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BIOC_BACT6
ID   BIOC_BACT6              Reviewed;         274 AA.
AC   E6SRF9;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 54.
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=Bache_2091;
OS   Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG
OS   15421 / P 36-108).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=693979;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108;
RX   PubMed=21475586; DOI=10.4056/sigs.1513795;
RA   Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brambilla E.,
RA   Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT   "Complete genome sequence of Bacteroides helcogenes type strain (P 36-
RT   108).";
RL   Stand. Genomic Sci. 4:45-53(2011).
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; CP002352; ADV44062.1; -; Genomic_DNA.
DR   RefSeq; WP_013547655.1; NC_014933.1.
DR   AlphaFoldDB; E6SRF9; -.
DR   SMR; E6SRF9; -.
DR   STRING; 693979.Bache_2091; -.
DR   EnsemblBacteria; ADV44062; ADV44062; Bache_2091.
DR   KEGG; bhl:Bache_2091; -.
DR   PATRIC; fig|693979.3.peg.2201; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_046586_1_0_10; -.
DR   OMA; SADYWLF; -.
DR   OrthoDB; 1664438at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000008630; 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..274
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000412484"
SQ   SEQUENCE   274 AA;  31152 MW;  8DA853F334472680 CRC64;
     MDKQLIAERF AKARNTYTRE ALVQQQVAGK MIRILTDVLS SAEHLLPEEI AVRFRHIVEF
     GCGTGSYSRI LLHTLHPETL LLNDLCREME ECVGELCSTQ TAGRKKDGTE IRVSFLPGDA
     ENFDFPKGTD LITSCSTLQW FNNPETFFLR CHHALTKDGI LAFSTFGTKN MHQIRCLTGH
     GLYYLPIEEL QALLSPYFNI LHAEEEIVPL SFATPQAVLK HLKQTGVTGT EKRMWTRGRL
     QAFCEEYIRQ FSSPPTGNVT LTYHPIYIIA KNKE
 
 
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