MSRA_PAEAT
ID MSRA_PAEAT Reviewed; 174 AA.
AC A1R7D2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=AAur_2415;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM09216.1; -; Genomic_DNA.
DR RefSeq; WP_011775087.1; NC_008711.1.
DR AlphaFoldDB; A1R7D2; -.
DR SMR; A1R7D2; -.
DR STRING; 290340.AAur_2415; -.
DR EnsemblBacteria; ABM09216; ABM09216; AAur_2415.
DR KEGG; aau:AAur_2415; -.
DR eggNOG; COG0225; Bacteria.
DR HOGENOM; CLU_031040_10_0_11; -.
DR OMA; GYCAFVV; -.
DR OrthoDB; 1554384at2; -.
DR Proteomes; UP000000637; 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..174
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /id="PRO_1000068307"
FT ACT_SITE 10
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ SEQUENCE 174 AA; 19770 MW; A8064E88CD956FEA CRC64;
MKTFVLGGGC FWCLDAVYQK TRGVSSVVSG YTGGHVRNPD YYEVCSGTTG HAEVVAVTFD
ETVVPEEVIL DMFFALHDPT TLNRQGYDVG TQYRSSMFYT TTEEKVLFEE AIERAQALWS
DPIVTEVSRL PEFHEAEEVH QNYYAKFPYQ GYCQVIINPK LAKARKYYSA WLTA
