MDDA_SALTY
ID MDDA_SALTY Reviewed; 171 AA.
AC Q8ZPD3;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=L-methionine sulfoximine/L-methionine sulfone acetyltransferase {ECO:0000303|PubMed:25368301};
DE EC=2.3.1.- {ECO:0000269|PubMed:25368301};
DE AltName: Full=L-amino acid N-acyltransferase {ECO:0000250|UniProtKB:P76112};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P76112};
DE AltName: Full=Methionine derivative detoxifier A {ECO:0000303|PubMed:25368301};
DE Short=MDDA {ECO:0000303|PubMed:25368301};
GN Name=yncA; OrderedLocusNames=STM1590;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, MUTAGENESIS OF GLU-82, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=25368301; DOI=10.1128/jb.02311-14;
RA Hentchel K.L., Escalante-Semerena J.C.;
RT "In Salmonella enterica, the Gcn5-related acetyltransferase MddA (formerly
RT YncA) acetylates methionine sulfoximine and methionine sulfone, blocking
RT their toxic effects.";
RL J. Bacteriol. 197:314-325(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ACETYL-COA, AND
RP SUBUNIT.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RG Center for structural genomics of infectious diseases (CSGID);
RT "Structure of yncA, a putative acetyltransferase from Salmonella
RT typhimurium with its cofactor acetyl-CoA.";
RL Submitted (JUL-2008) 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 MSX. It can
CC also use L-methionine sulfone (MSO) (PubMed:25368301). Also catalyzes
CC the acylation of free L-amino acids using an acyl-CoA as acyl donor (By
CC similarity). {ECO:0000250|UniProtKB:P76112,
CC ECO:0000269|PubMed:25368301}.
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:25368301};
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:25368301};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=156 uM for acetyl-CoA (at pH 7.2 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25368301};
CC KM=230 uM for MSO (at pH 7.2 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25368301};
CC KM=576 uM for MSX (at pH 7.2 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25368301};
CC Note=kcat is 35 sec(-1) for acetyltransferase activity with MSX as
CC substrate (at pH 7.2 and 30 degrees Celsius). kcat is 31 sec(-1) for
CC acetyltransferase activity with MSO as substrate (at pH 7.2 and 30
CC degrees Celsius). kcat is 23 sec(-1) for acetyltransferase activity
CC with acetyl-CoA as substrate (at pH 7.2 and 30 degrees Celsius).
CC {ECO:0000269|PubMed:25368301};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25368301, ECO:0000269|Ref.3}.
CC -!- DISRUPTION PHENOTYPE: In minimal medium, cells lacking this gene grow
CC normally with MSO, but growth is inhibited by MSX. In rich medium,
CC growth of cells lacking this gene are partially inhibited by MSX, only
CC when its concentration is at least 50 uM.
CC {ECO:0000269|PubMed:25368301}.
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DR EMBL; AE006468; AAL20508.1; -; Genomic_DNA.
DR RefSeq; NP_460549.1; NC_003197.2.
DR RefSeq; WP_000155373.1; NC_003197.2.
DR PDB; 3DR6; X-ray; 1.75 A; A/B/C=1-171.
DR PDB; 3DR8; X-ray; 1.95 A; A/B=1-171.
DR PDBsum; 3DR6; -.
DR PDBsum; 3DR8; -.
DR AlphaFoldDB; Q8ZPD3; -.
DR SMR; Q8ZPD3; -.
DR STRING; 99287.STM1590; -.
DR PaxDb; Q8ZPD3; -.
DR EnsemblBacteria; AAL20508; AAL20508; STM1590.
DR GeneID; 1253108; -.
DR KEGG; stm:STM1590; -.
DR PATRIC; fig|99287.12.peg.1681; -.
DR HOGENOM; CLU_013985_4_4_6; -.
DR OMA; IFAHNQP; -.
DR PhylomeDB; Q8ZPD3; -.
DR BioCyc; SENT99287:STM1590-MON; -.
DR EvolutionaryTrace; Q8ZPD3; -.
DR Proteomes; UP000001014; 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..171
FT /note="L-methionine sulfoximine/L-methionine sulfone
FT acetyltransferase"
FT /id="PRO_0000433346"
FT DOMAIN 1..163
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 72..74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6VCX3"
FT BINDING 82..84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6VCX3"
FT BINDING 85..87
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 93..98
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 124
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 82
FT /note="E->Q: Loss of acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:25368301"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3DR6"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:3DR6"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:3DR6"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:3DR6"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:3DR6"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3DR6"
FT STRAND 61..74
FT /evidence="ECO:0007829|PDB:3DR6"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3DR6"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:3DR6"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3DR6"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:3DR6"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:3DR6"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:3DR6"
FT STRAND 137..148
FT /evidence="ECO:0007829|PDB:3DR6"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:3DR6"
SQ SEQUENCE 171 AA; 19188 MW; D40DD786C750E073 CRC64;
MTIRFADKAD CAAITEIYNH AVLHTAAIWN DRTVDTDNRL AWYEARQLLG YPVLVSEENG
VVTGYASFGD WRSFDGFRYT VEHSVYVHPA HQGKGLGRKL LSRLIDEARR CGKHVMVAGI
ESQNAASIRL HHSLGFTVTA QMPQVGVKFG RWLDLTFMQL QLDEHAAPDA C
