MENH_YERPE
ID MENH_YERPE Reviewed; 272 AA.
AC Q7CJ75; Q74T54;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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}; Synonyms=mhpC3;
GN OrderedLocusNames=YPO2526, y1661, YP_2337;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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; AE009952; AAM85230.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62543.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL21152.1; -; Genomic_DNA.
DR PIR; AE0308; AE0308.
DR RefSeq; WP_002210246.1; NZ_WUCM01000021.1.
DR RefSeq; YP_002347488.1; NC_003143.1.
DR AlphaFoldDB; Q7CJ75; -.
DR SMR; Q7CJ75; -.
DR STRING; 214092.YPO2526; -.
DR ESTHER; yerpe-YPO2526; MenH_SHCHC.
DR PaxDb; Q7CJ75; -.
DR DNASU; 1146608; -.
DR EnsemblBacteria; AAM85230; AAM85230; y1661.
DR EnsemblBacteria; AAS62543; AAS62543; YP_2337.
DR GeneID; 57976161; -.
DR KEGG; ype:YPO2526; -.
DR KEGG; ypk:y1661; -.
DR KEGG; ypm:YP_2337; -.
DR PATRIC; fig|214092.21.peg.2944; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_38_2_6; -.
DR OMA; LNDWYQQ; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..272
FT /note="2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
FT carboxylate synthase"
FT /id="PRO_0000341930"
SQ SEQUENCE 272 AA; 30282 MW; 33CA8CF8D6B9ABF5 CRC64;
MTTLACRKLA PHPESPRHQH AGPWLVWLHG LLGSGQDWLP VAQLCGDYPS LLIDLPGHGQ
SVSLSADGFA DISRQLSQTL QANGIREYWL AGYSLGGRIA IYHACYGRHH GLQGLLVEGG
NLGLENAELR QARLQQDRQW AQRFRQEPLP QVLDDWYQQA VFADLDPQQR EQLVLLRADN
HGPAVAEMLE ATSLGHQPWL LPALQRLNVP YTYLCGDRDH KFLQLAQQYR LPLHTLARAG
HNAHRANPGA FAAQVLAFLS QSSCLPPSSL SR
