ID A0A1H4GM43_9GAMM Unreviewed; 289 AA.
AC A0A1H4GM43;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=SAMN05660964_03576 {ECO:0000313|EMBL:SEB10644.1};
OS Thiothrix caldifontis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=525918 {ECO:0000313|EMBL:SEB10644.1, ECO:0000313|Proteomes:UP000199397};
RN [1] {ECO:0000313|EMBL:SEB10644.1, ECO:0000313|Proteomes:UP000199397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21228 {ECO:0000313|EMBL:SEB10644.1,
RC ECO:0000313|Proteomes:UP000199397};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNQP01000036; SEB10644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4GM43; -.
DR STRING; 525918.SAMN05660964_03576; -.
DR OrthoDB; 9760689at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000199397; Unassembled WGS sequence.
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};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835,
KW ECO:0000313|EMBL:SEB10644.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199397};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00835, ECO:0000313|EMBL:SEB10644.1}.
FT DOMAIN 55..151
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
SQ SEQUENCE 289 AA; 32612 MW; C847AF4A35EA84D5 CRC64;
MHSDTNPHLL DKRKTRQGFE RAAHTYDANA VLQREIGERL LERLDFIKMQ PETVLDLGCG
TGAISEHLLK RYKKARIIGV DLAVNMVQKT RQRGGWFRKP QGVCADANHL PFQSQCADML
LSNLMLQWCN DLPAVFGEWV QVLKPNGLLM FATFGPDTLK ELRASWGRVD GFTHASQFVD
MHDVGDALLQ AGFRDPVVDM ETITLTYTDV RGLLRDLKGI GANNATQGRN HGLTGKAHLQ
AFLQAYEYFR QENGLYPATY EVVYGHAWAP MLLPSKLPEK FIPIMRSKS
//