ID N9GFD5_ACIHA Unreviewed; 252 AA.
AC N9GFD5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=F927_01653 {ECO:0000313|EMBL:ENW18215.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW18215.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW18215.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW18215.1,
RC ECO:0000313|Proteomes:UP000017667};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENW18215.1}.
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DR EMBL; APQQ01000020; ENW18215.1; -; Genomic_DNA.
DR RefSeq; WP_005081439.1; NZ_KB849800.1.
DR AlphaFoldDB; N9GFD5; -.
DR PATRIC; fig|1217659.3.peg.1622; -.
DR HOGENOM; CLU_046586_1_0_6; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000017667; 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; 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 {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW Rule:MF_00835}; Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00835}.
SQ SEQUENCE 252 AA; 29112 MW; 40465C9C7691AB88 CRC64;
MFVSVDKALV AQRFAKAGQS YIEHAVVQKQ ISAQLFEYLK AYCPKTFDSV LEIGCGSGNL
THLFQTHFQF DQLFLNDLYK DVDQHFSTIQ NIAWLIGDIE QLELPSELDA MISSSALQWM
TDLPALLQRI HDALKPKAYL GFSTFGENNL IEIKKLTGQG LNYYSSEVLK QKLEENGFEI
VFIQEEQKHL YFDDPKLVLH HLKATGVTAT AKSHRWTKQS LLQFYSDYQQ FHDEHGFRLT
YHPIYVIARR KA
//
