ID   BIOC_SERMA              Reviewed;         255 AA.
AC   P36571;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE BIOTIN BIOSYNTHESIS.
RC   STRAIN=Sr41;
RX   PubMed=8250549; DOI=10.1128/aem.59.10.3225-3232.1993;
RA   Sakurai N., Imai Y., Masuda M., Komatsubara S., Tosa T.;
RT   "Molecular breeding of a biotin-hyperproducing Serratia marcescens
RT   strain.";
RL   Appl. Environ. Microbiol. 59:3225-3232(1993).
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       ECO:0000269|PubMed:8250549}.
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; D17468; BAA04287.1; -; Genomic_DNA.
DR   AlphaFoldDB; P36571; -.
DR   SMR; P36571; -.
DR   STRING; 273526.SMDB11_0562; -.
DR   PRIDE; P36571; -.
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; 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; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..255
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000204419"
SQ   SEQUENCE   255 AA;  27777 MW;  1DD2532B3FCA7F67 CRC64;
     MTSANDTVNK QAVASAFSRA AGSYDAAAAL QRDVGERLLG MGSSHPGEQL LDAGCGTGYF
     SRMWRERGKR VTALDLAPGM LDVARQRQAA HHYLLGDIEQ VPLPDAAMDI CFSSLVVQWC
     SDLPAALAEL YRVTRPGGVI LFSTLAAGSL QELGDAWQQV DGERHVNAFL PLTQIRTACA
     AYRHELVTEL RTLNYPDVMT LMRSLKGIGA THLHQGREGG LMSRGRLAAL QAAYPCRQGQ
     FPLSYHLAYG VIYRE