MDDA_PSEA7
ID MDDA_PSEA7 Reviewed; 172 AA.
AC A6VCX3;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=L-methionine sulfoximine/L-methionine sulfone acetyltransferase {ECO:0000303|PubMed:17253769};
DE EC=2.3.1.- {ECO:0000269|PubMed:17253769};
DE AltName: Full=Methionine derivative detoxifier A {ECO:0000250|UniProtKB:Q8ZPD3};
DE Short=MDDA {ECO:0000250|UniProtKB:Q8ZPD3};
GN OrderedLocusNames=PSPA7_5587;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE,
RP SUBUNIT, AND SUBSTRATE SPECIFICITY.
RX PubMed=17253769; DOI=10.1021/bi0615238;
RA Davies A.M., Tata R., Beavil R.L., Sutton B.J., Brown P.R.;
RT "l-Methionine sulfoximine, but not phosphinothricin, is a substrate for an
RT acetyltransferase (gene PA4866) from Pseudomonas aeruginosa: structural and
RT functional studies.";
RL Biochemistry 46:1829-1839(2007).
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). It can also use L-methionine sulfone (MSO).
CC {ECO:0000269|PubMed:17253769}.
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:0000269|PubMed:17253769};
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:0000269|PubMed:17253769};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for acetyl-CoA (at pH 7.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17253769};
CC KM=1.3 mM for MSX (at pH 7.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17253769};
CC KM=1.3 mM for MSO (at pH 7.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17253769};
CC Note=kcat is 610 sec(-1) for acetyltransferase activity with MSO as
CC substrate (at pH 7.2 and 37 degrees Celsius). kcat is 505 sec(-1) for
CC acetyltransferase activity with MSX as substrate (at pH 7.2 and 37
CC degrees Celsius). {ECO:0000269|PubMed:17253769};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17253769}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not have
CC acetyltransferase activity and induce a degradation of proteins. Growth
CC in succinate medium with glutamate, ammonium, urea, and proline as
CC nitrogen sources is stopped by the addition of 200 uM MSX at the
CC beginning of the log phase, and no further growth is observed for the
CC next 12 h. Growth with glutamine as a nitrogen source is unaffected.
CC {ECO:0000269|PubMed:17253769}.
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DR EMBL; CP000744; ABR81107.1; -; Genomic_DNA.
DR RefSeq; WP_003157482.1; NC_009656.1.
DR PDB; 2J8M; X-ray; 1.44 A; A/B=1-172.
DR PDB; 2J8N; X-ray; 2.35 A; A/B=1-172.
DR PDB; 2J8R; X-ray; 1.55 A; A/B=1-172.
DR PDBsum; 2J8M; -.
DR PDBsum; 2J8N; -.
DR PDBsum; 2J8R; -.
DR AlphaFoldDB; A6VCX3; -.
DR SMR; A6VCX3; -.
DR EnsemblBacteria; ABR81107; ABR81107; PSPA7_5587.
DR KEGG; pap:PSPA7_5587; -.
DR HOGENOM; CLU_013985_4_4_6; -.
DR OMA; IFAHNQP; -.
DR OrthoDB; 1809950at2; -.
DR Proteomes; UP000001582; 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; Transferase.
FT CHAIN 1..172
FT /note="L-methionine sulfoximine/L-methionine sulfone
FT acetyltransferase"
FT /id="PRO_0000433344"
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:0000269|PubMed:17253769"
FT BINDING 85..87
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17253769"
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 4..7
FT /evidence="ECO:0007829|PDB:2J8M"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2J8M"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:2J8M"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2J8M"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:2J8M"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2J8M"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:2J8M"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2J8M"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2J8M"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2J8N"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:2J8M"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:2J8M"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:2J8M"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:2J8M"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:2J8M"
SQ SEQUENCE 172 AA; 18713 MW; 30E711632F1CD833 CRC64;
MSASIRDAGV ADLPGILAIY NDAVGNTTAI WNETPVDLAN RQAWFDARAR QGYPILVASD
AAGEVLGYAS YGDWRPFEGF RGTVEHSVYV RDDQRGKGLG VQLLQALIER ARAQGLHVMV
AAIESGNAAS IGLHRRLGFE ISGQMPQVGQ KFGRWLDLTF MQLNLDPTRS AP
