ID   MENH_SALTY              Reviewed;         252 AA.
AC   Q8ZNE9;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01660};
DE            Short=SHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01660};
DE            EC=4.2.99.20 {ECO:0000255|HAMAP-Rule:MF_01660};
GN   Name=menH {ECO:0000255|HAMAP-Rule:MF_01660}; OrderedLocusNames=STM2308;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes a proton abstraction reaction that results in 2,5-
CC       elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-
CC       cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-
CC       hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). {ECO:0000255|HAMAP-
CC       Rule:MF_01660}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-
CC         carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-
CC         carboxylate + pyruvate; Xref=Rhea:RHEA:25597, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:58689, ChEBI:CHEBI:58818; EC=4.2.99.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01660};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
CC       {ECO:0000255|HAMAP-Rule:MF_01660}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01660}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01660}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MenH family.
CC       {ECO:0000255|HAMAP-Rule:MF_01660}.
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DR   EMBL; AE006468; AAL21209.1; -; Genomic_DNA.
DR   RefSeq; NP_461250.1; NC_003197.2.
DR   RefSeq; WP_000979146.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZNE9; -.
DR   SMR; Q8ZNE9; -.
DR   STRING; 99287.STM2308; -.
DR   ESTHER; salty-YFBB; MenH_SHCHC.
DR   PaxDb; Q8ZNE9; -.
DR   EnsemblBacteria; AAL21209; AAL21209; STM2308.
DR   GeneID; 1253830; -.
DR   KEGG; stm:STM2308; -.
DR   PATRIC; fig|99287.12.peg.2443; -.
DR   HOGENOM; CLU_020336_38_2_6; -.
DR   OMA; LNDWYQQ; -.
DR   PhylomeDB; Q8ZNE9; -.
DR   BioCyc; SENT99287:STM2308-MON; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00900.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01660; MenH; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR022485; SHCHC_synthase_MenH.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03695; menH_SHCHC; 1.
PE   3: Inferred from homology;
KW   Lyase; Menaquinone biosynthesis; Reference proteome.
FT   CHAIN           1..252
FT                   /note="2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341922"
SQ   SEQUENCE   252 AA;  27692 MW;  8D7CA5F4A44BA47D CRC64;
     MMLHAQHMPG QPGTPSLVFL HGFSGDCHEW QPVGEQFHGC SRLYIDLPGH GGSAAIPVDG
     FADVIRLLRA TLISYNILKF WLVGYSLGGR VAMMAACQGI PGLCGLVVEG GHPGLQNEQA
     RAERRLSDGR WAERFRHEPL TEVFHDWYQQ PVFASLTAQQ RQALTALRSQ NNGETLAAML
     EATSLAVQPD LREALNALAF PFYYLCGERD SKFRALAQEV AATCHVIRNA GHNAHRENPA
     GVVDSLAQIL RL