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BIOC1_COXBU
ID   BIOC1_COXBU             Reviewed;         282 AA.
AC   Q83E64;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00835};
DE            Short=Malonyl-ACP O-methyltransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00835};
GN   Name=bioC1 {ECO:0000255|HAMAP-Rule:MF_00835}; OrderedLocusNames=CBU_0467;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90016.1; -; Genomic_DNA.
DR   RefSeq; NP_819502.1; NC_002971.3.
DR   RefSeq; WP_010957596.1; NC_002971.4.
DR   AlphaFoldDB; Q83E64; -.
DR   SMR; Q83E64; -.
DR   STRING; 227377.CBU_0467; -.
DR   EnsemblBacteria; AAO90016; AAO90016; CBU_0467.
DR   GeneID; 1208351; -.
DR   KEGG; cbu:CBU_0467; -.
DR   PATRIC; fig|227377.7.peg.457; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_2_1_6; -.
DR   OMA; PSMWELM; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002671; 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..282
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase
FT                   1"
FT                   /id="PRO_0000412491"
SQ   SEQUENCE   282 AA;  31709 MW;  23ED44FE6266B879 CRC64;
     MPKTQFQVDQ NAVKKALHAA ARTYDNVGMV PKAIADRLLE RLDFIRLNPL CVVDVGARTG
     YATQQLEERY REAIVVGLDF SVAILKAASS KMMVGEYTAL PFADRSVDLI FSNLAFQWSS
     DLQQTLQECH RVLKPGGLLL FSTVGPDTLK ELHSSFADGH RHVHPFYDMH DIGDMLTQLR
     FTDPVMDTER LIVHYSSVPQ LIKDLKQLGA QNASQDRLKG LMGKTQWRQM LTNYENCREE
     NGALPATVEV IYGHAFGTES NSFKNANGEE VTVPIDKIIR RN
 
 
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