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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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