|
Name |
Accession |
Description |
Interval |
E-value |
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
4-316 |
1.10e-90 |
|
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: 271.83 E-value: 1.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 4 INIIPRVLHFKQPAGTSRGSYTTRNVWYIHLSSIEcpGRVGVGECAPLPklscddlpdyeqvlrsacqrleqtgeldies 83
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLT--GPVGWGEIAPLP------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 84 lrgypsILFGLETALRHYETQSWalwdtPFSRGEAGIPINGLIWMGSFDRMlQQIEVKMQAGYRCIKLKIGAINFEEELA 163
Cdd:cd03320 48 ------LAFGIESALANLEALLV-----GFTRPRNRIPVNALLPAGDAAAL-GEAKAAYGGGYRTVKLKVGATSFEEDLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 164 LLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAesPLPIALDEELIGCNALE 243
Cdd:cd03320 116 RLRALREALPA-DAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAA--GVPIALDESLRRLDDPL 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492344807 244 RkreLLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQWCATF-RNPLPQGLGT 316
Cdd:cd03320 193 A---LAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALpPLPAACGLGT 263
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
4-324 |
1.66e-57 |
|
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: 190.03 E-value: 1.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 4 INIIPRVLHFKQPAGTSRGSYTTRNVWYIHLSSIEcpGRVGVGECAPLPklsCDDLPDYEQVLRSACQRLEQTGELDIE- 82
Cdd:COG4948 6 IEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDD--GITGWGEAVPGG---TGAEAVAAALEEALAPLLIGRDPLDIEa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 83 -------SLRGYPSILFGLETAL-----RHYETQSWALWDTPFSRGeagIPINGLIWMGSFDRMLQQIEVKMQAGYRCIK 150
Cdd:COG4948 81 lwqrlyrALPGNPAAKAAVDMALwdllgKALGVPVYQLLGGKVRDR---VPVYATLGIDTPEEMAEEAREAVARGFRALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 151 LKIGAINFEEELALLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPI 230
Cdd:COG4948 158 LKVGGPDPEEDVERVRAVREAVGP-DARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 231 ALDEELIGCNALerkRELLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQWCATFRNPL 310
Cdd:COG4948 237 AADESLTSRADF---RRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFD 313
|
330
....*....|....
gi 492344807 311 PQGLGTGLLFTDNV 324
Cdd:COG4948 314 IVELDGPLLLADDL 327
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
12-325 |
1.81e-31 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 120.50 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 12 HFKQPAGTSRGSYTTRNVWYIHLSSIEcpGRVGVGECAPLPKLSCDDLpdyEQVLrSACQRLEqtGELDIESLRG----Y 87
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDET--GKIGWGEIAPLPWFGSETL---EEAL-AFCQQLP--GEITPEQIFSipdaL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 88 PSILFGLETALRhYETQSWAlwdtpfSRGEAGIPINGLIWMGSfdRMLQQIEVKMQAGYRCIKLKIGAINFEEELALLRH 167
Cdd:PRK02714 85 PACQFGFESALE-NESGSRS------NVTLNPLSYSALLPAGE--AALQQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 168 IRAHYSAReIELRVDANGAFSPADA---MDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEELIGCNALER 244
Cdd:PRK02714 156 LLERLPAG-AKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVANLAQLQQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 245 kreLLAAIHPRYIILKPSLHGGISGGNEWIaeaeKQH-IGWWITSALESNIGLNAIAQWCATF-RNPLPQGLGTGLLFTD 322
Cdd:PRK02714 235 ---CYQQGWRGIFVIKPAIAGSPSRLRQFC----QQHpLDAVFSSVFETAIGRKAALALAAELsRPDRALGFGVTHWFSD 307
|
...
gi 492344807 323 NVE 325
Cdd:PRK02714 308 EEE 310
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
13-325 |
7.01e-30 |
|
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: 115.67 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 13 FKQPAGTSRGSYTTRNVWYIHLSSiecPGRVGVGECAPLPKLSCDDLPDYEQVLRSACQRLEQtgeLDIESLRG-YPSIL 91
Cdd:TIGR01927 7 FDAPVVTRHGLLARREGLIVRLTD---EGRTGWGEIAPLPGFGTETLAEALDFCRALIEEITR---GDIEAIDDqLPSVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 92 FGLETALRHYE-----TQSWALWDTPFSRGEAGIPINGLIWMgsfdrmlqqievkmqAGYRCIKLKIGAINFEEELALLR 166
Cdd:TIGR01927 81 FGFESALIELEsgdelPPASNYYVALLPAGDPALLLLRSAKA---------------EGFRTFKWKVGVGELAREGMLVN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 167 HIRAHYSAReIELRVDANGAFSPADA---MDKLNRLAELDLHSIEQPIRAGqwEEMARLAAESPLPIALDEeligcnALE 243
Cdd:TIGR01927 146 LLLEALPDK-AELRLDANGGLSPDEAqqfLKALDPNLRGRIAFLEEPLPDA--DEMSAFSEATGTAIALDE------SLW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 244 RKRELLAAIHPRY---IILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQWCATF-RNPLPQGLGTGLL 319
Cdd:TIGR01927 217 ELPQLADEYGPGWrgaLVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLsPDPAAVGFTTALL 296
|
....*.
gi 492344807 320 FTDNVE 325
Cdd:TIGR01927 297 RAQDLE 302
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
143-331 |
3.41e-29 |
|
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: 111.50 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 143 QAGYRCIKLKIGAINFEEELALLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARL 222
Cdd:pfam13378 12 ARGFRAFKLKVGGPDPEEDVERVRAVREAVGP-GVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 223 AAESPLPIALDEELIGcnaLERKRELLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESnIGLNAIAQW 302
Cdd:pfam13378 91 RRATPVPIATGESLYS---REDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP-IGLAASLHL 166
|
170 180 190
....*....|....*....|....*....|.
gi 492344807 303 CATFRNPLPQGLGTG--LLFTDNVEMPLEIR 331
Cdd:pfam13378 167 AAAVPNLLIQEYFLDplLLEDDLLTEPLEVE 197
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
132-228 |
2.66e-21 |
|
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: 86.95 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 132 DRMLQQIEVKMQA-GYRCIKLKIGAiNFEEELALLRHIRAHYsAREIELRVDANGAFSPADAMDKLNRLAELDLHSIEQP 210
Cdd:smart00922 2 EELAEAARRAVAEaGFRAVKVKVGG-GPLEDLARVAAVREAV-GPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 492344807 211 IRAGQWEEMARLAAESPL 228
Cdd:smart00922 80 VPPDDLEGLAELRRATPI 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
4-316 |
1.10e-90 |
|
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: 271.83 E-value: 1.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 4 INIIPRVLHFKQPAGTSRGSYTTRNVWYIHLSSIEcpGRVGVGECAPLPklscddlpdyeqvlrsacqrleqtgeldies 83
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLT--GPVGWGEIAPLP------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 84 lrgypsILFGLETALRHYETQSWalwdtPFSRGEAGIPINGLIWMGSFDRMlQQIEVKMQAGYRCIKLKIGAINFEEELA 163
Cdd:cd03320 48 ------LAFGIESALANLEALLV-----GFTRPRNRIPVNALLPAGDAAAL-GEAKAAYGGGYRTVKLKVGATSFEEDLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 164 LLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAesPLPIALDEELIGCNALE 243
Cdd:cd03320 116 RLRALREALPA-DAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAA--GVPIALDESLRRLDDPL 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492344807 244 RkreLLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQWCATF-RNPLPQGLGT 316
Cdd:cd03320 193 A---LAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALpPLPAACGLGT 263
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
4-324 |
1.66e-57 |
|
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: 190.03 E-value: 1.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 4 INIIPRVLHFKQPAGTSRGSYTTRNVWYIHLSSIEcpGRVGVGECAPLPklsCDDLPDYEQVLRSACQRLEQTGELDIE- 82
Cdd:COG4948 6 IEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDD--GITGWGEAVPGG---TGAEAVAAALEEALAPLLIGRDPLDIEa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 83 -------SLRGYPSILFGLETAL-----RHYETQSWALWDTPFSRGeagIPINGLIWMGSFDRMLQQIEVKMQAGYRCIK 150
Cdd:COG4948 81 lwqrlyrALPGNPAAKAAVDMALwdllgKALGVPVYQLLGGKVRDR---VPVYATLGIDTPEEMAEEAREAVARGFRALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 151 LKIGAINFEEELALLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPI 230
Cdd:COG4948 158 LKVGGPDPEEDVERVRAVREAVGP-DARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 231 ALDEELIGCNALerkRELLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQWCATFRNPL 310
Cdd:COG4948 237 AADESLTSRADF---RRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFD 313
|
330
....*....|....
gi 492344807 311 PQGLGTGLLFTDNV 324
Cdd:COG4948 314 IVELDGPLLLADDL 327
|
|
| 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 ... |
3-302 |
6.41e-37 |
|
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: 135.01 E-value: 6.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 3 TINIIPRVLHFKQPAGTSRGSYTTRNVWYIhlsSIECPGRVGVGECAPLPKLSCDDLPDYEQVLRSACQRLEQTGELDI- 81
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIV---EIELDGITGYGEAAPTPRVTGETVESVLAALKSVRPALIGGDPRLEk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 82 ------ESLRGYPSILFGLETALRHYETQSWA--LWDTPFSRGEAGIPINGLIWMGSFDRMLQQIEVKMQAGYRCIKLKI 153
Cdd:cd03319 78 llealqELLPGNGAARAAVDIALWDLEAKLLGlpLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 154 GAiNFEEELALLRHIRAHysAREIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALD 233
Cdd:cd03319 158 GG-DLEDDIERIRAIREA--APDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMAD 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492344807 234 EELIGCNALERKRELLAAihpRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQW 302
Cdd:cd03319 235 ESCFSAADAARLAGGGAY---DGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHL 300
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
12-325 |
1.81e-31 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 120.50 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 12 HFKQPAGTSRGSYTTRNVWYIHLSSIEcpGRVGVGECAPLPKLSCDDLpdyEQVLrSACQRLEqtGELDIESLRG----Y 87
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDET--GKIGWGEIAPLPWFGSETL---EEAL-AFCQQLP--GEITPEQIFSipdaL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 88 PSILFGLETALRhYETQSWAlwdtpfSRGEAGIPINGLIWMGSfdRMLQQIEVKMQAGYRCIKLKIGAINFEEELALLRH 167
Cdd:PRK02714 85 PACQFGFESALE-NESGSRS------NVTLNPLSYSALLPAGE--AALQQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 168 IRAHYSAReIELRVDANGAFSPADA---MDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEELIGCNALER 244
Cdd:PRK02714 156 LLERLPAG-AKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVANLAQLQQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 245 kreLLAAIHPRYIILKPSLHGGISGGNEWIaeaeKQH-IGWWITSALESNIGLNAIAQWCATF-RNPLPQGLGTGLLFTD 322
Cdd:PRK02714 235 ---CYQQGWRGIFVIKPAIAGSPSRLRQFC----QQHpLDAVFSSVFETAIGRKAALALAAELsRPDRALGFGVTHWFSD 307
|
...
gi 492344807 323 NVE 325
Cdd:PRK02714 308 EEE 310
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
13-325 |
7.01e-30 |
|
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: 115.67 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 13 FKQPAGTSRGSYTTRNVWYIHLSSiecPGRVGVGECAPLPKLSCDDLPDYEQVLRSACQRLEQtgeLDIESLRG-YPSIL 91
Cdd:TIGR01927 7 FDAPVVTRHGLLARREGLIVRLTD---EGRTGWGEIAPLPGFGTETLAEALDFCRALIEEITR---GDIEAIDDqLPSVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 92 FGLETALRHYE-----TQSWALWDTPFSRGEAGIPINGLIWMgsfdrmlqqievkmqAGYRCIKLKIGAINFEEELALLR 166
Cdd:TIGR01927 81 FGFESALIELEsgdelPPASNYYVALLPAGDPALLLLRSAKA---------------EGFRTFKWKVGVGELAREGMLVN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 167 HIRAHYSAReIELRVDANGAFSPADA---MDKLNRLAELDLHSIEQPIRAGqwEEMARLAAESPLPIALDEeligcnALE 243
Cdd:TIGR01927 146 LLLEALPDK-AELRLDANGGLSPDEAqqfLKALDPNLRGRIAFLEEPLPDA--DEMSAFSEATGTAIALDE------SLW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 244 RKRELLAAIHPRY---IILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQWCATF-RNPLPQGLGTGLL 319
Cdd:TIGR01927 217 ELPQLADEYGPGWrgaLVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLsPDPAAVGFTTALL 296
|
....*.
gi 492344807 320 FTDNVE 325
Cdd:TIGR01927 297 RAQDLE 302
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
143-331 |
3.41e-29 |
|
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: 111.50 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 143 QAGYRCIKLKIGAINFEEELALLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARL 222
Cdd:pfam13378 12 ARGFRAFKLKVGGPDPEEDVERVRAVREAVGP-GVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 223 AAESPLPIALDEELIGcnaLERKRELLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESnIGLNAIAQW 302
Cdd:pfam13378 91 RRATPVPIATGESLYS---REDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP-IGLAASLHL 166
|
170 180 190
....*....|....*....|....*....|.
gi 492344807 303 CATFRNPLPQGLGTG--LLFTDNVEMPLEIR 331
Cdd:pfam13378 167 AAAVPNLLIQEYFLDplLLEDDLLTEPLEVE 197
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
4-295 |
2.42e-28 |
|
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: 112.71 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 4 INIIPRVLHFKQPAGTSRGSYTTRNVWYIHLSSIEcpGRVGVGECA--PLPKLSCDDLPDYEQVLRS-ACQRLEQTGELD 80
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEE--GITGYGEVVafEGPFYTEETNATAWHILKDyLLPLLLGREFSH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 81 IESL-------RGYPSILFGLETALrhyetqsWALW----DTPFSRG--------EAGIPInGLiwMGSFDRMLQQIEVK 141
Cdd:cd03317 79 PEEVserlapiKGNNMAKAGLEMAV-------WDLYakaqGQSLAQYlggtrdsiPVGVSI-GI--QDDVEQLLKQIERY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 142 MQAGYRCIKLKIGAinfEEELALLRHIRAHYSarEIELRVDANGAFSPADAmDKLNRLAELDLHSIEQPIRAGQWEEMAR 221
Cdd:cd03317 149 LEEGYKRIKLKIKP---GWDVEPLKAVRERFP--DIPLMADANSAYTLADI-PLLKRLDEYGLLMIEQPLAADDLIDHAE 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492344807 222 LAAESPLPIALDEELIGCNALERKRELLAAihpRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIG 295
Cdd:cd03317 223 LQKLLKTPICLDESIQSAEDARKAIELGAC---KIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIG 293
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
25-327 |
1.28e-27 |
|
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: 109.97 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 25 TTRNVWYIHLSsieCPGRVGVGECAPLPKLSCDDLPDYEQVLRSACQRLEQTGELDIESLrgYPSILFGLETALrhYETQ 104
Cdd:COG1441 25 KTRDGLLVRLQ---EGGREGWGEIAPLPGFSQETLEQAEQQALAWLQRWLAGDLLDEKSL--LPSVAFGLSCAL--AELE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 105 SwalwDTPFsrgEAGIPINGLIWmGSFD---RMLQQIEvkmqaGYRCIKLKIGAINFEEELALLRHIRAHYSarEIELRV 181
Cdd:COG1441 98 G----ELPE---AANYRAAPLCS-GDPDeliARLNQMP-----GEKVAKVKVGLYEAVRDGMVVNLLLEAIP--DLRLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 182 DANGAFSPADAM---DKLNRLAELDLHSIEQPIRAGqwEEMARLAAESPLPIALDEELIGCNALERKRELLAAihpryII 258
Cdd:COG1441 163 DANRSWTLDKAVqfaKYVNPEHRSRIAFLEEPCKTP--EESREFARETGIAIAWDESVREPDFRVEAEPGVAA-----IV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492344807 259 LKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLN---AIAQWCATfrnPLPQGLGTGLLFTDNVEMP 327
Cdd:COG1441 236 IKPTLVGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTqlaRLAAWLTP---DTAPGLDTLDLMQAQLLRP 304
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
11-295 |
2.27e-25 |
|
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: 103.77 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 11 LHFKQPAGTSRGSYTTRNVWYIHLssIECPGRVGVGECAPLPklscddLPDY-EQVLRSACQRLEQTGELDI-------- 81
Cdd:TIGR01928 5 EPFKSPFKTSKGTLNHRDCLIIEL--IDDKGNAGFGEVVAFQ------TPWYtHETIATVKHIIEDFFEPNInkefehps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 82 ---ESLRGY---PSILFGLETALRHYETQswaLWDTPFSRGEAG----IPINGLIWMGSFDRMLQQIEVKMQAGYRCIKL 151
Cdd:TIGR01928 77 ealELVRSLkgtPMAKAGLEMALWDMYHK---LPSFSLAYGQGKlrdkAPAGAVSGLANDEQMLKQIESLKATGYKRIKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 152 KIgAINFEEELALLRHIRAHysarEIELRVDANGAFSPADaMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIA 231
Cdd:TIGR01928 154 KI-TPQIMHQLVKLRRLRFP----QIPLVIDANESYDLQD-FPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPIC 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492344807 232 LDEELIGCNALERKRELLAAihpRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIG 295
Cdd:TIGR01928 228 LDESITSLDDARNLIELGNV---KVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGIS 288
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
120-337 |
1.37e-23 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 99.70 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 120 IPINGLIWMGSFDRMLQQIEVKMQAG-YRCIKLKIGAINFEEELALLRHIRAHYSAReIELRVDANGAFSPADAMDKLNR 198
Cdd:cd03318 132 LPVAWTLASGDTERDIAEAEEMLEAGrHRRFKLKMGARPPADDLAHVEAIAKALGDR-ASVRVDVNQAWDESTAIRALPR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 199 LAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEELIG-CNALERKRELLAAIhpryIILKPSLHGGISGGNEWIAEA 277
Cdd:cd03318 211 LEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGpADAFELARRGAADV----FSLKIAKSGGLRRAQKVAAIA 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492344807 278 EKQHIGWWITSALESNIGLNAIAQWCATFRNpLPQG---LGTGLLFTDNVEMPLEIRKDCLWF 337
Cdd:cd03318 287 EAAGIALYGGTMLESSIGTAASAHLFATLPS-LPFGcelFGPLLLAEDLLEEPLAYRDGELHV 348
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
92-309 |
1.70e-22 |
|
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: 94.72 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 92 FGLETALrhyetqsWALWDTpfSRGE----------AGIPINGLIWMGSFDRMLQQIEVKMQAGYRCIKLKIGAiNFEEE 161
Cdd:cd03315 46 AAVDMAL-------WDLWGK--RLGVpvylllggyrDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGR-DPARD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 162 LALLRHIRAHYsAREIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEeliGCNA 241
Cdd:cd03315 116 VAVVAALREAV-GDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADE---SAFT 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492344807 242 LERKRELLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNA---IAQWCATFRNP 309
Cdd:cd03315 192 PHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLAnahLAAALRAVTLP 262
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
132-228 |
2.66e-21 |
|
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: 86.95 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 132 DRMLQQIEVKMQA-GYRCIKLKIGAiNFEEELALLRHIRAHYsAREIELRVDANGAFSPADAMDKLNRLAELDLHSIEQP 210
Cdd:smart00922 2 EELAEAARRAVAEaGFRAVKVKVGG-GPLEDLARVAAVREAV-GPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 492344807 211 IRAGQWEEMARLAAESPL 228
Cdd:smart00922 80 VPPDDLEGLAELRRATPI 97
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
163-314 |
9.88e-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: 80.83 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 163 ALLRHIRAHYSA--REIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEEligCN 240
Cdd:cd00308 79 GSIERVRAVREAfgPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADES---VT 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492344807 241 ALERKRELLAAIHPRYIILKPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNAIAQWCATFRNPLPQGL 314
Cdd:cd00308 156 TVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPNDRAIET 229
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
107-308 |
1.13e-17 |
|
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: 82.66 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 107 ALWDTpfsRG-EAGIPI----------------NGLIWMGSFDRMLQQIEVKMQAGYRCIKLKIGAIN-----FEEELAL 164
Cdd:cd03316 102 ALWDI---KGkAAGVPVykllggkvrdrvrvyaSGGGYDDSPEELAEEAKRAVAEGFTAVKLKVGGPDsggedLREDLAR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 165 LRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEELIGcnaler 244
Cdd:cd03316 179 VRAVREAVGP-DVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYT------ 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492344807 245 KRELLAAIHPRYI-ILKPSLH--GGISGGNEWIAEAEKQHIgWWITSALESNIGLNAIAQWCATFRN 308
Cdd:cd03316 252 RWEFRDLLEAGAVdIIQPDVTkvGGITEAKKIAALAEAHGV-RVAPHGAGGPIGLAASLHLAAALPN 317
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
25-302 |
4.28e-16 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 77.57 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 25 TTRNVWYIHLssiECPGRVGVGECAPLPKLSCDDLPDYEQVLRSACQRLEQTGELDIESLrgYPSILFGLETAlrHYEtq 104
Cdd:PRK05105 25 KTRDGLVVQL---REGEREGWGEIAPLPGFSQETLEEAQEALLAWLNNWLAGDCDDELSQ--YPSVAFGLSCA--LAE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 105 swaLWDT-PFSRGEAGIPingLIWmGSFDRMLQQIEvKMQaGYRCIKLKIGAINFEEELALLRHIRAhysAR-EIELRVD 182
Cdd:PRK05105 96 ---LAGTlPQAANYRTAP---LCY-GDPDELILKLA-DMP-GEKVAKVKVGLYEAVRDGMLVNLLLE---AIpDLKLRLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 183 ANGAFSPADAMDKLNRLAELDLHSI---EQPIRagQWEEMARLAAESPLPIALDEELIgcnalERKRELLAAIHPRYIIL 259
Cdd:PRK05105 164 ANRGWTLEKAQQFAKYVPPDYRHRIaflEEPCK--TPDDSRAFARATGIAIAWDESLR-----EPDFQFEAEPGVRAIVI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 492344807 260 KPSLHGGISGGNEWIAEAEKQHIGWWITSALESNIGLNA---IAQW 302
Cdd:PRK05105 237 KPTLTGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQlarLAAW 282
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
41-332 |
3.84e-14 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 73.74 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 41 GRVGVGECAPLpKLSCDDLPDYEQVLRSACQRLEQT------------------GELDIESLRGYPSILFGLETALRHY- 101
Cdd:PLN02980 973 GSVGFGEVAPL-EIHEEDLLDVEEQLRFLLHVIKGAkisfmlpllkgsfsswiwSELGIPPSSIFPSVRCGLEMAILNAi 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 102 -ETQSWALWD--TPFSRGEAGIPINGLIWM-GSFDRMLQQIEVK------MQAGYRCIKLKIGA-INFEEELALLRHIRa 170
Cdd:PLN02980 1052 aVRHGSSLLNilDPYQKDENGSEQSHSVQIcALLDSNGSPLEVAyvarklVEEGFSAIKLKVGRrVSPIQDAAVIQEVR- 1130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 171 HYSAREIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGqwEEMARLAAESPLPIALDEEL--IGCNALerkREL 248
Cdd:PLN02980 1131 KAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDE--DDLIKFCEETGLPVALDETIdkFEECPL---RML 1205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 249 LAAIHPRYI--ILKPSLHGGISGG---NEWIAEAEKQHIgwwITSALESNIGLNAIAQWCATF----------RN----- 308
Cdd:PLN02980 1206 TKYTHPGIVavVIKPSVVGGFENAaliARWAQQHGKMAV---ISAAYESGLGLSAYIQFASYLemqnakasreMNkgtcp 1282
|
330 340
....*....|....*....|....*
gi 492344807 309 PLPQGLGTGLLFTDNVEM-PLEIRK 332
Cdd:PLN02980 1283 SVAHGLGTYRWLKEDVTMnPLGIFR 1307
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
145-335 |
4.52e-11 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 63.06 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 145 GYRCIKLKIG--AINFEEELALLRHIRAHYSAREIeLRVDANGAFSPADAmdkLNRLAELD----LHSIEQPIRAgqWEE 218
Cdd:PRK02901 102 GCRTAKVKVAepGQTLADDVARVNAVRDALGPDGR-VRVDANGGWSVDEA---VAAARALDadgpLEYVEQPCAT--VEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 219 MARLAAESPLPIALDEELigcnaleRK-------RELLAAihpRYIILKPSLHGGISGGNEwIAEAEKqhIGWWITSALE 291
Cdd:PRK02901 176 LAELRRRVGVPIAADESI-------RRaedplrvARAGAA---DVAVLKVAPLGGVRAALD-IAEQIG--LPVVVSSALD 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492344807 292 SNIGLNA-IAQWCATFRNPLPQGLGTGLLFTDNVEMPLEIRKDCL 335
Cdd:PRK02901 243 TSVGIAAgLALAAALPELDHACGLATGGLFEEDVADPLLPVDGFL 287
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
145-274 |
3.10e-09 |
|
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: 57.49 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 145 GYRCIKLKIGAINFEEELALLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAA 224
Cdd:cd03321 156 GFHAVKTKIGYPTADEDLAVVRSIRQAVGD-GVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIAS 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 492344807 225 ESPLPIALDEELIGCNALerkRELLAAIHPRYIIlkPSLH--GGISGgneWI 274
Cdd:cd03321 235 ALRTPVQMGENWLGPEEM---FKALSAGACDLVM--PDLMkiGGVTG---WL 278
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
107-268 |
9.79e-08 |
|
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: 53.10 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 107 ALWDTpfsRGEA-GIPINGLI------------WMG--SFDRMLQQIEVKMQAGYRCIKLkigaiNFEEEL--------- 162
Cdd:cd03325 88 ALWDI---KGKVlGVPVHQLLggqvrdrvrvysWIGgdRPSDVAEAARARREAGFTAVKM-----NATEELqwidtskkv 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 163 -ALLRHIRAHYSAR--EIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEELIGC 239
Cdd:cd03325 160 dAAVERVAALREAVgpDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSR 239
|
170 180 190
....*....|....*....|....*....|..
gi 492344807 240 NALerkRELLAAihpRYI-ILKPSL-H-GGIS 268
Cdd:cd03325 240 WDF---KELLED---GAVdIIQPDIsHaGGIT 265
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
107-236 |
4.96e-06 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 47.97 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 107 ALWDTpfsRGEA-GIPINGLI------------WMGSfDR---MLQQIEVKMQAGYRCIKLkigaiNFEEELALLRHIRA 170
Cdd:PRK14017 89 ALWDI---KGKAlGVPVHELLgglvrdrirvysWIGG-DRpadVAEAARARVERGFTAVKM-----NGTEELQYIDSPRK 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492344807 171 HYSA-------RE-----IELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMARLAAESPLPIALDEEL 236
Cdd:PRK14017 160 VDAAvarvaavREavgpeIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERL 237
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
1-280 |
6.59e-06 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 47.05 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 1 MYTINIIPRVLHFKQPAGTSRGSYTTRNVWYIHLssiECPGRVGVGECAPLPKLSCDD----------LPDYEQVL-RSA 69
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVEL---EEEGIKGTGECTPYPRYGESDasvmaqimsvVPQLEKGLtREA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 70 CQRLEQTGEldieSLRGYPSILFGLETALRHyetQSwaLWDTPFSRGEAGIPINGLIWMGSFDRMLQQIEVKMQAGYRCI 149
Cdd:PRK15129 78 LQKLLPAGA----ARNAVDCALWDLAARQQQ---QS--LAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 150 KLKIGAINFEEELALLRHirahySAREIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGqwEEMARLAAESPLP 229
Cdd:PRK15129 149 KVKLDNHLISERMVAIRS-----AVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQ--DDAALENFIHPLP 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 492344807 230 IALDEEligCNAlerkRELLAAIHPRY--IILKPSLHGGISGGNEWIAEAEKQ 280
Cdd:PRK15129 222 ICADES---CHT----RSSLKALKGRYemVNIKLDKTGGLTEALALATEARAQ 267
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
107-211 |
6.23e-05 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239444 [Multi-domain] Cd Length: 352 Bit Score: 44.33 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 107 ALWD-----------TPFSRGEAGIPINGliwMGSF-----DRMLQQIEVKMQAGYRCIKLKIGAiNFEEELALLRHIRA 170
Cdd:cd03328 102 ALWDlkarllglplaRLLGRAHDSVPVYG---SGGFtsyddDRLREQLSGWVAQGIPRVKMKIGR-DPRRDPDRVAAARR 177
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 492344807 171 HYSArEIELRVDANGAFSPADAMDKLNRLAELDLHSIEQPI 211
Cdd:cd03328 178 AIGP-DAELFVDANGAYSRKQALALARAFADEGVTWFEEPV 217
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
145-236 |
9.50e-05 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. 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: 239442 [Multi-domain] Cd Length: 385 Bit Score: 43.92 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 145 GYRCIKLKIGAINFEEEL----ALLRHIRAhySAReieLRVDANGAFSPADAMDKLNRLAELDLHSIEQPIRAGQWEEMA 220
Cdd:cd03326 175 GYTVVKIKIGGAPLDEDLrrieAALDVLGD--GAR---LAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQA 249
|
90
....*....|....*.
gi 492344807 221 RLAAESPLPIALDEEL 236
Cdd:cd03326 250 ELADHYDGPIATGENL 265
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
127-210 |
1.18e-04 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239440 [Multi-domain] Cd Length: 415 Bit Score: 43.49 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 127 WMG-SFDRMLQQIEVKMQAGYRCIKLKIGAiNFEEELALLRHIRAHYSArEIELRVDANGAFSPADAMDKLNRLAELDLH 205
Cdd:cd03324 192 WLGySDEKLRRLCKEALAQGFTHFKLKVGA-DLEDDIRRCRLAREVIGP-DNKLMIDANQRWDVPEAIEWVKQLAEFKPW 269
|
....*
gi 492344807 206 SIEQP 210
Cdd:cd03324 270 WIEEP 274
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
145-231 |
1.96e-04 |
|
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: 42.69 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492344807 145 GYRCIKLKIGAINFEEELALLRHIRAHYSarEIELRVDANGAFSPADAMdKLNRLAELDLHSIEQPirAGQWEEMARLAA 224
Cdd:cd03323 184 GFKSFKLKGGVLPGEEEIEAVKALAEAFP--GARLRLDPNGAWSLETAI-RLAKELEGVLAYLEDP--CGGREGMAEFRR 258
|
....*..
gi 492344807 225 ESPLPIA 231
Cdd:cd03323 259 ATGLPLA 265
|
|
| |
