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MENC_ECOL5
ID   MENC_ECOL5              Reviewed;         320 AA.
AC   Q0TFI0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE            Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE            Short=OSBS {ECO:0000255|HAMAP-Rule:MF_00470};
DE            EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_00470};
DE   AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE   AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00470};
GN   Name=menC {ECO:0000255|HAMAP-Rule:MF_00470}; OrderedLocusNames=ECP_2305;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC       carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000255|HAMAP-
CC       Rule:MF_00470}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate
CC         = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00470};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00470};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
CC       {ECO:0000255|HAMAP-Rule:MF_00470}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00470}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. MenC type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00470}.
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DR   EMBL; CP000247; ABG70299.1; -; Genomic_DNA.
DR   RefSeq; WP_001255594.1; NC_008253.1.
DR   AlphaFoldDB; Q0TFI0; -.
DR   SMR; Q0TFI0; -.
DR   STRING; 362663.ECP_2305; -.
DR   EnsemblBacteria; ABG70299; ABG70299; ECP_2305.
DR   KEGG; ecp:ECP_2305; -.
DR   HOGENOM; CLU_030273_0_1_6; -.
DR   OMA; YEANRDG; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000009182; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   HAMAP; MF_00470; MenC_1; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR010196; OSB_synthase_MenC1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding.
FT   CHAIN           1..320
FT                   /note="o-succinylbenzoate synthase"
FT                   /id="PRO_1000013799"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
SQ   SEQUENCE   320 AA;  35523 MW;  E8C3FB5C1B04FB80 CRC64;
     MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLREGERE GWGEISPLPG FSQETWEDAQ
     SVLLAWVNNW LAGDCELPQM PSVAFGVSCA LAELAETLPQ AANYRAAPLC NGDPDDLILK
     LADMPGEKVA KVKVGLYEAV RDGMVVNLLL EAIPDLHLRL DANRAWTPLK GQQFAKYVNP
     DYRHRIAFLE EPCKTRDDSR AFARETDIAI AWDESLREPD FAFVAEEGVR AVVIKPTLTG
     SLEKVREQVK AAHALGLTAV ISSSIESSLG LTQLARIAAW LTPDTIPGLD TLDLMQAQQV
     RRWPGSPLPL VDVDALERLL
 
 
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