ID B0BPM2_ACTPJ Unreviewed; 256 AA.
AC B0BPM2;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000256|ARBA:ARBA00012327, 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|ARBA:ARBA00012327, 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 ECO:0000313|EMBL:ABY69507.1};
GN OrderedLocusNames=APJL_0949 {ECO:0000313|EMBL:ABY69507.1};
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271 {ECO:0000313|EMBL:ABY69507.1, ECO:0000313|Proteomes:UP000008547};
RN [1] {ECO:0000313|EMBL:ABY69507.1, ECO:0000313|Proteomes:UP000008547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03 {ECO:0000313|EMBL:ABY69507.1,
RC ECO:0000313|Proteomes:UP000008547};
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
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|ARBA:ARBA00000852, ECO:0000256|HAMAP-
CC Rule:MF_00835};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746, 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; CP000687; ABY69507.1; -; Genomic_DNA.
DR RefSeq; WP_012263027.1; NC_010278.1.
DR AlphaFoldDB; B0BPM2; -.
DR KEGG; apj:APJL_0949; -.
DR HOGENOM; CLU_046586_1_0_6; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000008547; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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; IPR013216; Methyltransf_11.
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; PF08241; Methyltransf_11; 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}.
FT DOMAIN 50..148
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
SQ SEQUENCE 256 AA; 29259 MW; 1786BA6313DF0CB9 CRC64;
MAELDKPLIA QRFAAHITEY DEHAIAQQQI NRQLVNLLAQ TNKQCFRRVL EIGCGTGDLT
QHLMREYQVE HLAVNDLSNV YQDCVVQKID ENRPLISFKF IAGDAEHLAF DGQFDLISSA
SAVQWFEQPQ TFVSQAAKLL QPNGVLLFNS FTTENLAEIR ELTGVGLTYP SPADWHFWLS
KDFTQLQIMQ RQIRLTFASP LAVLQHLRKT GVTAISTQTW TRKKLMEFSE QYQAQFSCEQ
GVYLTYAPIF ILGVKK
//
