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BIOC_SHEON
ID   BIOC_SHEON              Reviewed;         275 AA.
AC   Q8EDK8;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=SO_2738;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55766.1; -; Genomic_DNA.
DR   RefSeq; NP_718322.1; NC_004347.2.
DR   RefSeq; WP_011072677.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EDK8; -.
DR   SMR; Q8EDK8; -.
DR   STRING; 211586.SO_2738; -.
DR   PaxDb; Q8EDK8; -.
DR   DNASU; 1170436; -.
DR   KEGG; son:SO_2738; -.
DR   PATRIC; fig|211586.12.peg.2637; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_2_2_6; -.
DR   OMA; SWQAVDG; -.
DR   OrthoDB; 1664438at2; -.
DR   PhylomeDB; Q8EDK8; -.
DR   BioCyc; SONE211586:G1GMP-2517-MON; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000008186; 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:0008168; F:methyltransferase activity; IBA:GO_Central.
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..275
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000412523"
SQ   SEQUENCE   275 AA;  30069 MW;  6FEBFCFEEF0880DB CRC64;
     MSMPLGVSVN SHQSASQVEH IADRFSAAAK HYQEHNCLQR LSGASLLQGF VAKGAILDIG
     AGPGTDFANR AMGEEMRVYA LDIALGMLQQ LKTIYPEHQC VCGNAEQLPF VDRSIDCIYS
     NLALQWCHDF SAATSEMARV LKSGGEAHLS IVAAGSLAQL SNLGLRVNGF LSLESLQAAF
     DDTDWQFLDV KLMPMTVYFQ DLKALLYSIK GVGASVQSSV QTVTSSESDA HFGKLRGRHD
     WQALQQRAEQ FREAQGLPLT YQIAQFRVRR QGGSV
 
 
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