ID   MSRA_BRUC2              Reviewed;         218 AA.
AC   A9MCZ5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000255|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000255|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000255|HAMAP-Rule:MF_01401}; OrderedLocusNames=BCAN_B1091;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01401}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01401}.
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DR   EMBL; CP000873; ABX64232.1; -; Genomic_DNA.
DR   RefSeq; WP_002965585.1; NC_010104.1.
DR   AlphaFoldDB; A9MCZ5; -.
DR   SMR; A9MCZ5; -.
DR   EnsemblBacteria; ABX64232; ABX64232; BCAN_B1091.
DR   GeneID; 45126367; -.
DR   GeneID; 55592689; -.
DR   KEGG; bcs:BCAN_B1091; -.
DR   HOGENOM; CLU_031040_10_3_5; -.
DR   OMA; AGPFYYA; -.
DR   PhylomeDB; A9MCZ5; -.
DR   Proteomes; UP000001385; Chromosome II.
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.
FT   CHAIN           1..218
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_1000087345"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   218 AA;  24017 MW;  64B43110667417B0 CRC64;
     MSFFDSYRKK MQMPSKEEVL PGRVQPIPTA AAHFVSGHPL KGPWPDGMKQ VLFGMGCFWG
     AERLFWQVPG VYVTAVGYAG GITPNPTYEE TCTGLTGHAE VVLVVYDPKV VTLNELLALF
     WEEHDPTQGM RQGNDIGTTY RSVIYTFNAV DRAVAEKSRD AYSQALASRG LGPVTTQIAD
     APDFYYAEDY HQQYLAKNPD GYCGLRGTGV SCPIPLAH