ID   PAT_STRVT               Reviewed;         183 AA.
AC   Q57146;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Phosphinothricin N-acetyltransferase {ECO:0000303|PubMed:3240868};
DE            Short=PPT N-acetyltransferase {ECO:0000305};
DE            EC=2.3.1.183 {ECO:0000269|PubMed:3290054};
DE   AltName: Full=Phosphinothricin-resistance protein {ECO:0000305};
GN   Name=pat {ECO:0000303|PubMed:3240868};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=591159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=3240868; DOI=10.1016/0378-1119(88)90101-1;
RA   Wohlleben W., Arnold W., Broer I., Hillemann D., Strauch E., Puehler A.;
RT   "Nucleotide sequence of the phosphinothricin N-acetyltransferase gene from
RT   Streptomyces viridochromogenes Tu494 and its expression in Nicotiana
RT   tabacum.";
RL   Gene 70:25-37(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=8593056; DOI=10.1128/aem.62.2.570-577.1996;
RA   Schwartz D., Alijah R., Nussbaumer B., Pelzer S., Wohlleben W.;
RT   "The peptide synthetase gene phsA from Streptomyces viridochromogenes is
RT   not juxtaposed with other genes involved in nonribosomal biosynthesis of
RT   peptides.";
RL   Appl. Environ. Microbiol. 62:570-577(1996).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=3290054; DOI=10.1016/0378-1119(88)90546-x;
RA   Strauch E., Wohlleben W., Puehler A.;
RT   "Cloning of a phosphinothricin N-acetyltransferase gene from Streptomyces
RT   viridochromogenes Tue494 and its expression in Streptomyces lividans and
RT   Escherichia coli.";
RL   Gene 63:65-74(1988).
CC   -!- FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an acetyl
CC       group from acetyl CoA. This enzyme is an effector of phosphinothricin
CC       tripeptide (PTT or bialaphos) resistance. {ECO:0000269|PubMed:3290054}.
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:3290054};
CC   -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
CC       glufosinate-tolerant canola and maize by Agrevo.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X65195; CAA46314.1; -; Genomic_DNA.
DR   EMBL; M22827; AAA72709.1; -; Genomic_DNA.
DR   PIR; JT0409; JT0409.
DR   RefSeq; WP_003988626.1; NZ_GG657757.1.
DR   AlphaFoldDB; Q57146; -.
DR   SMR; Q57146; -.
DR   STRING; 591159.ACEZ01000045_gene2938; -.
DR   eggNOG; COG1247; Bacteria.
DR   OrthoDB; 1809950at2; -.
DR   BioCyc; MetaCyc:MON-15056; -.
DR   BRENDA; 2.3.1.183; 6116.
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; Genetically modified food;
KW   Herbicide resistance; Transferase.
FT   CHAIN           1..183
FT                   /note="Phosphinothricin N-acetyltransferase"
FT                   /id="PRO_0000074575"
FT   DOMAIN          8..169
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         91..93
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT   BINDING         99..104
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT   BINDING         130
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
SQ   SEQUENCE   183 AA;  20618 MW;  AF8B9C1914D8A553 CRC64;
     MSPERRPVEI RPATAADMAA VCDIVNHYIE TSTVNFRTEP QTPQEWIDDL ERLQDRYPWL
     VAEVEGVVAG IAYAGPWKAR NAYDWTVEST VYVSHRHQRL GLGSTLYTHL LKSMEAQGFK
     SVVAVIGLPN DPSVRLHEAL GYTARGTLRA AGYKHGGWHD VGFWQRDFEL PAPPRPVRPV
     TQI