ID   MENH_YERPS              Reviewed;         272 AA.
AC   Q669C8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
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};
GN   OrderedLocusNames=YPTB2559;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH21797.1; -; Genomic_DNA.
DR   RefSeq; WP_011192655.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q669C8; -.
DR   SMR; Q669C8; -.
DR   ESTHER; yerpe-YPO2526; MenH_SHCHC.
DR   GeneID; 66845018; -.
DR   KEGG; ypo:BZ17_4079; -.
DR   KEGG; yps:YPTB2559; -.
DR   PATRIC; fig|273123.14.peg.4289; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00900.
DR   Proteomes; UP000001011; 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; alpha/beta hydrolase; 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   NCBIfam; TIGR03695; menH_SHCHC; 1.
DR   PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Lyase; Menaquinone biosynthesis.
FT   CHAIN           1..272
FT                   /note="2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341934"
SQ   SEQUENCE   272 AA;  30258 MW;  33CE37CF96FC0D21 CRC64;
     MTTLACQKLA PHPESPRHQH AGPWLVWLHG LLGSGQDWLP VAQLCGDYPS LLIDLPGHGQ
     SVSLSADGFA DISRQLSQTL QANGIREYWL AGYSLGGRIA IYHACYGRHH GLQGLLVEGG
     NLGLENAELR QARLQQDRQW AQRFRQEPLP QVLDDWYQQA VFADLDPQQR EQLVLLRADN
     HGTAVAEMLE ATSLGHQPWL LPALQRLNVP YTYLCGDRDH KFLQLAQQYR LPLHTLARAG
     HNAHRANPGA FAAQVLAFLS QSSCLPPSSL SR
//