ID   Q7VCK0_PROMA            Unreviewed;       237 AA.
AC   Q7VCK0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   10-JUN-2026, entry version 126.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000256|HAMAP-Rule:MF_01401,
GN   ECO:0000313|EMBL:AAP99784.1};
GN   OrderedLocusNames=Pro_0740 {ECO:0000313|EMBL:AAP99784.1};
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167539 {ECO:0000313|EMBL:AAP99784.1, ECO:0000313|Proteomes:UP000001420};
RN   [1] {ECO:0000313|EMBL:AAP99784.1, ECO:0000313|Proteomes:UP000001420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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       {ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-
CC         methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol;
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         Evidence={ECO:0000256|ARBA:ARBA00047806, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + L-methionine + H2O = L-methionine
CC         (S)-S-oxide + [thioredoxin]-dithiol; 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         Evidence={ECO:0000256|ARBA:ARBA00048782, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01401}.
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DR   EMBL; AE017126; AAP99784.1; -; Genomic_DNA.
DR   RefSeq; WP_011124892.1; NC_005042.1.
DR   AlphaFoldDB; Q7VCK0; -.
DR   STRING; 167539.Pro_0740; -.
DR   EnsemblBacteria; AAP99784; AAP99784; Pro_0740.
DR   KEGG; pma:Pro_0740; -.
DR   PATRIC; fig|167539.5.peg.782; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_3_3; -.
DR   OrthoDB; 4174719at2; -.
DR   Proteomes; UP000001420; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0033744; F:L-methionine (S)-S-oxide reductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter.
DR   Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   InterPro; IPR050162; MsrA_MetSO_reductase.
DR   NCBIfam; TIGR00401; msrA; 1.
DR   PANTHER; PTHR42799; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR42799:SF2; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01401}; Reference proteome {ECO:0000313|Proteomes:UP000001420}.
FT   DOMAIN          37..197
FT                   /note="Peptide methionine sulphoxide reductase MsrA"
FT                   /evidence="ECO:0000259|Pfam:PF01625"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   237 AA;  27110 MW;  3EACD05CF3796540 CRC64;
     MFLNWLNPKK VEAQGKTTSK HFVLNSLINK PANKDEEEIF FGCGCFWGAE KGFWKLPGVI
     TTAVGYAGGA KKNPTYREVC SGRTNHAEVV RVIWNKLEID LSDLLKMFWE CHDPTQGNRQ
     GNDSGSQYRS AIYLTKQDHK TLAINSLEKY QVLLQEKGFG SITTQIETNI DFYYAEDYHQ
     QYLAKPGSRP YCSAMPTNVS LKDFKGSNYK LNSRVWDNFN WEQNHCVLRS SNSPIIN
//