BIOC_BACAN
ID BIOC_BACAN Reviewed; 269 AA.
AC Q81MB2; E9R8E5; E9R8E6; Q6HTR4; Q6KN02;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835};
DE Short=Malonyl-ACP O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835};
DE EC=2.1.1.197 {ECO:0000255|HAMAP-Rule:MF_00835};
DE AltName: Full=Biotin synthesis protein BioC {ECO:0000255|HAMAP-Rule:MF_00835};
GN Name=bioC {ECO:0000255|HAMAP-Rule:MF_00835};
GN OrderedLocusNames=BA_4337, GBAA_4337, BAS4024;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
CC -!- FUNCTION: Converts the free carboxyl group of a malonyl-thioester to
CC its methyl ester by transfer of a methyl group from S-adenosyl-L-
CC methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty
CC acid synthetic pathway. {ECO:0000255|HAMAP-Rule:MF_00835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl
CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17105, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9954, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78845; EC=2.1.1.197;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00835};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00835}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00835}.
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DR EMBL; AE016879; AAP28056.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33458.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56325.1; -; Genomic_DNA.
DR RefSeq; NP_846570.1; NC_003997.3.
DR RefSeq; WP_000608924.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030274.1; NC_005945.1.
DR AlphaFoldDB; Q81MB2; -.
DR SMR; Q81MB2; -.
DR STRING; 260799.BAS4024; -.
DR DNASU; 1087555; -.
DR EnsemblBacteria; AAP28056; AAP28056; BA_4337.
DR EnsemblBacteria; AAT33458; AAT33458; GBAA_4337.
DR GeneID; 45024004; -.
DR KEGG; ban:BA_4337; -.
DR KEGG; bar:GBAA_4337; -.
DR KEGG; bat:BAS4024; -.
DR PATRIC; fig|198094.11.peg.4306; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_046586_2_3_9; -.
DR OMA; SWQAVDG; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102130; F:malonyl-CoA methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00835; BioC; 1.
DR InterPro; IPR011814; BioC.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02072; BioC; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..269
FT /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT /id="PRO_0000412477"
SQ SEQUENCE 269 AA; 31237 MW; 534281841BB12275 CRC64;
MINKTLLQKR FNVAAVSYDQ YANVQKKMAH SLLSTLDRRY SANSSIRILE LGCGTGYVTE
QLSNLFPKAH ITAIDFAESM IAVAKTRQNV KNVMFYCEDI ERLQLEETYD VIISNATFQW
LNDLKQVIRN LFHHLSIDGI LLFSTFGQET FQELHTSFQR AKEEKNIQNE TSIGQRFYSK
NQLRHICEVE TGDVHVSETC YIERFTEVRE FLHSIRKVGA TNSNEESYCQ SPSLFRAMLR
IYERDFTGNE GIMATYHALF MHITKEGKR