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Database: UniProt
Entry: G7UTG8_PSEUP
LinkDB: G7UTG8_PSEUP
Original site: G7UTG8_PSEUP 
ID   G7UTG8_PSEUP            Unreviewed;       300 AA.
AC   G7UTG8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=DSC_01080 {ECO:0000313|EMBL:AER54869.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER54869.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER54869.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER54869.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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; CP003093; AER54869.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7UTG8; -.
DR   STRING; 1045855.DSC_01080; -.
DR   KEGG; psd:DSC_01080; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_2_1_6; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000005870; 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   Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00835}.
FT   DOMAIN          56..152
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
SQ   SEQUENCE   300 AA;  33054 MW;  FC62650FA876FA7F CRC64;
     MADNGAMPMF DSRQIRRAFS RSATTYADAA VLHHEVEKRL LESLDYLGQR VPQVVLDVGS
     GPATAAAQMR KRWPRAQVIA LDLALPMLRQ ARKQAGWWKP FARVAADARA LPLAEHSADV
     LFCNLCLPWL EDLPAVFAGF RRVLKPDGLL LCSTFGPQTL IELRQAFAAD PAPHVSPFAP
     IAQFGDALMR SGFRDPVLDR DQFTLTYPDL PALMAELRAI GATNALSMRR ASLTGRSRFA
     DAAQAYEPLR TAEGRLPSTW EVLYAHAWAP QAGTPIREDG HDVAAVPLSR IPIRRRSTPA
//
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