BIOC_HAEDU
ID BIOC_HAEDU Reviewed; 258 AA.
AC Q7VL11;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835};
DE Short=Malonyl-ACP O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835};
DE EC=2.1.1.197 {ECO:0000255|HAMAP-Rule:MF_00835};
DE AltName: Full=Biotin synthesis protein BioC {ECO:0000255|HAMAP-Rule:MF_00835};
GN Name=bioC {ECO:0000255|HAMAP-Rule:MF_00835}; OrderedLocusNames=HD_1681;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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:0000255|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:0000255|HAMAP-Rule:MF_00835};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00835}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00835}.
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DR EMBL; AE017143; AAP96448.1; -; Genomic_DNA.
DR RefSeq; WP_010945480.1; NC_002940.2.
DR AlphaFoldDB; Q7VL11; -.
DR SMR; Q7VL11; -.
DR STRING; 233412.HD_1681; -.
DR DNASU; 1491540; -.
DR EnsemblBacteria; AAP96448; AAP96448; HD_1681.
DR KEGG; hdu:HD_1681; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_046586_1_0_6; -.
DR OMA; SADYWLF; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001022; 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:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00835; BioC; 1.
DR InterPro; IPR011814; BioC.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02072; BioC; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..258
FT /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT /id="PRO_0000412500"
SQ SEQUENCE 258 AA; 29501 MW; 241782017A908EBE CRC64;
MAKLAKQLIA KRFVSHLTEY DQYAIAQQQI NHQLVDLLQA NTDKTFQRAL EIGCGTGNLT
EKLLAKIPIE HLTLNDFNAI YYPTVLQKIK QKKPLVVVDF MQGDAEQLVF TRNFDLVSAA
SVVQWFDSPQ QFLRNSAYAL KPGGVVLFNS FSPLNLQEIR QLTGIGLNYP TRLQWQEWLA
QDFEQCQLIE QPIKLTFDSP LAVLIHLKKT GVTAVSNKPW NRHQIKQFCM EYQAHFACEQ
GVYLTYTPIL MLGIKKNG