MENH_ECOL6
ID MENH_ECOL6 Reviewed; 252 AA.
AC Q8FFL2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=c2807;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81261.1; -; Genomic_DNA.
DR RefSeq; WP_000600525.1; NC_004431.1.
DR AlphaFoldDB; Q8FFL2; -.
DR SMR; Q8FFL2; -.
DR STRING; 199310.c2807; -.
DR ESTHER; ecoli-YFBB; MenH_SHCHC.
DR MEROPS; S33.996; -.
DR EnsemblBacteria; AAN81261; AAN81261; c2807.
DR KEGG; ecc:c2807; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_38_2_6; -.
DR OMA; LNDWYQQ; -.
DR BioCyc; ECOL199310:C2807-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR Proteomes; UP000001410; 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_0000341912"
SQ SEQUENCE 252 AA; 27673 MW; C10A950E37DC5FF1 CRC64;
MILHAQAKHG KPGLPWLVFL HGFSGDCHEW QEVGEAFADY SRLYVDLPGH GGSATISVDG
FDDVTGLLCK TLVSYNILNF WLVGYSLGGR VAMMAACQEL AGLCGVVVEG GHPGLQNAEQ
RAERQRSDRQ WAQRFRTEPL TAVFADWYQQ PVFASLNDDQ RRELVALRSN NNGATLAAML
EATSLAVQPD LRANLSARTF AFYYLCGERD SKFRALAAEL AADCHVIPRA GHNAHRENPA
GVIASLAQIL RF