ID   SRX1_YEAST              Reviewed;         127 AA.
AC   P36077; D6VXK2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   04-NOV-2026, entry version 173.
DE   RecName: Full=Sulfiredoxin {ECO:0000303|PubMed:14586471};
DE            EC=1.8.98.2;
DE   AltName: Full=Sulphiredoxin {ECO:0000303|PubMed:14586471};
GN   Name=SRX1 {ECO:0000303|PubMed:14586471}; OrderedLocusNames=YKL086W;
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=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
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   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION, DISULFIDE BOND WITH
RP   TSA1, AND MUTAGENESIS OF CYS-48; CYS-84 AND CYS-106.
RX   PubMed=14586471; DOI=10.1038/nature02075;
RA   Biteau B., Labarre J., Toledano M.B.;
RT   "ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae
RT   sulphiredoxin.";
RL   Nature 425:980-984(2003).
CC   -!- FUNCTION: Contributes to oxidative stress resistance by reducing
CC       cysteine-sulfinic acid formed under exposure to oxidants in the
CC       peroxiredoxin TSA1. May catalyze the reduction in a multi-step process
CC       by acting both as a specific phosphotransferase and as
CC       thioltransferase. {ECO:0000269|PubMed:14586471}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-hydroxy-S-oxy-L-cysteinyl-[peroxiredoxin] + [protein]-
CC         dithiol + ATP = S-hydroxy-L-cysteinyl-[peroxiredoxin] + [protein]-
CC         disulfide + ADP + phosphate; Xref=Rhea:RHEA:17545, Rhea:RHEA-
CC         COMP:10593, Rhea:RHEA-COMP:10594, Rhea:RHEA-COMP:13681, Rhea:RHEA-
CC         COMP:17976, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:61973, ChEBI:CHEBI:61974,
CC         ChEBI:CHEBI:456216; EC=1.8.98.2;
CC         Evidence={ECO:0000269|PubMed:14586471};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:14586471};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: By hydrogen peroxide. {ECO:0000269|PubMed:14586471}.
CC   -!- PTM: Forms a transient disulfide bond with TSA1 during the reduction of
CC       cysteine sulfinic acid (-SO2H). {ECO:0000269|PubMed:14586471}.
CC   -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the sulfiredoxin family. {ECO:0000305}.
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DR   EMBL; Z28086; CAA81924.1; -; Genomic_DNA.
DR   EMBL; AY558350; AAS56676.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09072.1; -; Genomic_DNA.
DR   PIR; S37911; S37911.
DR   RefSeq; NP_012837.1; NM_001179652.1.
DR   AlphaFoldDB; P36077; -.
DR   BMRB; P36077; -.
DR   SMR; P36077; -.
DR   BioGRID; 34047; 56.
DR   DIP; DIP-4344N; -.
DR   FunCoup; P36077; 483.
DR   IntAct; P36077; 5.
DR   STRING; 4932.YKL086W; -.
DR   CarbonylDB; P36077; -.
DR   iPTMnet; P36077; -.
DR   PaxDb; 4932-YKL086W; -.
DR   PeptideAtlas; P36077; -.
DR   EnsemblFungi; YKL086W_mRNA; YKL086W; YKL086W.
DR   GeneID; 853776; -.
DR   KEGG; sce:YKL086W; -.
DR   AGR; SGD:S000001569; -.
DR   SGD; S000001569; SRX1.
DR   VEuPathDB; FungiDB:YKL086W; -.
DR   eggNOG; KOG3388; Eukaryota.
DR   HOGENOM; CLU_124532_1_1_1; -.
DR   InParanoid; P36077; -.
DR   OMA; ADLRMYL; -.
DR   OrthoDB; 10023328at2759; -.
DR   BioCyc; YEAST:G3O-31879-MONOMER; -.
DR   Reactome; R-SCE-9818027; NFE2L2 regulating anti-oxidant/detoxification enzymes.
DR   BioGRID-ORCS; 853776; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P36077; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36077; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0032542; F:sulfiredoxin activity; IDA:SGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   GO; GO:0032272; P:negative regulation of protein polymerization; IMP:CAFA.
DR   CDD; cd16395; Srx; 1.
DR   FunFam; 3.90.1530.10:FF:000005; Sulfiredoxin; 1.
DR   Gene3D; 3.90.1530.10; Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, ParB domain; 1.
DR   InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR   InterPro; IPR003115; ParB_N.
DR   InterPro; IPR016692; Sulfiredoxin.
DR   PANTHER; PTHR21348; -; 1.
DR   PANTHER; PTHR21348:SF2; SULFIREDOXIN-1; 1.
DR   Pfam; PF02195; ParB_N; 1.
DR   PIRSF; PIRSF017267; Sulfiredoxin; 1.
DR   SMART; SM00470; ParB; 1.
DR   SUPFAM; SSF110849; ParB/Sulfiredoxin; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; ATP-binding; Cytoplasm; Disulfide bond; Magnesium;
KW   Nucleotide-binding; Nucleus; Oxidoreductase; Reference proteome.
FT   CHAIN           1..127
FT                   /note="Sulfiredoxin"
FT                   /id="PRO_0000211435"
FT   DISULFID        84
FT                   /note="Interchain (with C-48 in TSA1); transient"
FT                   /evidence="ECO:0000269|PubMed:14586471"
FT   MUTAGEN         48
FT                   /note="C->S: Minor effect on formation of disulfide bond
FT                   with TSA1 and reduction of cysteine-sulfinic acid."
FT                   /evidence="ECO:0000269|PubMed:14586471"
FT   MUTAGEN         84
FT                   /note="C->S: Abolishes formation of disulfide bond with
FT                   TSA1 and reduction of cysteine-sulfinic acid."
FT                   /evidence="ECO:0000269|PubMed:14586471"
FT   MUTAGEN         106
FT                   /note="C->S: No effect on formation of disulfide bond with
FT                   TSA1 and reduction of cysteine-sulfinic acid."
FT                   /evidence="ECO:0000269|PubMed:14586471"
SQ   SEQUENCE   127 AA;  13854 MW;  AC15AFD2F6CBC9A0 CRC64;
     MSLQSNSVKP TEIPLSEIRR PLAPVLDPQK IDAMVATMKG IPTASKTCSL EQAEAAASAG
     ELPPVDVLGV RVKGQTLYYA FGGCHRLQAY DRRARETQNA AFPVRCRVLP ATPRQIRMYL
     GSSLDIE
//