MSRA_CLOTE
ID MSRA_CLOTE Reviewed; 164 AA.
AC Q899M3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=CTC_00149;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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: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; AE015927; AAO34801.1; -; Genomic_DNA.
DR AlphaFoldDB; Q899M3; -.
DR SMR; Q899M3; -.
DR STRING; 212717.CTC_00149; -.
DR EnsemblBacteria; AAO34801; AAO34801; CTC_00149.
DR KEGG; ctc:CTC_00149; -.
DR HOGENOM; CLU_031040_10_2_9; -.
DR OMA; GYCAFVV; -.
DR Proteomes; UP000001412; 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..164
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /id="PRO_0000138540"
FT ACT_SITE 16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ SEQUENCE 164 AA; 19092 MW; 1B0A9AC6DC43C1E3 CRC64;
MKGVKFMKEI ILAGGCFWGV EEYFSRIYGV VDTKVGYVNG VTKNPSYEEV CNGNTGYAEG
CYIKFDESII GLKRILDKFW DIIDPTILNR QGPDVGHQYR TGIYYYDKED LDDILKSKDE
ISKKYDKPIV TEVEKVTYFY LAEEYHQKYL KKNPNGYCHI NLDN
