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Database: UniProt
Entry: Q2T1G7_BURTA
LinkDB: Q2T1G7_BURTA
Original site: Q2T1G7_BURTA 
ID   Q2T1G7_BURTA            Unreviewed;       338 AA.
AC   Q2T1G7;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
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   OrderedLocusNames=BTH_I0424 {ECO:0000313|EMBL:ABC37246.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC37246.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC37246.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC37246.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2T1G7; -.
DR   KEGG; bte:BTH_I0424; -.
DR   HOGENOM; CLU_046586_2_1_4; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001930; Chromosome I.
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   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|HAMAP-Rule:MF_00835};
KW   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          75..188
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
SQ   SEQUENCE   338 AA;  37407 MW;  757B84AD72946AE6 CRC64;
     MARSERVYFG LFASVPDMSP ASAKTGRPAY DPRRLRRIFD RRAAAFDAVS FLPREIAQRM
     RERLDYIKVN PSGVLDAGCG TGDDLPLLRA RFPEAPVFGV DASGGMLARA AARDTVETSW
     RRFLPATLTK ALGHRGPRVA QADFSALPFA SDAFDLLWSN FALHWHARPD LVFPEWHRVL
     RVDGLLMFST LGPDTLRELR AACADAAAAT GDTRAVARVI DFVDMHDLGD MLVESGFEIP
     VMDQETLTVT YKSAGSLLAD VRRLGAYPFE REASGHASRR LHAALHDALE ARRRDDGTIP
     LTYEVIYGHA WKAAPRMTAE GFSIVRVQDI GKGRPKRS
//
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