQTVQQQVAQAHaqcLTAVISSSIESSLGLTQLARLAAWLtPGVTP--GLDTLALMQAQLVRP 303
Cdd:PRK02901 208 advaVLKVAPLGGVRAALDIAEQIG---LPVVVSSALDTSVGIAAGLALAAAL-PELDHacGLATGGLFEEDVADP 279
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
117-209 |
8.74e-11 |
|
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: 57.68 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 117 ELFARLAGLTGKKVAKVKVGLYEAvRDGMVVNLLLEAI-PDLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCK 195
Cdd:smart00922 6 EAARRAVAEAGFRAVKVKVGGGPL-EDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDEL---GLEWIEEPVP 81
|
90
....*....|....*.
gi 1355064373 196 TPDDS--RAFAAETGI 209
Cdd:smart00922 82 PDDLEglAELRRATPI 97
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
129-220 |
5.98e-10 |
|
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: 58.35 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 129 KVAKVKVGLYEAVRDGMVVNLLLEAI-PDLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKTPDDS--RAFAA 205
Cdd:pfam13378 16 RAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEEL---GLLWIEEPVPPDDLEglARLRR 92
|
90
....*....|....*
gi 1355064373 206 ETGIAIAWDESLRER 220
Cdd:pfam13378 93 ATPVPIATGESLYSR 107
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
26-220 |
1.93e-06 |
|
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: 48.76 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 26 TRDGLLVRL-SDNGREGWGDIAPlpGFSDETLDAALSA----------ARDWLRAWQR-----GDAQPLPEVASVAFGLS 89
Cdd:cd03316 23 WRNLVLVRVtTDDGITGWGEAYP--GGRPSAVAAAIEDllaplligrdPLDIERLWEKlyrrlFWRGRGGVAMAAISAVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 90 MA----QAELHGtLPVAA-----------NYHTAPLCTGDPDELFARLAGL--TGKKVAKVKVGLYEAV-----RDGMVV 147
Cdd:cd03316 101 IAlwdiKGKAAG-VPVYKllggkvrdrvrVYASGGGYDDSPEELAEEAKRAvaEGFTAVKLKVGGPDSGgedlrEDLARV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355064373 148 NLLLEAI-PDLTLRLDANRAWTPLKAQQFAKYVNPAyrsRIEFIEEPCKT--PDDSRAFAAETGIAIAWDESLRER 220
Cdd:cd03316 180 RAVREAVgPDVDLMVDANGRWDLAEAIRLARALEEY---DLFWFEEPVPPddLEGLARLRQATSVPIAAGENLYTR 252
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
150-215 |
8.84e-05 |
|
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: 43.85 E-value: 8.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355064373 150 LLEAIPDLTLRLDANRAWTPLKAQQFAKYVnpayRSRIEFIEEPCKTPDDSRAFAAETG-------IAIAWDE 215
Cdd:cd03323 207 LAEAFPGARLRLDPNGAWSLETAIRLAKEL----EGVLAYLEDPCGGREGMAEFRRATGlplatnmIVTDFRQ 275
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
30-289 |
8.95e-04 |
|
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: 40.76 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 30 LLVRL-SDNGREGWGDIAPL--PGFSDETLDAALSAARDWLR-------AWQRGDAqpLPEVASVAFG-------LSMA- 91
Cdd:cd03318 31 VLVRLtTSDGVVGIGEATTPggPAWGGESPETIKAIIDRYLAplligrdATNIGAA--MALLDRAVAGnlfakaaIEMAl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 92 ---QAELHG-------------TLPVAAnyhtaPLCTGDPDELFARLAGL--TGKKVA-KVKVGLYEAVRDGMVVNLLLE 152
Cdd:cd03318 109 ldaQGRRLGlpvsellggrvrdSLPVAW-----TLASGDTERDIAEAEEMleAGRHRRfKLKMGARPPADDLAHVEAIAK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 153 AIPD-LTLRLDANRAWTPLKAqqfAKYVNPAYRSRIEFIEEPckTPDDSRA----FAAETGIAIAWDESL--RERDFSIT 225
Cdd:cd03318 184 ALGDrASVRVDVNQAWDESTA---IRALPRLEAAGVELIEQP--VPRENLDglarLRSRNRVPIMADESVsgPADAFELA 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1355064373 226 AEPGLRAVIIKPTLTGSLQTVQQQVAQAHAQCLTAVISSSIESSLGLTQLARLAAwLTPGVTPG 289
Cdd:cd03318 259 RRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFA-TLPSLPFG 321
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
105-199 |
3.88e-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: 38.86 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355064373 105 YHTAPLCTGDPDElfaRLAGLTGKKVA------KVKVG--LYEAVRDgmvVNLLLEAI-PDLTLRLDANRAWtplKAQQF 175
Cdd:cd03324 186 YTTSAGWLGYSDE---KLRRLCKEALAqgfthfKLKVGadLEDDIRR---CRLAREVIgPDNKLMIDANQRW---DVPEA 256
|
90 100
....*....|....*....|....
gi 1355064373 176 AKYVNPAYRSRIEFIEEPcKTPDD 199
Cdd:cd03324 257 IEWVKQLAEFKPWWIEEP-TSPDD 279
|
|
| |
