ID   MSRA_MYCSS              Reviewed;         171 AA.
AC   Q1B1N8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Mmcs_5092;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) 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; CP000384; ABG11196.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1B1N8; -.
DR   SMR; Q1B1N8; -.
DR   KEGG; mmc:Mmcs_5092; -.
DR   HOGENOM; CLU_031040_10_2_11; -.
DR   OMA; GYCAFVV; -.
DR   BioCyc; MSP164756:G1G6O-5205-MON; -.
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..171
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_1000145421"
FT   ACT_SITE        13
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   171 AA;  19443 MW;  17009E2D6DCCDBE0 CRC64;
     MSDHKKAILA GGCFWGMQDL IRKQPGVVST RVGYTGGQND HPTYRNHPGH AESIEITYDP
     AQTDYRALLE FFFQIHDPTT KNRQGNDVGT SYRSAIFYVD DEQKRVALDT IADVDASGLW
     PGKVVTEVTP AGEFWEAEPE HQDYLERMPW GYTCHFPRPD WKLPKRADAK A