ID   BIOC_ERWP6              Reviewed;         262 AA.
AC   D2T333;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
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}; OrderedLocusNames=EPYR_02595;
OS   Erwinia pyrifoliae (strain DSM 12163 / CIP 106111 / Ep16/96).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=644651;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12163 / CIP 106111 / Ep16/96;
RX   PubMed=20047678; DOI=10.1186/1471-2164-11-2;
RA   Smits T.H., Jaenicke S., Rezzonico F., Kamber T., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia pyrifoliae
RT   DSM 12163T and comparative genomic insights into plant pathogenicity.";
RL   BMC Genomics 11:2-2(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. {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; FN392235; CAY74975.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2T333; -.
DR   SMR; D2T333; -.
DR   EnsemblBacteria; CAY74975; CAY74975; EPYR_02595.
DR   KEGG; epr:EPYR_02595; -.
DR   PATRIC; fig|644651.3.peg.2363; -.
DR   HOGENOM; CLU_046586_2_2_6; -.
DR   OMA; SWQAVDG; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000008690; 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; 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   3: Inferred from homology;
KW   Biotin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..262
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000412497"
SQ   SEQUENCE   262 AA;  28873 MW;  534C93907FC111B8 CRC64;
     MISTACWRDC MPQTVNKQAV AAAFGRAARS YNQHAELQRQ CGERLLEHAR PGNALRVLDA
     GCGTGWFSQR WRAGGHWVTA LDLSEKMLQH ARENQAADCY LPGDIEALPF ADASFDRCWS
     NLAVQWCSSL PLALRELRRV TKPGGQVLFS TLTEGSLKEV SAAWQQIGRS APLNRFASLP
     VIEQAAGSLA LTLAGYTLTL AFPDVLSALR SLKGIGATHL HQGRSNGMIS RRELQQLEQV
     WQRDARGCLL SYQLVSGVIE RE