MENC_PASMU
ID MENC_PASMU Reviewed; 337 AA.
AC Q9CLV7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=PM1094;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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; AE004439; AAK03178.1; -; Genomic_DNA.
DR RefSeq; WP_010907015.1; NC_002663.1.
DR AlphaFoldDB; Q9CLV7; -.
DR SMR; Q9CLV7; -.
DR STRING; 747.DR93_870; -.
DR EnsemblBacteria; AAK03178; AAK03178; PM1094.
DR KEGG; pmu:PM1094; -.
DR PATRIC; fig|272843.6.peg.1108; -.
DR HOGENOM; CLU_030273_0_1_6; -.
DR OMA; YEANRDG; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000000809; 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;
KW Reference proteome.
FT CHAIN 1..337
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000171273"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
SQ SEQUENCE 337 AA; 37891 MW; 8D73660A028B6A3C CRC64;
MTMIRKFKLY QYSIPVDSQL ILRNRFLKKR EGLLVQVCCD DAQGWGEIAP LPEFSQETLE
QAREQALAWL EEWSASDGSA GKLPLEHLFP SVAFGLSCAL AEMKGLLHEE GNYQVAPLCY
GDPDELYDPL NQMQGEKVAK IKVGMYEANR DGLIADMLLE AIPDLHLRLD ANRSWTPSKA
QMFAKYVKPE HRARIQFLEE PCKTPAESLQ FAEETGIAIA WDETVRDAEF QQNPPHFFTP
QVKAIVIKPT LVGSIQRCVE LIKQAHAHGI QAVISSSIES SLGLTQLARL AQQYTPNTVP
GLDTLDLMDY QVIRPWPSST LPLIDLDSEY IVPIKLD
