MENH_ECOLI
ID MENH_ECOLI Reviewed; 252 AA.
AC P37355; P76477; P76932;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
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=yfbB;
GN OrderedLocusNames=b2263, JW2258;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Sharma V., Hudspeth M.E., Meganathan R.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-252.
RC STRAIN=K12;
RX PubMed=1629162; DOI=10.1128/jb.174.15.5057-5062.1992;
RA Sharma V., Suvarna K., Meganathan R., Hudspeth M.E.;
RT "Menaquinone (vitamin K2) biosynthesis: nucleotide sequence and expression
RT of the menB gene from Escherichia coli.";
RL J. Bacteriol. 174:5057-5062(1992).
RN [6]
RP FUNCTION AS AN ACYL-COA THIOESTER HYDROLASE.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [7]
RP FUNCTION AS A SHCHC SYNTHASE, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-86;
RP ASP-210 AND HIS-232, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=18284213; DOI=10.1021/bi7023755;
RA Jiang M., Chen X., Guo Z.-F., Cao Y., Chen M., Guo Z.;
RT "Identification and characterization of (1R,6R)-2-succinyl-6-hydroxy-2,4-
RT cyclohexadiene-1-carboxylate synthase in the menaquinone Biosynthesis of
RT Escherichia coli.";
RL Biochemistry 47:3426-3434(2008).
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). Is also able to
CC catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in
CC vitro. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:18284213}.
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 ECO:0000269|PubMed:18284213};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.1 uM for SEPHCHC (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:18284213};
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 ECO:0000269|PubMed:18284213}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MenH family.
CC {ECO:0000255|HAMAP-Rule:MF_01660, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24151.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=M93421; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L35030; AAA24151.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75323.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16087.2; -; Genomic_DNA.
DR EMBL; M93421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64997; E64997.
DR RefSeq; NP_416766.1; NC_000913.3.
DR RefSeq; WP_000600499.1; NZ_LN832404.1.
DR PDB; 4GDM; X-ray; 2.75 A; A/B/C=1-252.
DR PDB; 4GEC; X-ray; 2.50 A; A/B/C=1-252.
DR PDB; 4GEG; X-ray; 2.49 A; A/B/C=1-252.
DR PDB; 4MXD; X-ray; 1.45 A; A=1-252.
DR PDB; 4MYD; X-ray; 1.37 A; A/B/C=1-252.
DR PDB; 4MYS; X-ray; 1.42 A; A/B/C=1-252.
DR PDBsum; 4GDM; -.
DR PDBsum; 4GEC; -.
DR PDBsum; 4GEG; -.
DR PDBsum; 4MXD; -.
DR PDBsum; 4MYD; -.
DR PDBsum; 4MYS; -.
DR AlphaFoldDB; P37355; -.
DR SMR; P37355; -.
DR BioGRID; 4260505; 14.
DR BioGRID; 851077; 1.
DR IntAct; P37355; 5.
DR STRING; 511145.b2263; -.
DR ESTHER; ecoli-YFBB; MenH_SHCHC.
DR MEROPS; S33.996; -.
DR PaxDb; P37355; -.
DR PRIDE; P37355; -.
DR EnsemblBacteria; AAC75323; AAC75323; b2263.
DR EnsemblBacteria; BAA16087; BAA16087; BAA16087.
DR GeneID; 946736; -.
DR KEGG; ecj:JW2258; -.
DR KEGG; eco:b2263; -.
DR PATRIC; fig|1411691.4.peg.4473; -.
DR EchoBASE; EB2333; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_38_2_6; -.
DR InParanoid; P37355; -.
DR OMA; LNDWYQQ; -.
DR PhylomeDB; P37355; -.
DR BioCyc; EcoCyc:EG12438-MON; -.
DR BioCyc; MetaCyc:EG12438-MON; -.
DR BRENDA; 3.1.2.2; 2026.
DR BRENDA; 4.2.99.20; 2026.
DR SABIO-RK; P37355; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR PRO; PR:P37355; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IDA:EcoCyc.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Menaquinone biosynthesis; Reference proteome.
FT CHAIN 1..252
FT /note="2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
FT carboxylate synthase"
FT /id="PRO_0000169174"
FT MUTAGEN 86
FT /note="S->A: 1400-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18284213"
FT MUTAGEN 210
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18284213"
FT MUTAGEN 232
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18284213"
FT CONFLICT 176
FT /note="L -> V (in Ref. 1; AAA24151)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4MYD"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:4MYD"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4GEC"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:4MYD"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:4MYD"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:4MYD"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:4MYD"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:4MYD"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:4MYD"
SQ SEQUENCE 252 AA; 27682 MW; FE7D77861842B68C CRC64;
MILHAQAKHG KPGLPWLVFL HGFSGDCHEW QEVGEAFADY SRLYVDLPGH GGSAAISVDG
FDDVTDLLRK TLVSYNILDF WLVGYSLGGR VAMMAACQGL AGLCGVIVEG GHPGLQNAEQ
RAERQRSDRQ WVQRFLTEPL TAVFADWYQQ PVFASLNDDQ RRELVALRSN NNGATLAAML
EATSLAVQPD LRANLSARTF AFYYLCGERD SKFRALAAEL AADCHVIPRA GHNAHRENPA
GVIASLAQIL RF
