BIOC_HAMD5
ID BIOC_HAMD5 Reviewed; 258 AA.
AC C4K5L7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=HDEF_1201;
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX NCBI_TaxID=572265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT;
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ67860.1; -; Genomic_DNA.
DR RefSeq; WP_015873654.1; NC_012751.1.
DR AlphaFoldDB; C4K5L7; -.
DR SMR; C4K5L7; -.
DR STRING; 572265.HDEF_1201; -.
DR EnsemblBacteria; ACQ67860; ACQ67860; HDEF_1201.
DR GeneID; 66260915; -.
DR KEGG; hde:HDEF_1201; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_046586_2_2_6; -.
DR OMA; SWQAVDG; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002334; 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_0000412503"
SQ SEQUENCE 258 AA; 29323 MW; DE227DB12C88BE65 CRC64;
MISKNFFIES VNKTAIASAF SRAAHSYEQA ASLQKEVGFR LLQMTGDIKK SWVLDAGCGT
GYFSQFWRQK GNRVLSLDLS FEMLKKAKKK SAAQAYLLAD IEHLPILDQK IDLCFSNMAI
QWCDDLKVVL AEFHRVTRSG GVILFSTLAM GSLKELAQAW QKVDEEPHIN RFLSFEEIQQ
ICTPYHSELK MCLSKVCFPD LRSLIQSLRG VGATHLHRGR KVGLSSRARI QKLENAYPVK
FGEYPLSYQL VYGIIYRD
