ID   BIOC_CALNY              Reviewed;         245 AA.
AC   E4TI44;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 54.
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=Calni_1049;
OS   Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae.
OX   NCBI_TaxID=768670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19672 / NBRC 101217 / Yu37-1;
RX   PubMed=21475587; DOI=10.4056/sigs.1523807;
RA   Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Land M.;
RT   "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT   (Yu37-1).";
RL   Stand. Genomic Sci. 4:54-62(2011).
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; CP002347; ADR18960.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4TI44; -.
DR   SMR; E4TI44; -.
DR   STRING; 768670.Calni_1049; -.
DR   EnsemblBacteria; ADR18960; ADR18960; Calni_1049.
DR   KEGG; cni:Calni_1049; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_046586_1_0_0; -.
DR   OMA; SADYWLF; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000007039; 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; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02072; BioC; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..245
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000412488"
SQ   SEQUENCE   245 AA;  29072 MW;  62C6FD139E332E1F CRC64;
     MLTSKNNFHK VAPFYEQNAL IQKKMAERLM ELVEKNVGCE FDDVLEIGCG TGLFTKLIQK
     KINYNRLFLN DLHNFISFEG GYDFLEGDIE EINLSDKFDI IFSNATFQWV KDFEQLIQKL
     YQSLKPQGYL CFTTFGEENL KEVKRITNVG LNYLTFNEYL DFLGRYFKIV AHYHTKECLY
     FQSPVDVLKH MKLTGVNSVE KVQWTKRDFV NFCESYEQFK TEEGYLLTYH PFYFIVSKNK
     EVCYD