ID N6XHM0_9RHOO Unreviewed; 306 AA.
AC N6XHM0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=B447_08933 {ECO:0000313|EMBL:ENO81231.1};
OS Thauera sp. 27.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO81231.1, ECO:0000313|Proteomes:UP000013140};
RN [1] {ECO:0000313|EMBL:ENO81231.1, ECO:0000313|Proteomes:UP000013140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=27 {ECO:0000313|EMBL:ENO81231.1,
RC ECO:0000313|Proteomes:UP000013140};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENO81231.1}.
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DR EMBL; AMXB01000013; ENO81231.1; -; Genomic_DNA.
DR RefSeq; WP_002938918.1; NZ_AMXB01000013.1.
DR AlphaFoldDB; N6XHM0; -.
DR eggNOG; COG2226; Bacteria.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000013140; 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 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|HAMAP-Rule:MF_00835};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835,
KW ECO:0000313|EMBL:ENO81231.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013140};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00835, ECO:0000313|EMBL:ENO81231.1}.
FT DOMAIN 56..168
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
SQ SEQUENCE 306 AA; 33375 MW; 7F4FBCA006241032 CRC64;
MSTDTAPVFA LDRALLRRRC ERAAGTVDGA DVLAREVARR MDERLDYIRI APRRILDLGC
GTGADLARLS ARFPEASVLA ADFSPAMLAR AGARTRASTG GRGLLDRLFG RHHATPLPHL
VADAAALPLA RASLSLIWSN LMLPALTDPL PVFKEAHRSL EVGGLLMFST LGPDTLRELR
ATLPTTHGER VHRFIDMHDL GDALVQAGFS DPVMDMEVLT LTYTDLDTLF ADLRACGARN
AATNRPRGLS GRSGWQAARA AYERLRKDGR LPATFEIIQG HAWKTAAKTT DDGRSIVRFQ
PRHGGR
//