MENH_ECO27
ID MENH_ECO27 Reviewed; 252 AA.
AC B7UFS6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=E2348C_2408;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM180568; CAS09956.1; -; Genomic_DNA.
DR RefSeq; WP_000600527.1; NC_011601.1.
DR AlphaFoldDB; B7UFS6; -.
DR SMR; B7UFS6; -.
DR ESTHER; ecoli-YFBB; MenH_SHCHC.
DR MEROPS; S33.996; -.
DR EnsemblBacteria; CAS09956; CAS09956; E2348C_2408.
DR KEGG; ecg:E2348C_2408; -.
DR HOGENOM; CLU_020336_38_2_6; -.
DR OMA; LNDWYQQ; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR Proteomes; UP000008205; 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_1000187103"
SQ SEQUENCE 252 AA; 27601 MW; C108B70C17FE5DD3 CRC64;
MILHAQAKHG KPGLPWLVFL HGFSGDCHEW QEVGEAFADY SRLYVDLPGH GGSATISVDG
FDDVTGLLCK TLVSYNILNF WLVGYSLGGR VAMMAACQEL AGLCGVVVEG GHPGLQNAEQ
RAERQRSDRQ WAQRFRTEPL TAVFADWYQQ PVFASLNDDQ RRGLVALRSN NNGATLAAML
EATSLAVQPD LRANLSARTF AFYYLCGERD SKFRALAAEL AADCHVIPRA GHNAHRENPA
GVIASLAQIL RF
