ID   BIOC_BACF6              Reviewed;         490 AA.
AC   E1WTS2;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase;
DE            Short=Malonyl-ACP O-methyltransferase;
DE            EC=2.1.1.197;
DE   AltName: Full=Biotin synthesis protein BioC;
GN   Name=bioC; OrderedLocusNames=BF638R_1616;
OS   Bacteroides fragilis (strain 638R).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=862962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638R;
RX   PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA   Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA   Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA   Barron A., Clark L., Bentley S.D., Parkhill J.;
RT   "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT   strain capsule diversity in three strains of Bacteroides fragilis.";
RL   Microbiology 156:3255-3269(2010).
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 (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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; FQ312004; CBW22145.1; -; Genomic_DNA.
DR   RefSeq; WP_014298602.1; NC_016776.1.
DR   AlphaFoldDB; E1WTS2; -.
DR   SMR; E1WTS2; -.
DR   ESTHER; bacfr-q64vx6; Duf_452.
DR   PRIDE; E1WTS2; -.
DR   EnsemblBacteria; CBW22145; CBW22145; BF638R_1616.
DR   KEGG; bfg:BF638R_1616; -.
DR   PATRIC; fig|862962.3.peg.1622; -.
DR   HOGENOM; CLU_590080_0_0_10; -.
DR   OMA; DIVHTEE; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000008560; 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; IPR029058; AB_hydrolase.
DR   InterPro; IPR011814; BioC.
DR   InterPro; IPR007398; BioG.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04301; DUF452; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR02072; BioC; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..490
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000412483"
FT   REGION          1..248
FT                   /note="Unknown"
FT   REGION          249..490
FT                   /note="Malonyl-CoA O-methyltransferase"
SQ   SEQUENCE   490 AA;  55699 MW;  306F0D4BC24EA0A1 CRC64;
     MKLKRLYPPQ KAVNSLHSET GTGCEVAGCP PLRKEALLFF AGWGMDETPF MHNLPPNKDL
     IICYDYRSLD FDSTLLSTYE GIYVVAWSMG VWAASQVLPD SNLPLKQSIA INGTPFPIDD
     MRGIPPAIFE GTLNNLNEAT LQKFRRRMCG SGSAFQAFLE IAPQRPVEEL KEELVAIGRQ
     YSELPPSTFV WNKAIIGESD HIFPPKNQEQ AWQKYCNEIQ RYDGAHYDEK ILKENLAPAA
     SSKLLIAQRF TKAIGTYPHE ARVQQQIARK MCSLLQQHLP AHSLRRVVEF GCGTGTYSRL
     LLRSFRPEHL LLNDLCEEMR HSCRDILNER VSFLPGDAEA LDFPHGTELI TSCSVLQWFE
     HPDAFFRKCE NILNAQGYIA FSTFGKENMK EIRQLTGQGL AYRSREELTA SLSALYDIVH
     TEEEVISLNF NNPMEVLYHL KQTGVTGTCN QSWTRSKLNL FCQEYERLFS PGKGSVSLTY
     HPIYIIAKKR