ID   MENH_SALPA              Reviewed;         252 AA.
AC   Q5PN75;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=SPA0555;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76557.1; -; Genomic_DNA.
DR   RefSeq; WP_000979139.1; NC_006511.1.
DR   AlphaFoldDB; Q5PN75; -.
DR   SMR; Q5PN75; -.
DR   ESTHER; salty-YFBB; MenH_SHCHC.
DR   EnsemblBacteria; AAV76557; AAV76557; SPA0555.
DR   KEGG; spt:SPA0555; -.
DR   HOGENOM; CLU_020336_38_2_6; -.
DR   OMA; LNDWYQQ; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00900.
DR   Proteomes; UP000008185; 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.
FT   CHAIN           1..252
FT                   /note="2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341919"
SQ   SEQUENCE   252 AA;  27651 MW;  4C7CC1C11AD277D3 CRC64;
     MMLHAQHMPG QPGAPSLVFL HGFSGDCREW QPVGEQFHGC SRLYIDLPGH GGSAAIPVGG
     FADVIRLLRA TLISYNILKF WLVGYSLGGR VAMMAACQGI PGLCGLVVEG GHPGLQNERA
     RAERRLSDGR WAERFRHEPL TEVFHDWYQQ PVFASLTAQQ RQALTALRSQ NNGETLAAML
     EATSLAVQPD LREALNALAF PFYYLCGERD SKFRALAQEV AATCHVIRNA GHNAHRENPA
     GVVDSLAQIL RL