ATSE3_PSEAE
ID ATSE3_PSEAE Reviewed; 192 AA.
AC Q9HX72;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acetyltransferase PA3944 {ECO:0000303|PubMed:23184347};
DE EC=2.3.1.-;
DE AltName: Full=GCN5-related N-acetyltransferase {ECO:0000303|PubMed:23184347};
DE Short=GNAT {ECO:0000303|PubMed:23184347};
GN OrderedLocusNames=PA3944;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23184347; DOI=10.1002/pro.2199;
RA Kuhn M.L., Majorek K.A., Minor W., Anderson W.F.;
RT "Broad-substrate screen as a tool to identify substrates for bacterial
RT Gcn5-related N-acetyltransferases with unknown substrate specificity.";
RL Protein Sci. 22:222-230(2013).
CC -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl
CC coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and
CC the acetylated product. It prefers the peptide Asp-Phe methyl ester (or
CC aspartame) and the peptide antibiotics polymyxin B and colistin. Other
CC substrates like dopamine, serotonin, puromycin, chloramphenicol, D-
CC glucosamine, glycine and N-alpha-acetyl-L-glutamine are used and
CC displayed lower activity. {ECO:0000269|PubMed:23184347}.
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DR EMBL; AE004091; AAG07331.1; -; Genomic_DNA.
DR PIR; D83153; D83153.
DR RefSeq; NP_252633.1; NC_002516.2.
DR RefSeq; WP_003106018.1; NZ_QZGE01000001.1.
DR PDB; 6EDD; X-ray; 1.55 A; A/B=1-192.
DR PDB; 6EDV; X-ray; 1.35 A; A=1-192.
DR PDB; 7KPP; X-ray; 1.45 A; A/B=1-192.
DR PDB; 7KPS; X-ray; 1.80 A; A/B=1-192.
DR PDB; 7KYE; X-ray; 1.93 A; A=1-192.
DR PDB; 7KYJ; X-ray; 2.00 A; A/B=1-192.
DR PDBsum; 6EDD; -.
DR PDBsum; 6EDV; -.
DR PDBsum; 7KPP; -.
DR PDBsum; 7KPS; -.
DR PDBsum; 7KYE; -.
DR PDBsum; 7KYJ; -.
DR AlphaFoldDB; Q9HX72; -.
DR SMR; Q9HX72; -.
DR STRING; 287.DR97_3922; -.
DR PaxDb; Q9HX72; -.
DR DNASU; 878785; -.
DR EnsemblBacteria; AAG07331; AAG07331; PA3944.
DR GeneID; 878785; -.
DR KEGG; pae:PA3944; -.
DR PATRIC; fig|208964.12.peg.4133; -.
DR PseudoCAP; PA3944; -.
DR HOGENOM; CLU_013985_3_1_6; -.
DR InParanoid; Q9HX72; -.
DR OMA; HKRANIS; -.
DR PhylomeDB; Q9HX72; -.
DR BioCyc; PAER208964:G1FZ6-4017-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..192
FT /note="Acetyltransferase PA3944"
FT /id="PRO_0000433349"
FT DOMAIN 18..187
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 105..107
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT BINDING 113
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT BINDING 145
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT BINDING 150..152
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT TURN 1..4
FT /evidence="ECO:0007829|PDB:7KPP"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6EDV"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:6EDV"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:6EDV"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:6EDV"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7KPS"
FT HELIX 50..67
FT /evidence="ECO:0007829|PDB:6EDV"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6EDV"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6EDV"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:6EDV"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6EDV"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:6EDV"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6EDV"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:6EDV"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:6EDV"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:6EDV"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6EDV"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:6EDV"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:6EDV"
SQ SEQUENCE 192 AA; 21857 MW; EA68509897E57B7D CRC64;
MNANLPPSAI SELHGPRLLL RAWRDSDREA FAEMCADPQV MEFFPSVLDR AQSDALVDRV
QAHFAERGYG PWALELPGEA AFIGFTGLFD VTMDVHFAPT VEIGWRLAPA YWGRGLAREA
AETALDFAFE RLRLPEVVAF TTPPNRRSWG LMERLGMRRD PAEDFDHPLL AADHPMRRHI
LYRVDAARWA ER
