ID   BIOC_PAESJ              Reviewed;         276 AA.
AC   C6CWS7;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=Pjdr2_1466;
OS   Paenibacillus sp. (strain JDR-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=324057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDR-2;
RX   PubMed=22675593; DOI=10.4056/sigs.2374349;
RA   Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA   Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., Nolan M.,
RA   Pati A., Martin J., Copeland A., Land M.L., Goodwin L., Jones J.B.,
RA   Ingram L.O., Shanmugam K.T., Preston J.F.;
RT   "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL   Stand. Genomic Sci. 6:1-10(2012).
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; CP001656; ACT00141.1; -; Genomic_DNA.
DR   RefSeq; WP_015843086.1; NC_012914.1.
DR   AlphaFoldDB; C6CWS7; -.
DR   SMR; C6CWS7; -.
DR   STRING; 324057.Pjdr2_1466; -.
DR   EnsemblBacteria; ACT00141; ACT00141; Pjdr2_1466.
DR   KEGG; pjd:Pjdr2_1466; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_046586_2_3_9; -.
DR   OMA; SWQAVDG; -.
DR   OrthoDB; 1664438at2; -.
DR   UniPathway; UPA00078; -.
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; IPR029063; SAM-dependent_MTases_sf.
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..276
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000412515"
SQ   SEQUENCE   276 AA;  31242 MW;  A1985CB5D0A47C97 CRC64;
     MNNPKTAIQR QFNRSAAGSY DIHADVQRTM AAELAKSIIE RNSRGKATEP KILEIGCGTG
     QFTELLLNQW PHVSITALDL APAMIHTAEQ RFKSRQSANI RFLQADVEIW AVEAPSDSFD
     LIVSNACFQW LSHPRQTISH LKRFLREGGS LVFTTFGPNT FLELHQAFAE VYHAYGMEPQ
     RHGLSVLSTN QWEEVLAEAG FSTIYCQQDT QKETYASPRD FLRSIKSMGA SHSEAIPIDG
     LSPRKLFNEM YKVYEEKFNM KDGIVATYEW LLIYAG