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MENC_YERPY
ID   MENC_YERPY              Reviewed;         323 AA.
AC   B1JH91;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=YPK_1592;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA67885.1; -; Genomic_DNA.
DR   RefSeq; WP_012303942.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JH91; -.
DR   SMR; B1JH91; -.
DR   PRIDE; B1JH91; -.
DR   EnsemblBacteria; ACA67885; ACA67885; YPK_1592.
DR   KEGG; ypy:YPK_1592; -.
DR   PATRIC; fig|502800.11.peg.2239; -.
DR   OMA; YEANRDG; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
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_1000125590"
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;  35298 MW;  5386C053CD316584 CRC64;
     MRTATLYRYS VPMEAGVILR HQRLKSRDGL LVKLQQGELS GWGEIAPLPE FSQETLDQAQ
     VAAECWLQHW VSGVESDDSV LPSVAFGLSC AQAELKQTLP LSADYRKAPL CTGDPDELFA
     VLQALPGEKV AKVKVGLYEA VRDGMIVNVL LEALPDLTLR LDANRSWSRA KADGFAKYVN
     PALRSRIAFL EEPCKTRAES REFARDTGIA IAWDESVREA DFQVEAEPGV AAIVIKPTLV
     GSLARCQQLV QQAHQAGLVA VISSSIESSL GLTQLARLAA WLTPATVPGL DTLDLMQAQV
     VRPWPDSPLP LITTEQLGVV WHR
 
 
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