MENF_BACSU
ID MENF_BACSU Reviewed; 471 AA.
AC P23973; P23972;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Isochorismate synthase MenF {ECO:0000255|HAMAP-Rule:MF_01935};
DE EC=5.4.4.2 {ECO:0000255|HAMAP-Rule:MF_01935};
DE AltName: Full=Isochorismate mutase {ECO:0000255|HAMAP-Rule:MF_01935};
GN Name=menF {ECO:0000255|HAMAP-Rule:MF_01935}; Synonyms=icsM;
GN OrderedLocusNames=BSU30830;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / RB1;
RX PubMed=1629163; DOI=10.1128/jb.174.15.5063-5071.1992;
RA Driscoll J.R., Taber H.W.;
RT "Sequence organization and regulation of the Bacillus subtilis menBE
RT operon.";
RL J. Bacteriol. 174:5063-5071(1992).
RN [2]
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 [3]
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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=3131310; DOI=10.1128/jb.170.6.2742-2748.1988;
RA Miller P., Mueller J., Hill K., Taber H.W.;
RT "Transcriptional regulation of a promoter in the men gene cluster of
RT Bacillus subtilis.";
RL J. Bacteriol. 170:2742-2748(1988).
CC -!- FUNCTION: Catalyzes the conversion of chorismate to isochorismate.
CC {ECO:0000255|HAMAP-Rule:MF_01935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01935};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01935};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7.
CC {ECO:0000255|HAMAP-Rule:MF_01935}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01935}.
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01935}.
CC -!- CAUTION: Used to include what was called 'menR'. {ECO:0000305}.
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DR EMBL; M74521; AAA50396.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M74521; AAA50397.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M74538; AAC37013.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00223.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15061.1; -; Genomic_DNA.
DR EMBL; M21320; AAA22594.1; -; Genomic_DNA.
DR PIR; A69657; A69657.
DR RefSeq; NP_390961.1; NC_000964.3.
DR RefSeq; WP_004398674.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P23973; -.
DR SMR; P23973; -.
DR STRING; 224308.BSU30830; -.
DR PaxDb; P23973; -.
DR PRIDE; P23973; -.
DR EnsemblBacteria; CAB15061; CAB15061; BSU_30830.
DR GeneID; 937190; -.
DR KEGG; bsu:BSU30830; -.
DR PATRIC; fig|224308.179.peg.3341; -.
DR eggNOG; COG1169; Bacteria.
DR InParanoid; P23973; -.
DR OMA; TGHGQSI; -.
DR PhylomeDB; P23973; -.
DR BioCyc; BSUB:BSU30830-MON; -.
DR BioCyc; MetaCyc:MON-13806; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00163.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008909; F:isochorismate synthase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IGC:UniProtKB.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.120.10; -; 1.
DR HAMAP; MF_01935; MenF; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR004561; IsoChor_synthase.
DR InterPro; IPR034681; MenF.
DR Pfam; PF00425; Chorismate_bind; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00543; isochor_syn; 1.
PE 3: Inferred from homology;
KW Isomerase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..471
FT /note="Isochorismate synthase MenF"
FT /id="PRO_0000154150"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT CONFLICT 12
FT /note="E -> K (in Ref. 5; AAA50396/AAA22594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 52812 MW; 94C047C549FC4CF9 CRC64;
MVTTVQRTFR KEVLHALHKA KEVNHAVLIS YSRQIESLDP LSFFNYGAKK YTGNRFFWSD
PESELTIVGL GKEAVFQTNQ KNSERYREVF EQWERFKKTA FHIYEEEKLQ HSAVGPVLFG
GFSFDPCEER GSQWDHFSEG DFFVPALMLT MTAEGPFLTV NRWVSGGEDA EAVLEGLKAF
AAEFMVPDFK QEDQAVIAAA EELDKDDWLK AIETATSQIK EKQYDKVVLA RELLLTFDGP
IQIEPVLKTL LDDQQTSYVF AIEQEGKTFV GASPERLIKR DGGTVMSSCL AGSIKRGVNE
EDDRRIGLEL LNDEKNLLEH DIVVGMIHNA FVSSCSEVEK PDGPVLYKTK SVQHLFTPIV
GQLRESASIF DLIEKLHPTP ALGGSPQEKA VDVIREIEPM SRGWYAAPIG WIDSQDNGEF
AVAIRSGLIE GSTARLFAGC GIVEDSEPIS EYEETQIKLK PMISALGGER R
