PAT_STRHY
ID PAT_STRHY Reviewed; 183 AA.
AC P16426; P72461;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phosphinothricin N-acetyltransferase {ECO:0000303|PubMed:16453790};
DE Short=PPT N-acetyltransferase {ECO:0000303|PubMed:16453790};
DE EC=2.3.1.183 {ECO:0000269|PubMed:16453790};
DE AltName: Full=Phosphinothricin-resistance protein {ECO:0000305};
GN Name=bar {ECO:0000303|PubMed:16453790};
OS Streptomyces hygroscopicus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1912;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX PubMed=2315036; DOI=10.1093/nar/18.4.1062;
RA White J., Chang S.-Y.P., Bibb M.J., Bibb M.J.;
RT "A cassette containing the bar gene of Streptomyces hygroscopicus: a
RT selectable marker for plant transformation.";
RL Nucleic Acids Res. 18:1062-1062(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-12, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16453790; DOI=10.1002/j.1460-2075.1987.tb02538.x;
RA Thompson C.J., Movva N.R., Tizard R., Crameri R., Davies J.E.,
RA Lauwereys M., Botterman J.;
RT "Characterization of the herbicide-resistance gene bar from Streptomyces
RT hygroscopicus.";
RL EMBO J. 6:2519-2523(1987).
CC -!- FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an acetyl
CC group from acetyl CoA. Can also acetylate demethylphosphinothricin but
CC not PTT or glutamate. This enzyme is an effector of phosphinothricin
CC tripeptide (PTT or bialaphos) resistance.
CC {ECO:0000269|PubMed:16453790}.
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:16453790};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for phosphinothricin {ECO:0000269|PubMed:16453790};
CC KM=2 mM for demethylphosphinothricin {ECO:0000269|PubMed:16453790};
CC KM=36 mM for methionine sulfoximine {ECO:0000269|PubMed:16453790};
CC KM=56 mM for hydroxylysine {ECO:0000269|PubMed:16453790};
CC KM=240 mM for glutamate {ECO:0000269|PubMed:16453790};
CC -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
CC glufosinate-tolerant maize by Dekalb Genetics.
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; X17220; CAA35093.1; -; Genomic_DNA.
DR EMBL; X05822; CAA29262.1; -; Genomic_DNA.
DR PIR; S08615; S08615.
DR PDB; 5T7D; X-ray; 1.40 A; A/B/C/D=1-183.
DR PDB; 5T7E; X-ray; 1.80 A; A/B/C/D=1-183.
DR PDBsum; 5T7D; -.
DR PDBsum; 5T7E; -.
DR AlphaFoldDB; P16426; -.
DR SMR; P16426; -.
DR KEGG; ag:CAA35093; -.
DR BRENDA; 2.3.1.183; 6043.
DR SABIO-RK; P16426; -.
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 3D-structure; Acyltransferase; Antibiotic resistance;
KW Direct protein sequencing; Genetically modified food; Herbicide resistance;
KW Transferase.
FT CHAIN 1..183
FT /note="Phosphinothricin N-acetyltransferase"
FT /id="PRO_0000074574"
FT DOMAIN 8..173
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"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:5T7D"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:5T7D"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:5T7D"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5T7D"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:5T7D"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5T7D"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5T7D"
FT STRAND 67..80
FT /evidence="ECO:0007829|PDB:5T7D"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5T7D"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:5T7D"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5T7D"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:5T7D"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:5T7D"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:5T7D"
FT STRAND 143..154
FT /evidence="ECO:0007829|PDB:5T7D"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:5T7D"
SQ SEQUENCE 183 AA; 20637 MW; 1FBC2E1E876239F0 CRC64;
MSPERRPADI RRATEADMPA VCTIVNHYIE TSTVNFRTEP QEPQEWTDDL VRLRERYPWL
VAEVDGEVAG IAYAGPWKAR NAYDWTAEST VYVSPRHQRT GLGSTLYTHL LKSLEAQGFK
SVVAVIGLPN DPSVRMHEAL GYAPRGMLRA AGFKHGNWHD VGFWQLDFSL PVPPRPVLPV
TEI
