ID   MENC_YERP3              Reviewed;         323 AA.
AC   A7FGT5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=YpsIP31758_1485;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS47810.1; -; Genomic_DNA.
DR   RefSeq; WP_012104916.1; NC_009708.1.
DR   AlphaFoldDB; A7FGT5; -.
DR   SMR; A7FGT5; -.
DR   EnsemblBacteria; ABS47810; ABS47810; YpsIP31758_1485.
DR   KEGG; ypi:YpsIP31758_1485; -.
DR   HOGENOM; CLU_030273_0_1_6; -.
DR   OMA; YEANRDG; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000002412; 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..323
FT                   /note="o-succinylbenzoate synthase"
FT                   /id="PRO_1000060379"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   ACT_SITE        236
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
SQ   SEQUENCE   323 AA;  35271 MW;  98F947AA6AB5329D CRC64;
     MRTATLYRYS VPMEAGVILR HQRLKSRDGL LVKLQQGELS GWGEIAPLPE FSQETLDQAQ
     VAAECWLQHW VSGVESDDSV LPSVAFGLSC AQAELNQTLP LSADYRKAPL CTGDPDELFA
     VLQALPGEKV AKVKVGLYEA VRDGMIVNVL LEALPDLTLR LDANRSWSRA KADGFAKYVN
     PALRSRIAFL EEPCKTRAES REFAQDTGIA IAWDESVREA DFQVEAEPGV AAIVIKPTLV
     GSLSRCQQLV QQAHQAGLVA VISSSIESSL GLTQLARLAA WLTPATVPGL DTLDLMQAQV
     VRPWPDSPLP LITTEQLGVV WHR