BIOC1_COXBU
ID BIOC1_COXBU Reviewed; 282 AA.
AC Q83E64;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00835};
DE Short=Malonyl-ACP O-methyltransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00835};
GN Name=bioC1 {ECO:0000255|HAMAP-Rule:MF_00835}; OrderedLocusNames=CBU_0467;
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; AAO90016.1; -; Genomic_DNA.
DR RefSeq; NP_819502.1; NC_002971.3.
DR RefSeq; WP_010957596.1; NC_002971.4.
DR AlphaFoldDB; Q83E64; -.
DR SMR; Q83E64; -.
DR STRING; 227377.CBU_0467; -.
DR EnsemblBacteria; AAO90016; AAO90016; CBU_0467.
DR GeneID; 1208351; -.
DR KEGG; cbu:CBU_0467; -.
DR PATRIC; fig|227377.7.peg.457; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_046586_2_1_6; -.
DR OMA; PSMWELM; -.
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; 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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..282
FT /note="Malonyl-[acyl-carrier protein] O-methyltransferase
FT 1"
FT /id="PRO_0000412491"
SQ SEQUENCE 282 AA; 31709 MW; 23ED44FE6266B879 CRC64;
MPKTQFQVDQ NAVKKALHAA ARTYDNVGMV PKAIADRLLE RLDFIRLNPL CVVDVGARTG
YATQQLEERY REAIVVGLDF SVAILKAASS KMMVGEYTAL PFADRSVDLI FSNLAFQWSS
DLQQTLQECH RVLKPGGLLL FSTVGPDTLK ELHSSFADGH RHVHPFYDMH DIGDMLTQLR
FTDPVMDTER LIVHYSSVPQ LIKDLKQLGA QNASQDRLKG LMGKTQWRQM LTNYENCREE
NGALPATVEV IYGHAFGTES NSFKNANGEE VTVPIDKIIR RN