ID   BIOC2_COXBU             Reviewed;         248 AA.
AC   Q83CU8;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00835};
DE            Short=Malonyl-ACP O-methyltransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00835};
GN   Name=bioC2 {ECO:0000255|HAMAP-Rule:MF_00835}; OrderedLocusNames=CBU_1004;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90525.1; -; Genomic_DNA.
DR   RefSeq; NP_820011.1; NC_002971.3.
DR   RefSeq; WP_010957947.1; NZ_CCYB01000044.1.
DR   AlphaFoldDB; Q83CU8; -.
DR   SMR; Q83CU8; -.
DR   STRING; 227377.CBU_1004; -.
DR   PRIDE; Q83CU8; -.
DR   EnsemblBacteria; AAO90525; AAO90525; CBU_1004.
DR   GeneID; 1208900; -.
DR   KEGG; cbu:CBU_1004; -.
DR   PATRIC; fig|227377.7.peg.997; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_2_3_6; -.
DR   OMA; HIGLFIC; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002671; 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; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
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..248
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase
FT                   2"
FT                   /id="PRO_0000412492"
SQ   SEQUENCE   248 AA;  28207 MW;  CE198B8FCF908B2C CRC64;
     MMVNSLKKRI QRSFNKAFDT YDDHASIQRE ICKQLLKPLK EMRIQTKIIA DFACGTGIST
     KAVADSFPYQ NLYAIDFCEK LLIQAKSKLK ESNVEFILAD FETNVFLCNS LDLIFCNMGF
     QWALDLKQTF FSLFSQLKAF GVLAFSVPLL GTFCELRNDC RNPFLTLQSI VQLLKAVGFE
     LLTADEKIFT DSFESPLDAI RSIKSIGANC LLYPKRNKGL SPMPIEKNNT DTTLTYHIGF
     FIAKKIIQ