BIOC_BACFR
ID BIOC_BACFR Reviewed; 491 AA.
AC Q64VX6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase;
DE Short=Malonyl-ACP O-methyltransferase;
DE EC=2.1.1.197;
DE AltName: Full=Biotin synthesis protein BioC;
GN Name=bioC; OrderedLocusNames=BF1601;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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 (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AP006841; BAD48350.1; -; Genomic_DNA.
DR RefSeq; WP_011202493.1; NC_006347.1.
DR RefSeq; YP_098884.1; NC_006347.1.
DR AlphaFoldDB; Q64VX6; -.
DR SMR; Q64VX6; -.
DR STRING; 295405.BF1601; -.
DR ESTHER; bacfr-q64vx6; Duf_452.
DR EnsemblBacteria; BAD48350; BAD48350; BF1601.
DR KEGG; bfr:BF1601; -.
DR PATRIC; fig|295405.11.peg.1558; -.
DR HOGENOM; CLU_590080_0_0_10; -.
DR OMA; DIVHTEE; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002197; 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; IPR029058; AB_hydrolase.
DR InterPro; IPR011814; BioC.
DR InterPro; IPR007398; BioG.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF04301; DUF452; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02072; BioC; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..491
FT /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT /id="PRO_0000412482"
FT REGION 1..249
FT /note="Unknown"
FT REGION 250..490
FT /note="Malonyl-CoA O-methyltransferase"
SQ SEQUENCE 491 AA; 55873 MW; 1243DD6AF4EE2BD8 CRC64;
MKLKRLYPPQ KSVNSLHSET GTRCEVAGCP PLRKEALLFF AGWGMDETPF MHNLPPNKDL
IICYDYRSLD FDSTLLSTYE GIYVVAWSMG VWAASQVLPD SNLPLKQSIA INGTPFPIDD
MRGIPPAIFE GTLNNLNEAT LQKFRRRMCG SGSAFQAFLE IAPQRPVEEL KEELAAIGRQ
YSELPLSTFV WNKAIIGESD HIFPPKNQEQ AWQKYCNEIQ RYDGAHYDEK ILKENLAPAA
ASSKLLIAQR FTKAIGTYPH EARVQQQIAR KMCSLLQQHL PAHSLRRVVE FGCGTGTYSR
LLLRSFRPEH LLLNDLCEEM RHSCRDILNE RVSFLPGDAE ALDFPHGTEL ITSCSVLQWF
EHPDAFFRKC ENILNAQGYI AFSTFGKENM KEIRQLTGQG LAYRSREELT ASLSALYDIV
HTEEEVISLN FNNPMEVLYH LKQTGVTGTC NQSWTRSKLN LFCQEYERLF SPGKGSVSLT
YHPIYIIAKK R
