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Database: UniProt
Entry: B2VBX2_ERWT9
LinkDB: B2VBX2_ERWT9
Original site: B2VBX2_ERWT9 
ID   B2VBX2_ERWT9            Unreviewed;       250 AA.
AC   B2VBX2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
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:CAO97310.1};
GN   OrderedLocusNames=ETA_22640 {ECO:0000313|EMBL:CAO97310.1};
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO97310.1, ECO:0000313|Proteomes:UP000001726};
RN   [1] {ECO:0000313|EMBL:CAO97310.1, ECO:0000313|Proteomes:UP000001726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC   {ECO:0000313|Proteomes:UP000001726};
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(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; CU468135; CAO97310.1; -; Genomic_DNA.
DR   RefSeq; WP_012441979.1; NC_010694.1.
DR   AlphaFoldDB; B2VBX2; -.
DR   STRING; 465817.ETA_22640; -.
DR   KEGG; eta:ETA_22640; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_2_2_6; -.
DR   OrthoDB; 9760689at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001726; 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; PTHR43464:SF95; MALONYL-[ACYL-CARRIER PROTEIN] O-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43464; METHYLTRANSFERASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000001726};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00835}.
FT   DOMAIN          48..139
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
SQ   SEQUENCE   250 AA;  27741 MW;  2239DF20D55A6C8C CRC64;
     MQQTVNKRAI AAAFGRAARS YNQHAELQRQ CGERLLAHAR PGDALRVLDA GCGTGWFSQR
     WRADGHRVTA LDLSEKMLQQ ARDNQAADDY HTGDIEALPF ADASFDRCWS NLAVQWCSSL
     PLALRELRRV TKPGGQVLFS TLTEGSLNEV RAAWQHLGRS APLNHFASLP VIERAADGMT
     LASYTLTLAF PDVLSALRSL KGIGATHLHQ GRSESMMSRR DVQQLEQVWR RDARGCLLSY
     QLVSGVIECE
//
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