ID   MENH_ECOUT              Reviewed;         252 AA.
AC   Q1R9F0;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=UTI89_C2547;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE08014.1; -; Genomic_DNA.
DR   RefSeq; WP_000600529.1; NC_007946.1.
DR   AlphaFoldDB; Q1R9F0; -.
DR   SMR; Q1R9F0; -.
DR   ESTHER; ecoli-YFBB; MenH_SHCHC.
DR   MEROPS; S33.996; -.
DR   EnsemblBacteria; ABE08014; ABE08014; UTI89_C2547.
DR   KEGG; eci:UTI89_C2547; -.
DR   HOGENOM; CLU_020336_38_2_6; -.
DR   OMA; LNDWYQQ; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00900.
DR   Proteomes; UP000001952; 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_0000341908"
SQ   SEQUENCE   252 AA;  27657 MW;  69CE408FEBDC4230 CRC64;
     MILHAQAKHG KPGLPWLVFL HGFSGDCHEW QEVGEAFADY SRLYVDLPGH GGSATISVDG
     FDDVTGLLCK TLVSYNILNF WLVGYSLGGR VAMMAACQEP AGLCGVVVEG GHPGLQNAEQ
     RAERQRSDRQ WAQRFRTEPL TAVFADWYQQ PVFASLNDDQ RRELVALRSN NNGATLAAML
     EATSLAVQPD LRANLSARTF AFYYLCGERD SKFRALAAEL AADCHVIPRA GHNAHRENPA
     GVIASLAQIL RF