ID   BIOC_ECOLI              Reviewed;         251 AA.
AC   P12999; Q2MBJ2;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 146.
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=b0777, JW0760;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3058702; DOI=10.1016/s0021-9258(19)77675-3;
RA   Otsuka A.J., Buoncristiani M.R., Howard P.K., Flamm J., Johnson O.,
RA   Yamamoto R., Uchida K., Cook C., Ruppert J., Matsuzaki J.;
RT   "The Escherichia coli biotin biosynthetic enzyme sequences predicted from
RT   the nucleotide sequence of the bio operon.";
RL   J. Biol. Chem. 263:19577-19585(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pearson B.M., McKee R.A.;
RT   "Genetic material for expression of biotin synthetase enzymes.";
RL   Patent number GB2216530, 11-OCT-1989.
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   FUNCTION IN THE BIOTIN BIOSYNTHESIS.
RX   PubMed=4864413; DOI=10.1128/jb.94.6.2065-2066.1967;
RA   Del Campillo-Campbell A., Kayajanian G., Campbell A., Adhya S.;
RT   "Biotin-requiring mutants of Escherichia coli K-12.";
RL   J. Bacteriol. 94:2065-2066(1967).
RN   [6]
RP   FUNCTION IN THE BIOTIN BIOSYNTHESIS, CATALYTIC ACTIVITY, AND SUBSTRATE
RP   SPECIFICITY.
RX   PubMed=20693992; DOI=10.1038/nchembio.420;
RA   Lin S., Hanson R.E., Cronan J.E.;
RT   "Biotin synthesis begins by hijacking the fatty acid synthetic pathway.";
RL   Nat. Chem. Biol. 6:682-688(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. E.coli employs a methylation and demethylation
CC       strategy to allow elongation of a temporarily disguised malonate moiety
CC       to a pimelate moiety by the fatty acid synthetic enzymes.
CC       {ECO:0000269|PubMed:20693992, ECO:0000269|PubMed:4864413}.
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:0000269|PubMed:20693992};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; J04423; AAA23517.1; -; Genomic_DNA.
DR   EMBL; A11534; CAA00966.1; -; Unassigned_DNA.
DR   EMBL; U00096; AAC73864.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76364.1; -; Genomic_DNA.
DR   PIR; A64814; BVECBC.
DR   RefSeq; NP_415298.1; NC_000913.3.
DR   RefSeq; WP_000246761.1; NZ_STEB01000028.1.
DR   AlphaFoldDB; P12999; -.
DR   SMR; P12999; -.
DR   BioGRID; 4259952; 8.
DR   BioGRID; 849763; 1.
DR   IntAct; P12999; 11.
DR   STRING; 511145.b0777; -.
DR   PaxDb; P12999; -.
DR   PRIDE; P12999; -.
DR   EnsemblBacteria; AAC73864; AAC73864; b0777.
DR   EnsemblBacteria; BAE76364; BAE76364; BAE76364.
DR   GeneID; 945388; -.
DR   KEGG; ecj:JW0760; -.
DR   KEGG; eco:b0777; -.
DR   PATRIC; fig|1411691.4.peg.1501; -.
DR   EchoBASE; EB0117; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_2_2_6; -.
DR   InParanoid; P12999; -.
DR   OMA; SWQAVDG; -.
DR   PhylomeDB; P12999; -.
DR   BioCyc; EcoCyc:EG10119-MON; -.
DR   BioCyc; MetaCyc:EG10119-MON; -.
DR   BRENDA; 2.1.1.197; 2026.
DR   UniPathway; UPA00078; -.
DR   PRO; PR:P12999; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IMP:EcoCyc.
DR   GO; GO:0102130; F:malonyl-CoA methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009102; P:biotin biosynthetic process; IMP:EcoCyc.
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; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02072; BioC; 1.
PE   1: Evidence at protein level;
KW   Biotin biosynthesis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..251
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000204416"
FT   CONFLICT        149
FT                   /note="L -> R (in Ref. 1; AAA23517)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   251 AA;  28276 MW;  D07DA38FFE974E45 CRC64;
     MATVNKQAIA AAFGRAAAHY EQHADLQRQS ADALLAMLPQ RKYTHVLDAG CGPGWMSRHW
     RERHAQVTAL DLSPPMLVQA RQKDAADHYL AGDIESLPLA TATFDLAWSN LAVQWCGNLS
     TALRELYRVV RPKGVVAFTT LVQGSLPELH QAWQAVDERP HANRFLPPDE IEQSLNGVHY
     QHHIQPITLW FDDALSAMRS LKGIGATHLH EGRDPRILTR SQLQRLQLAW PQQQGRYPLT
     YHLFLGVIAR E