ATSE2_PSEAE
ID ATSE2_PSEAE Reviewed; 186 AA.
AC Q9I0Q8;
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 PA2578 {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=PA2578;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COENZYME A, AND
RP SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of GNAT superfamily protein PA2578 from Pseudomonas
RT aeruginosa.";
RL Submitted (SEP-2010) to the PDB data bank.
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 antibiotic chloramphenicol.
CC {ECO:0000269|PubMed:23184347}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.3}.
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DR EMBL; AE004091; AAG05966.1; -; Genomic_DNA.
DR PIR; D83323; D83323.
DR RefSeq; NP_251268.1; NC_002516.2.
DR RefSeq; WP_003115331.1; NZ_QZGE01000008.1.
DR PDB; 3OWC; X-ray; 1.90 A; A/B=1-186.
DR PDBsum; 3OWC; -.
DR AlphaFoldDB; Q9I0Q8; -.
DR SMR; Q9I0Q8; -.
DR STRING; 287.DR97_5591; -.
DR PaxDb; Q9I0Q8; -.
DR PRIDE; Q9I0Q8; -.
DR DNASU; 880009; -.
DR EnsemblBacteria; AAG05966; AAG05966; PA2578.
DR GeneID; 880009; -.
DR KEGG; pae:PA2578; -.
DR PATRIC; fig|208964.12.peg.2698; -.
DR PseudoCAP; PA2578; -.
DR HOGENOM; CLU_013985_3_2_6; -.
DR InParanoid; Q9I0Q8; -.
DR OMA; RWFATEK; -.
DR PhylomeDB; Q9I0Q8; -.
DR BioCyc; PAER208964:G1FZ6-2615-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; PF00583; Acetyltransf_1; 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..186
FT /note="Acetyltransferase PA2578"
FT /id="PRO_0000433348"
FT DOMAIN 12..176
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 37
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 97..99
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 105
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 137
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 142..144
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:3OWC"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3OWC"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:3OWC"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:3OWC"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:3OWC"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:3OWC"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:3OWC"
FT STRAND 150..161
FT /evidence="ECO:0007829|PDB:3OWC"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:3OWC"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:3OWC"
SQ SEQUENCE 186 AA; 21032 MW; 4FC6FA03706EB02A CRC64;
MPTPGTGSVP ELQLVPFQLG HFPILQRWFA TEKELVQWAG PALRHPLSLE QMHEDLAESR
RRPPLRLLWS ACRDDQVIGH CQLLFDRRNG VVRLARIVLA PSARGQGLGL PMLEALLAEA
FADADIERVE LNVYDWNAAA RHLYRRAGFR EEGLRRSATR VGRERWNVVL MGLLRQEWAA
GGAGND
