MENH_BACSU
ID MENH_BACSU Reviewed; 274 AA.
AC P23974; O34312;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative 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=ytfB, ytxM;
GN OrderedLocusNames=BSU30810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / RB1;
RX PubMed=8566759; DOI=10.1016/0378-1119(95)00662-1;
RA Rowland B., Hill K., Miller P., Driscoll J.R., Taber H.W.;
RT "Structural organization of a Bacillus subtilis operon encoding menaquinone
RT biosynthetic enzymes.";
RL Gene 167:105-109(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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=AAA50400.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC37015.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M74538; AAC37015.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M74521; AAA50400.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF008220; AAC00225.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15059.1; -; Genomic_DNA.
DR PIR; H70003; H70003.
DR RefSeq; NP_390959.1; NC_000964.3.
DR RefSeq; WP_004398592.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P23974; -.
DR SMR; P23974; -.
DR STRING; 224308.BSU30810; -.
DR ESTHER; bacsu-ytxm; MenH_SHCHC.
DR PaxDb; P23974; -.
DR PRIDE; P23974; -.
DR EnsemblBacteria; CAB15059; CAB15059; BSU_30810.
DR GeneID; 937115; -.
DR KEGG; bsu:BSU30810; -.
DR PATRIC; fig|224308.179.peg.3339; -.
DR eggNOG; COG0596; Bacteria.
DR InParanoid; P23974; -.
DR OMA; LNDWYQQ; -.
DR PhylomeDB; P23974; -.
DR BioCyc; BSUB:BSU30810-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR Proteomes; UP000001570; 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; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR022485; SHCHC_synthase_MenH.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
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..274
FT /note="Putative 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
FT carboxylate synthase"
FT /id="PRO_0000207073"
FT DOMAIN 26..259
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 274 AA; 30703 MW; 7C9CB39D493D54CE CRC64;
MGTVNITVSD GVRYAVADEG PNASEAVVCL HGFTGSKQSW TFLDEMLPDS RLIKIDCLGH
GETDAPLNGK RYSTTRQVSD LAEIFDQLKL HKVKLIGYSM GGRLAYSFAM TYPERVSALV
LESTTPGLKT LGERRERIMR DRKLADFILR DGLEAFVAYW ENIPLFSSQQ RLAEDIRYRI
RSGRLRNNKI GLANSLTGMG TGSQPSLWSR VEEIDVPVLL ICGEWDEKFC AINQEVHKML
PSSRIEIVPK AGHTVHVEQP RLFGKIVSEF LTSI
