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Database: UniProt
Entry: Q731I1_BACC1
LinkDB: Q731I1_BACC1
Original site: Q731I1_BACC1 
ID   Q731I1_BACC1            Unreviewed;       269 AA.
AC   Q731I1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 117.
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   OrderedLocusNames=BCE_4185 {ECO:0000313|EMBL:AAS43086.1};
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS43086.1, ECO:0000313|Proteomes:UP000002527};
RN   [1] {ECO:0000313|EMBL:AAS43086.1, ECO:0000313|Proteomes:UP000002527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA   Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43086.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q731I1; -.
DR   DNASU; 2752745; -.
DR   KEGG; bca:BCE_4185; -.
DR   HOGENOM; CLU_046586_2_3_9; -.
DR   OMA; SWQAVDG; -.
DR   BRENDA; 2.1.1.197; 648.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002527; 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; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR02072; BioC; 1.
DR   PANTHER; PTHR43861:SF1; TRANS-ACONITATE 2-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43861; TRANS-ACONITATE 2-METHYLTRANSFERASE-RELATED; 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   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00835}.
FT   DOMAIN          43..162
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
SQ   SEQUENCE   269 AA;  31171 MW;  81B3B1D86413E8E6 CRC64;
     MINKTLLQKR FNVAAVSYDQ YANVQKKMAH SLLSTLNRRY STNSSIRILE LGCGTGYVTE
     QLSNLFPKAQ ITAIDFAESM IAVAKTRQNV NNVTFYCEDI ERLRLEETYD VIISNATFQW
     LNDLKQVITN LFRHLSIEGI LLFSTFGQET FQELHASFQR AKEEKNIQNE TSIGQRFYSK
     NQLRHICEIE TGDVHVSETC YIERFTEVRE FLHSIRKVGA TNSNEESYCQ SPSLFRAMLR
     IYERDFTGNE GIMATYHALF VHITKEGKR
//
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