MSRA1_STAAW
ID MSRA1_STAAW Reviewed; 169 AA.
AC P0A083; Q99QD5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 1;
DE Short=Protein-methionine-S-oxide reductase 1;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 1;
DE Short=Peptide Met(O) reductase 1;
GN Name=msrA1; Synonyms=msrA; OrderedLocusNames=MW1248;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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 (By similarity). {ECO:0000250}.
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;
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;
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; BA000033; BAB95113.1; -; Genomic_DNA.
DR RefSeq; WP_001024830.1; NC_003923.1.
DR AlphaFoldDB; P0A083; -.
DR SMR; P0A083; -.
DR EnsemblBacteria; BAB95113; BAB95113; BAB95113.
DR KEGG; sam:MW1248; -.
DR HOGENOM; CLU_031040_10_1_9; -.
DR OMA; GYCAFVV; -.
DR Proteomes; UP000000418; 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.
FT CHAIN 1..169
FT /note="Peptide methionine sulfoxide reductase MsrA 1"
FT /id="PRO_0000138591"
FT ACT_SITE 12
FT /evidence="ECO:0000250"
SQ SEQUENCE 169 AA; 19611 MW; 6C5406148DAAC9A0 CRC64;
MNINTAYFAG GCFWCMTKPF DTFDGIEKVT SGYMGGHIEN PTYEQVKSGT SGHLETVEIQ
YDVALFSYNK LLEIFFSVID PLDTGGQYQD RGPQYQTAIF YTNDHQKELA ETYIEQLKNT
INADKAIATK ILPASQFYKA EDYHQDFYKK NPERYAEEQK IRQEYKNKQ
