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MSRA_DICD3
ID   MSRA_DICD3              Reviewed;         213 AA.
AC   Q9ZEQ8; E0SEC6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE            Short=Protein-methionine-S-oxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=msrA; OrderedLocusNames=Dda3937_00164;
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3937;
RX   PubMed=9927663; DOI=10.1073/pnas.96.3.887;
RA   Hassouni M.E., Chambost J.P., Expert D., Van Gijsegem F., Barras F.;
RT   "The minimal gene set member msrA, encoding peptide methionine sulfoxide
RT   reductase, is a virulence determinant of the plant pathogen Erwinia
RT   chrysanthemi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:887-892(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937;
RX   PubMed=21217001; DOI=10.1128/jb.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
CC   -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC       that have been inactivated by oxidation. Catalyzes the reversible
CC       oxidation-reduction of methionine sulfoxide in proteins to methionine
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58772; EC=1.8.4.11;
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ012716; CAA10143.1; -; Genomic_DNA.
DR   EMBL; CP002038; ADM99860.1; -; Genomic_DNA.
DR   RefSeq; WP_013319285.1; NC_014500.1.
DR   AlphaFoldDB; Q9ZEQ8; -.
DR   BMRB; Q9ZEQ8; -.
DR   SMR; Q9ZEQ8; -.
DR   STRING; 198628.Dda3937_00164; -.
DR   EnsemblBacteria; ADM99860; ADM99860; Dda3937_00164.
DR   KEGG; ddd:Dda3937_00164; -.
DR   PATRIC; fig|198628.6.peg.3608; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_3_6; -.
DR   OMA; AGPFYYA; -.
DR   OrthoDB; 1554384at2; -.
DR   BioCyc; DDAD198628:DDA3937_RS17165-MON; -.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..213
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_0000138549"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23701 MW;  9EE0F02FE7428CB2 CRC64;
     MIANFDKTQP IGQSDALPGR TTPMPVARLH VVNQHSMTHV PDHMEVAIFA MGCFWGVERL
     FWQQPGVYST ASGYCGGYTP NPTYREVCTG KTGHAEAVRV VFDPAVVSYP QLLQLFWENH
     NPAQGMRQGN DIGTQYRSAI YTLTTEQETA AKESYQRFQQ AMRDAGNDHD ITTEIQPAGP
     FYYAEDEHQQ YLHKNPDGYC GLGGIGVCLP PQG
 
 
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