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Phosphinothricin N-acetyltransferase (PPT N-acetyltransferase) (EC 2.3.1.183) (Phosphinothricin-resistance protein)

 PAT_STRHY               Reviewed;         183 AA.
P16426; P72461;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
20-JUN-2018, entry version 79.
RecName: Full=Phosphinothricin N-acetyltransferase {ECO:0000303|PubMed:16453790};
Short=PPT N-acetyltransferase {ECO:0000303|PubMed:16453790};
EC=2.3.1.183 {ECO:0000269|PubMed:16453790};
AltName: Full=Phosphinothricin-resistance protein {ECO:0000305};
Name=bar {ECO:0000303|PubMed:16453790};
Streptomyces hygroscopicus.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1912;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
PubMed=2315036; DOI=10.1093/nar/18.4.1062;
White J., Chang S.-Y.P., Bibb M.J., Bibb M.J.;
"A cassette containing the bar gene of Streptomyces hygroscopicus: a
selectable marker for plant transformation.";
Nucleic Acids Res. 18:1062-1062(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-12, FUNCTION,
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16453790;
Thompson C.J., Movva N.R., Tizard R., Crameri R., Davies J.E.,
Lauwereys M., Botterman J.;
"Characterization of the herbicide-resistance gene bar from
Streptomyces hygroscopicus.";
EMBO J. 6:2519-2523(1987).
-!- FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an
acetyl group from acetyl CoA. Can also acetylate
demethylphosphinothricin but not PTT or glutamate. This enzyme is
an effector of phosphinothricin tripeptide (PTT or bialaphos)
resistance. {ECO:0000269|PubMed:16453790}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + phosphinothricin = CoA + N-
acetylphosphinothricin. {ECO:0000269|PubMed:16453790}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.06 mM for phosphinothricin {ECO:0000269|PubMed:16453790};
KM=2 mM for demethylphosphinothricin
{ECO:0000269|PubMed:16453790};
KM=36 mM for methionine sulfoximine
{ECO:0000269|PubMed:16453790};
KM=56 mM for hydroxylysine {ECO:0000269|PubMed:16453790};
KM=240 mM for glutamate {ECO:0000269|PubMed:16453790};
-!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
glufosinate-tolerant maize by Dekalb Genetics.
-!- SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR
subfamily. {ECO:0000305}.
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EMBL; X17220; CAA35093.1; -; Genomic_DNA.
EMBL; X05822; CAA29262.1; -; Genomic_DNA.
PIR; S08615; S08615.
PDB; 5T7D; X-ray; 1.40 A; A/B/C/D=1-183.
PDB; 5T7E; X-ray; 1.80 A; A/B/C/D=1-183.
PDBsum; 5T7D; -.
PDBsum; 5T7E; -.
ProteinModelPortal; P16426; -.
SMR; P16426; -.
PRIDE; P16426; -.
BRENDA; 2.3.1.183; 6043.
SABIO-RK; P16426; -.
GO; GO:0102971; F:phosphinothricin N-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Antibiotic resistance;
Direct protein sequencing; Genetically modified food;
Herbicide resistance; Transferase.
CHAIN 1 183 Phosphinothricin N-acetyltransferase.
/FTId=PRO_0000074574.
DOMAIN 8 173 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 91 93 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q8ZPD3}.
REGION 99 104 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q8ZPD3}.
BINDING 130 130 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q8ZPD3}.
STRAND 9 12 {ECO:0000244|PDB:5T7D}.
HELIX 15 17 {ECO:0000244|PDB:5T7D}.
HELIX 18 31 {ECO:0000244|PDB:5T7D}.
STRAND 33 35 {ECO:0000244|PDB:5T7D}.
HELIX 43 53 {ECO:0000244|PDB:5T7D}.
TURN 54 56 {ECO:0000244|PDB:5T7D}.
STRAND 59 64 {ECO:0000244|PDB:5T7D}.
STRAND 67 80 {ECO:0000244|PDB:5T7D}.
HELIX 81 83 {ECO:0000244|PDB:5T7D}.
STRAND 86 93 {ECO:0000244|PDB:5T7D}.
HELIX 95 97 {ECO:0000244|PDB:5T7D}.
HELIX 102 117 {ECO:0000244|PDB:5T7D}.
STRAND 120 129 {ECO:0000244|PDB:5T7D}.
HELIX 131 139 {ECO:0000244|PDB:5T7D}.
STRAND 143 154 {ECO:0000244|PDB:5T7D}.
STRAND 157 167 {ECO:0000244|PDB:5T7D}.
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


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