MSRA_THET2
ID MSRA_THET2 Reviewed; 176 AA.
AC Q746G0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=TT_P0095;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017222; AAS82425.1; -; Genomic_DNA.
DR RefSeq; WP_011174467.1; NC_005838.1.
DR AlphaFoldDB; Q746G0; -.
DR SMR; Q746G0; -.
DR STRING; 262724.TT_P0095; -.
DR EnsemblBacteria; AAS82425; AAS82425; TT_P0095.
DR KEGG; tth:TT_P0095; -.
DR eggNOG; COG0225; Bacteria.
DR HOGENOM; CLU_031040_10_0_0; -.
DR OMA; AGPFYYA; -.
DR OrthoDB; 1554384at2; -.
DR Proteomes; UP000000592; Plasmid pTT27.
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; Plasmid.
FT CHAIN 1..176
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /id="PRO_0000138603"
FT ACT_SITE 12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ SEQUENCE 176 AA; 19838 MW; 699C57E1A4279EE0 CRC64;
MPEEIATLAG GCFWCTEAAF KLLRGVLEVV PGYAGGHVPH PTYEEVCTGT TGHREAVQVR
FDPGVLPYAD LLRYFFAVHD PTSEDRQGPD VGPQYSPAIF YHSEEQKRVA EAVMRELAPL
YPKPIATKLL PFTTFYPAEA YHRDYFARHP EAPYCRLVIA PKLEKARKAF KSLLRP
