ID BIOC1_ILYPC Reviewed; 268 AA.
AC E3H9W1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=Ilyop_0229;
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Ilyobacter.
OX NCBI_TaxID=572544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1;
RX PubMed=21304735; DOI=10.4056/sigs.1273360;
RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL Stand. Genomic Sci. 3:304-314(2010).
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; CP002281; ADO82018.1; -; Genomic_DNA.
DR RefSeq; WP_013386689.1; NC_014632.1.
DR AlphaFoldDB; E3H9W1; -.
DR SMR; E3H9W1; -.
DR STRING; 572544.Ilyop_0229; -.
DR KEGG; ipo:Ilyop_0229; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_046586_2_3_0; -.
DR OrthoDB; 9760689at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000006875; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00835; BioC; 1.
DR InterPro; IPR011814; BioC.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR02072; BioC; 1.
DR PANTHER; PTHR43861:SF1; TRANS-ACONITATE 2-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43861; TRANS-ACONITATE 2-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..268
FT /note="Malonyl-[acyl-carrier protein] O-methyltransferase
FT 1"
FT /id="PRO_0000412505"
SQ SEQUENCE 268 AA; 31219 MW; 872304AF5F9937D7 CRC64;
MAIIDKKRVN QNFSRGAKTY DNYAQVQKHM ADKLEIFVHG SKKQYNILEV GCGTGIFSQK
ILKRFPNSKI DLLDISPAMV ETAKEKLGDS PNLNFIVEDV ENYNPEKKYD LIFSNATFQW
IDDQMRLFNH LYSLLDYGGK IAFSTFGNKT YFELRESLST LDPELKYSQK FVKLDEMTEI
TNKNFRILAA DEDFFIEKFE NVMAFLKAIK GIGSNSALSN KRNFTREKFK ALDKIYRDKF
GDKNIINVTN HLLYMVLEKV KMRDENLK
//
