BIOC_HAHCH
ID BIOC_HAHCH Reviewed; 279 AA.
AC Q2SBD7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=HCH_05368;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC32037.1; -; Genomic_DNA.
DR RefSeq; WP_011399101.1; NC_007645.1.
DR AlphaFoldDB; Q2SBD7; -.
DR SMR; Q2SBD7; -.
DR STRING; 349521.HCH_05368; -.
DR EnsemblBacteria; ABC32037; ABC32037; HCH_05368.
DR KEGG; hch:HCH_05368; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_046586_2_2_6; -.
DR OMA; SWQAVDG; -.
DR OrthoDB; 1664438at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000238; 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..279
FT /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT /id="PRO_0000412501"
SQ SEQUENCE 279 AA; 30783 MW; 5D1A3E87AA3C97EA CRC64;
MNHAVTIKSF VSTSPLSDLE RGAVDKSKVA ESFSAAAATY DLLAGMQKEV GESLVSLSRE
GCPQDIIDVG CGTGWLTHRL KNSFPEARLC AYDLSPGMIE YALAHHDNVA EIWAVADMES
LPVANASQDL VFSNMAMQWL DDPRAWFAEA SRVLRPGGRL ICSTLLTQTL FELEQAWHGV
DGGRHVNRFL SAEQVAEAAV SCGLRGECRE SLYVRFHDSA LDVMKELKGI GAHNIQSERP
QGLTGKRRLR RVIENYEKCR QEQGVPATYH VGVCVYSRI