MSRA_YEAST
ID MSRA_YEAST Reviewed; 184 AA.
AC P40029; D3DLU2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Peptide methionine sulfoxide reductase;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE AltName: Full=Protein-methionine-S-oxide reductase;
GN Name=MXR1; OrderedLocusNames=YER042W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10473395; DOI=10.1128/aem.65.9.3915-3919.1999;
RA Hansen J.;
RT "Inactivation of MXR1 abolishes formation of dimethyl sulfide from dimethyl
RT sulfoxide in Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 65:3915-3919(1999).
RN [5]
RP MUTAGENESIS.
RX PubMed=10799493; DOI=10.1074/jbc.275.19.14167;
RA Moskovitz J., Poston J.M., Berlett B.S., Nosworthy N.J., Szczepanowski R.,
RA Stadtman E.R.;
RT "Identification and characterization of a putative active site for peptide
RT methionine sulfoxide reductase (MsrA) and its substrate
RT stereospecificity.";
RL J. Biol. Chem. 275:14167-14172(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the
CC product.
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 -!- MISCELLANEOUS: Present with 3070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; U18796; AAB64577.1; -; Genomic_DNA.
DR EMBL; AY692798; AAT92817.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07696.1; -; Genomic_DNA.
DR PIR; S50545; S50545.
DR RefSeq; NP_010960.1; NM_001178933.1.
DR PDB; 3PIL; X-ray; 2.04 A; A/B=2-184.
DR PDB; 3PIM; X-ray; 1.90 A; A/B/C=2-184.
DR PDB; 3PIN; X-ray; 2.70 A; B=2-184.
DR PDBsum; 3PIL; -.
DR PDBsum; 3PIM; -.
DR PDBsum; 3PIN; -.
DR AlphaFoldDB; P40029; -.
DR SMR; P40029; -.
DR BioGRID; 36778; 129.
DR IntAct; P40029; 2.
DR MINT; P40029; -.
DR STRING; 4932.YER042W; -.
DR iPTMnet; P40029; -.
DR MaxQB; P40029; -.
DR PaxDb; P40029; -.
DR PRIDE; P40029; -.
DR EnsemblFungi; YER042W_mRNA; YER042W; YER042W.
DR GeneID; 856765; -.
DR KEGG; sce:YER042W; -.
DR SGD; S000000844; MXR1.
DR VEuPathDB; FungiDB:YER042W; -.
DR eggNOG; KOG1635; Eukaryota.
DR GeneTree; ENSGT00390000003823; -.
DR HOGENOM; CLU_031040_10_2_1; -.
DR InParanoid; P40029; -.
DR OMA; AGPFYYA; -.
DR BioCyc; YEAST:YER042W-MON; -.
DR PRO; PR:P40029; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40029; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..184
FT /note="Peptide methionine sulfoxide reductase"
FT /id="PRO_0000138630"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:3PIM"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3PIL"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3PIM"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:3PIM"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:3PIM"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3PIM"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:3PIM"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3PIL"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3PIL"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3PIM"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3PIM"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:3PIM"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3PIL"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3PIL"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3PIM"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3PIM"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:3PIM"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:3PIM"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:3PIM"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:3PIM"
SQ SEQUENCE 184 AA; 21141 MW; 329CE3E8F4B006AD CRC64;
MSSLISKTIK YDPAKDKLIT LACGCFWGTE HMYRKYLNDR IVDCKVGYAN GEESKKDSPS
SVSYKRVCGG DTDFAEVLQV SYNPKVITLR ELTDFFFRIH DPTTSNSQGP DKGTQYRSGL
FAHSDADLKE LAKIKEEWQP KWGNKIATVI EPIKNFYDAE EYHQLYLDKN PQGYACPTHY
LREM
