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PAT_STRCO
ID   PAT_STRCO               Reviewed;         171 AA.
AC   P21861;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Phosphinothricin N-acetyltransferase {ECO:0000303|PubMed:1916276};
DE            Short=PPT N-acetyltransferase {ECO:0000303|PubMed:1916276};
DE            EC=2.3.1.183 {ECO:0000269|PubMed:1916276};
DE   AltName: Full=Phosphinothricin-resistance protein {ECO:0000305};
GN   Name=bar {ECO:0000303|PubMed:1916276}; OrderedLocusNames=SCO3203;
GN   ORFNames=SCE22.20;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=1916276; DOI=10.1016/0378-1119(91)90462-k;
RA   Bedford D.J., Lewis C.G., Buttner M.J.;
RT   "Characterization of a gene conferring bialaphos resistance in Streptomyces
RT   coelicolor A3(2).";
RL   Gene 104:39-45(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=2160942; DOI=10.1128/jb.172.6.3367-3378.1990;
RA   Buttner M.J., Chater K.F., Bibb M.J.;
RT   "Cloning, disruption, and transcriptional analysis of three RNA polymerase
RT   sigma factor genes of Streptomyces coelicolor A3(2).";
RL   J. Bacteriol. 172:3367-3378(1990).
CC   -!- FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an acetyl
CC       group from acetyl CoA. The physiological substrate could be a
CC       structurally related compound. {ECO:0000269|PubMed:1916276}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + phosphinothricin = CoA + H(+) + N-
CC         acetylphosphinothricin; Xref=Rhea:RHEA:12597, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58879,
CC         ChEBI:CHEBI:58882; EC=2.3.1.183;
CC         Evidence={ECO:0000269|PubMed:1916276};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1 mM for phosphinothricin {ECO:0000269|PubMed:1916276};
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M62753; AAA26705.1; -; Genomic_DNA.
DR   EMBL; AL939115; CAB90987.1; -; Genomic_DNA.
DR   EMBL; M37919; AAA26766.2; -; Genomic_DNA.
DR   PIR; JH0246; JH0246.
DR   PIR; T42042; T42042.
DR   RefSeq; NP_627417.1; NC_003888.3.
DR   RefSeq; WP_003975614.1; NZ_VNID01000013.1.
DR   AlphaFoldDB; P21861; -.
DR   SMR; P21861; -.
DR   STRING; 100226.SCO3203; -.
DR   GeneID; 1098637; -.
DR   KEGG; sco:SCO3203; -.
DR   PATRIC; fig|100226.15.peg.3263; -.
DR   eggNOG; COG1247; Bacteria.
DR   HOGENOM; CLU_013985_4_2_11; -.
DR   InParanoid; P21861; -.
DR   OMA; IFAHNQP; -.
DR   PhylomeDB; P21861; -.
DR   SABIO-RK; P21861; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0102971; F:phosphinothricin N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic resistance; Herbicide resistance;
KW   Reference proteome; Transferase.
FT   CHAIN           1..171
FT                   /note="Phosphinothricin N-acetyltransferase"
FT                   /id="PRO_0000074573"
FT   DOMAIN          7..171
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         94..96
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT   BINDING         102..107
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT   BINDING         133
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
SQ   SEQUENCE   171 AA;  19205 MW;  70146721ACD5731E CRC64;
     MPGTAEVQVR PGVEEDLKPL TDLYNHYVRE TPITFDTEPF TPEERRPWLL SHPEDGPYRL
     RVATDAESQE ILGYATSSPY RAKPAYATSV ETTVYVAPGA GGRGIGSLLY ASLFDALAAE
     DLHRAYAGIA QPNEASARLH ARFGFRHVGT YREVGRKFGR YWDVAWYERP L
 
 
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