MXR2_YEAST
ID MXR2_YEAST Reviewed; 168 AA.
AC P25566; D6VQY2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Peptide methionine sulfoxide reductase 2;
DE EC=1.8.4.12 {ECO:0000269|PubMed:15141092};
GN Name=MXR2; Synonyms=MSRB; OrderedLocusNames=YCL033C; ORFNames=YCL33C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15141092; DOI=10.1073/pnas.0307929101;
RA Koc A., Gasch A.P., Rutherford J.C., Kim H.Y., Gladyshev V.N.;
RT "Methionine sulfoxide reductase regulation of yeast lifespan reveals
RT reactive oxygen species-dependent and -independent components of aging.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7999-8004(2004).
RN [5]
RP FUNCTION.
RX PubMed=19202110; DOI=10.1099/mic.0.022665-0;
RA Sideri T.C., Willetts S.A., Avery S.V.;
RT "Methionine sulphoxide reductases protect iron-sulphur clusters from
RT oxidative inactivation in yeast.";
RL Microbiology 155:612-623(2009).
CC -!- FUNCTION: Methionine-R-sulfoxide reductase which catalyzes the
CC reduction of methionine sulfoxide (MetSO) to methionine in proteins.
CC Plays a protective role against oxidative stress by restoring activity
CC to proteins that have been inactivated by methionine oxidation.
CC Protects iron-sulfur clusters from oxidative inactivation along with
CC MXR1. Involved in the regulation of lifespan.
CC {ECO:0000269|PubMed:15141092, ECO:0000269|PubMed:19202110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC Evidence={ECO:0000269|PubMed:15141092};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24166;
CC Evidence={ECO:0000305|PubMed:15141092};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; X59720; CAA42383.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07451.1; -; Genomic_DNA.
DR PIR; S19361; S19361.
DR RefSeq; NP_009897.1; NM_001178678.1.
DR AlphaFoldDB; P25566; -.
DR SMR; P25566; -.
DR BioGRID; 30950; 52.
DR DIP; DIP-4861N; -.
DR IntAct; P25566; 2.
DR STRING; 4932.YCL033C; -.
DR MaxQB; P25566; -.
DR PaxDb; P25566; -.
DR PRIDE; P25566; -.
DR EnsemblFungi; YCL033C_mRNA; YCL033C; YCL033C.
DR GeneID; 850324; -.
DR KEGG; sce:YCL033C; -.
DR SGD; S000000538; MXR2.
DR VEuPathDB; FungiDB:YCL033C; -.
DR eggNOG; KOG0856; Eukaryota.
DR HOGENOM; CLU_031040_8_1_1; -.
DR InParanoid; P25566; -.
DR OMA; DEQWRAE; -.
DR BioCyc; YEAST:G3O-29293-MON; -.
DR PRO; PR:P25566; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25566; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR46081; PTHR46081; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Metal-binding; Oxidoreductase;
KW Redox-active center; Reference proteome; Transport; Zinc.
FT CHAIN 1..168
FT /note="Peptide methionine sulfoxide reductase 2"
FT /id="PRO_0000140326"
FT DOMAIN 40..168
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT DISULFID 97..157
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 168 AA; 19279 MW; C79BE75DC35D82F4 CRC64;
MNKWSRLYVI TVRRTFPGRR NIVLTQYWNK SKKMSDESND VKWNDALTPL QLMVLRDKAT
ERPNTGAYLH TNESGVYHCA NCDRPLYSSK AKFDARCGWP AFYEEVSPGA ITYHRDNSLM
PARVEICCAR CGGHLGHVFE GEGWKQLLNL PKDTRHCVNS ASLNLKKD
