ID BIOC2_ILYPC Reviewed; 259 AA.
AC E3HCT1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Ilyop_2721;
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OG Plasmid pILYOP01.
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; CP002282; ADO84476.1; -; Genomic_DNA.
DR RefSeq; WP_013389130.1; NC_014633.1.
DR AlphaFoldDB; E3HCT1; -.
DR SMR; E3HCT1; -.
DR KEGG; ipo:Ilyop_2721; -.
DR HOGENOM; CLU_046586_2_3_0; -.
DR OrthoDB; 9760689at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000006875; Plasmid pILYOP01.
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; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR02072; BioC; 1.
DR PANTHER; PTHR13090:SF1; ARGININE-HYDROXYLASE NDUFAF5, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13090; UNCHARACTERIZED; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Methyltransferase; Plasmid; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..259
FT /note="Malonyl-[acyl-carrier protein] O-methyltransferase
FT 2"
FT /id="PRO_0000412506"
SQ SEQUENCE 259 AA; 30192 MW; 0F0152F4F06DB256 CRC64;
MIDKKKVNRN FSKGAKTYDE YALIQRHMAD KLGIFIEDSE EVFNILEIGC GTGIFSEKIL
NKFPNSNIDF LDISHDMIKN VKDKIGSKEN LNFIVEDIEK YQPQKKYDLI FSNATFQWIQ
NKKGLFDHLD SFLKPGGLIL FSTFGKDTYF ELRESLKSID PDLEYSQNFI SLEDLKKVLD
DKYKILAAEE ERIKENYHCV MDFLKMIKGI GANSALSNSK PFTRDKFNRL EDEYRKNYCS
GDSIEVTNHL IYMILGKNY
//
