ID A0A1H2W7K6_9BACL Unreviewed; 281 AA.
AC A0A1H2W7K6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835};
DE Short=Malonyl-ACP O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835};
DE EC=2.1.1.197 {ECO:0000256|HAMAP-Rule:MF_00835};
DE AltName: Full=Biotin synthesis protein BioC {ECO:0000256|HAMAP-Rule:MF_00835};
GN Name=bioC {ECO:0000256|HAMAP-Rule:MF_00835};
GN ORFNames=SAMN05444487_10642 {ECO:0000313|EMBL:SDW76570.1};
OS Marininema mesophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDW76570.1, ECO:0000313|Proteomes:UP000198534};
RN [1] {ECO:0000313|EMBL:SDW76570.1, ECO:0000313|Proteomes:UP000198534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45610 {ECO:0000313|EMBL:SDW76570.1,
RC ECO:0000313|Proteomes:UP000198534};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00835};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00835}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00835}.
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DR EMBL; FNNQ01000006; SDW76570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2W7K6; -.
DR STRING; 1048340.SAMN05444487_10642; -.
DR OrthoDB; 9760689at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000198534; Unassembled WGS sequence.
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; IPR025714; Methyltranfer_dom.
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; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00835};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835,
KW ECO:0000313|EMBL:SDW76570.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198534};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00835, ECO:0000313|EMBL:SDW76570.1}.
FT DOMAIN 54..170
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
SQ SEQUENCE 281 AA; 32388 MW; E370D8243409B0F9 CRC64;
MGVIRSGMDV EKEKELIARQ FNRFADEYDR VAVVQQRMAH RILETLDEQG AEPQNILEIG
CGTGYLTQLL GEKYPDAKFT IIDIAEKMME LTKRRANESL DVRFVVGDVE NESWEPESFD
LIASNAMVHW LARPDSTLCQ LSSALKPGGG FVASTFGPDT LGELDQVYQN LGLNEEYSTQ
RRYYFQPPEE WYRMMKMADL EGDYVVCWHR IHYPDSNSLM NAIQRMGADY IHPEEEQLYG
QSQLVRAVIQ EQYNRIYRTR EGGVYATYQS VYAYGRKGLP T
//
