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Database: UniProt
Entry: Q87QN4_VIBPA
LinkDB: Q87QN4_VIBPA
Original site: Q87QN4_VIBPA 
ID   Q87QN4_VIBPA            Unreviewed;       268 AA.
AC   Q87QN4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=VP1115 {ECO:0000313|EMBL:BAC59378.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59378.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC59378.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC59378.1; -; Genomic_DNA.
DR   RefSeq; NP_797494.1; NC_004603.1.
DR   RefSeq; WP_005460024.1; NC_004603.1.
DR   AlphaFoldDB; Q87QN4; -.
DR   GeneID; 1188620; -.
DR   KEGG; vpa:VP1115; -.
DR   PATRIC; fig|223926.6.peg.1057; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_2_2_6; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002493; Chromosome 1.
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:UP000002493};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00835}.
FT   DOMAIN          58..148
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
SQ   SEQUENCE   268 AA;  29981 MW;  BB3ED5B826C12917 CRC64;
     MDNAENMVLD NVHQDKEAIA SSFGKAADTY DKHAAFQRDV GHRLLEKLPS DLTNKRVLDL
     GCGTGYFSQL LLERGASVVC ADLSQGMLDK ARERCGDHNV RYVVADAESL PFEDASFDYV
     FSSLALQWCV DLSYPLREIR RILAANGKGC FSTLVDGSLC ELRYSWAKID TYQHVNNFIT
     LNQVKIALAQ SRCHNHHLDS TTITVWYDSA FSVMRDLKGI GANHVSGRSH GLTSRRTLLQ
     VERAYQAFKN DQGLLPATYQ VCFGVIHL
//
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