ID   MENH_YERE8              Reviewed;         274 AA.
AC   A1JKU0;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
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=YE1376;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL11469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM286415; CAL11469.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_042661374.1; NC_008800.1.
DR   RefSeq; YP_001005691.1; NC_008800.1.
DR   AlphaFoldDB; A1JKU0; -.
DR   SMR; A1JKU0; -.
DR   STRING; 393305.YE1376; -.
DR   ESTHER; yere8-menh; MenH_SHCHC.
DR   EnsemblBacteria; CAL11469; CAL11469; YE1376.
DR   KEGG; yen:YE1376; -.
DR   PATRIC; fig|393305.7.peg.1496; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_38_2_6; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00900.
DR   Proteomes; UP000000642; 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..274
FT                   /note="2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000341929"
SQ   SEQUENCE   274 AA;  30412 MW;  9054E7A134387150 CRC64;
     MTLACCKLDP HPQSPARQHT GPWLVWLHGL LGSGQDWLPV AELCGDYPSL LIDLPGHGNS
     VALTTTGFED ISRQISETLQ ANGIREYWLA GYSLGGRIAM YHACYGHKVG LQGLLVEGGN
     LGLESDELRK ARFEQDCQWA QRFRHEPLPQ VLADWYQQDV FADLDSQQRE QLVAVRANNH
     GPAVADMLEA TSLGHQPWLL PALQCLSVPY TYLCGERDHK FQQVAHQYKL PLRTLARAGH
     NAHRANPGAF AALVLSFLSQ SSFLPLSSFL PPSR