MDDA_PSEAE
ID MDDA_PSEAE Reviewed; 172 AA.
AC Q9HUU7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=L-methionine sulfoximine/L-methionine sulfone acetyltransferase {ECO:0000250|UniProtKB:A6VCX3};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:A6VCX3};
DE AltName: Full=Methionine derivative detoxifier A {ECO:0000250|UniProtKB:Q8ZPD3};
DE Short=MDDA {ECO:0000250|UniProtKB:Q8ZPD3};
GN Name=pitA {ECO:0000303|PubMed:16161106}; OrderedLocusNames=PA4866;
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 X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16161106; DOI=10.1002/prot.20603;
RA Davies A.M., Tata R., Agha R., Sutton B.J., Brown P.R.;
RT "Crystal structure of a putative phosphinothricin acetyltransferase
RT (PA4866) from Pseudomonas aeruginosa PAC1.";
RL Proteins 61:677-679(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND 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 a hypothetical acetyltransferase from P.aeruginosa
RT PA01.";
RL Submitted (FEB-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the resistance against the toxic effects of
CC L-methionine sulfoximine (MSX), a rare amino acid, which inhibits
CC glutamine synthetase (GlnA). Catalyzes the acetylation of L-methionine
CC sulfoximine (MSX). {ECO:0000250|UniProtKB:A6VCX3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-methionine sulfoximine = CoA + H(+) + N-acetyl-
CC L-methionine sulfoximine; Xref=Rhea:RHEA:47660, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:87826,
CC ChEBI:CHEBI:87827; Evidence={ECO:0000250|UniProtKB:A6VCX3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-methionine sulfone = CoA + H(+) + N-acetyl-L-
CC methionine sulfone; Xref=Rhea:RHEA:47656, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:87824,
CC ChEBI:CHEBI:87825; Evidence={ECO:0000250|UniProtKB:A6VCX3};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16161106, ECO:0000269|Ref.3}.
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DR EMBL; AE004091; AAG08251.1; -; Genomic_DNA.
DR PIR; F83037; F83037.
DR RefSeq; NP_253553.1; NC_002516.2.
DR RefSeq; WP_003099390.1; NZ_QZGE01000002.1.
DR PDB; 1YVO; X-ray; 1.90 A; A/B=1-172.
DR PDB; 2BL1; X-ray; 2.00 A; A=1-172.
DR PDBsum; 1YVO; -.
DR PDBsum; 2BL1; -.
DR AlphaFoldDB; Q9HUU7; -.
DR SMR; Q9HUU7; -.
DR STRING; 287.DR97_2217; -.
DR PaxDb; Q9HUU7; -.
DR PRIDE; Q9HUU7; -.
DR DNASU; 882184; -.
DR EnsemblBacteria; AAG08251; AAG08251; PA4866.
DR GeneID; 882184; -.
DR KEGG; pae:PA4866; -.
DR PATRIC; fig|208964.12.peg.5099; -.
DR PseudoCAP; PA4866; -.
DR HOGENOM; CLU_013985_4_4_6; -.
DR InParanoid; Q9HUU7; -.
DR OMA; IFAHNQP; -.
DR PhylomeDB; Q9HUU7; -.
DR BioCyc; PAER208964:G1FZ6-4980-MON; -.
DR BRENDA; 2.3.1.183; 5087.
DR EvolutionaryTrace; Q9HUU7; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; ISS: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..172
FT /note="L-methionine sulfoximine/L-methionine sulfone
FT acetyltransferase"
FT /id="PRO_0000433345"
FT DOMAIN 3..166
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6VCX3"
FT BINDING 85..87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6VCX3"
FT BINDING 88..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT BINDING 96..101
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT BINDING 127
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1YVO"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1YVO"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:1YVO"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1YVO"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:1YVO"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1YVO"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:1YVO"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1YVO"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1YVO"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1YVO"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:1YVO"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1YVO"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:1YVO"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:1YVO"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:1YVO"
SQ SEQUENCE 172 AA; 18743 MW; 30E7117F5F15A826 CRC64;
MSASIRDAGV ADLPGILAIY NDAVGNTTAI WNETPVDLAN RQAWFDTRAR QGYPILVASD
AAGEVLGYAS YGDWRPFEGF RGTVEHSVYV RDDQRGKGLG VQLLQALIER ARAQGLHVMV
AAIESGNAAS IGLHRRLGFE ISGQMPQVGQ KFGRWLDLTF MQLNLDPTRS AP
