ID   MENC_MYCLE              Reviewed;         334 AA.
AC   Q9CBB2;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=ML2268;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583925; CAC31784.1; -; Genomic_DNA.
DR   PIR; H87192; H87192.
DR   RefSeq; NP_302476.1; NC_002677.1.
DR   RefSeq; WP_010908796.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBB2; -.
DR   SMR; Q9CBB2; -.
DR   STRING; 272631.ML2268; -.
DR   PRIDE; Q9CBB2; -.
DR   EnsemblBacteria; CAC31784; CAC31784; CAC31784.
DR   KEGG; mle:ML2268; -.
DR   PATRIC; fig|272631.5.peg.4339; -.
DR   Leproma; ML2268; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_057696_0_0_11; -.
DR   OMA; ANAAWDV; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000000806; 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   HAMAP; MF_00470; MenC_1; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR010196; OSB_synthase_MenC1.
DR   InterPro; IPR041338; OSBS_N.
DR   Pfam; PF18374; Enolase_like_N; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..334
FT                   /note="o-succinylbenzoate synthase"
FT                   /id="PRO_0000171278"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   ACT_SITE        209
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
SQ   SEQUENCE   334 AA;  35311 MW;  9590196DACF93145 CRC64;
     MIPTLTELLD RLHVVALPMR VRFRGITTRE VALIDGPAGW GEFGAFLEYQ PLEASAWLVA
     GIEAAYGEPP EGRRDRIPIN ATVPAVSATQ VPEVLARFPG VRTAKVKVAE PGQNLADDVD
     RVNAVRELVE TVRVDANGGW SVEAAAQAAV ALTADGPLEY LEQPCATVAE LAALRRRVDI
     PIAADESIRK ADDPLAVVRS HAADVAVLKV APLGGIASFL AIAAQIDIPV VVSSALDSVV
     GITAGLIAAA ALPELDYACG LGTGRLFVAD VAEPMLPVDG FLPVGPVTPD PARLQALGTP
     PARRQWWIDR VKTCYSLLVP CAGDQSGLRR PRDR