SRX1_YEAST
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 03-AUG-2022, entry version 158.
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=[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-
CC [peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy-
CC L-cysteinyl-[peroxiredoxin]; 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; 49.
DR DIP; DIP-4344N; -.
DR IntAct; P36077; 2.
DR STRING; 4932.YKL086W; -.
DR CarbonylDB; P36077; -.
DR MaxQB; P36077; -.
DR PaxDb; P36077; -.
DR PRIDE; P36077; -.
DR EnsemblFungi; YKL086W_mRNA; YKL086W; YKL086W.
DR GeneID; 853776; -.
DR KEGG; sce:YKL086W; -.
DR SGD; S000001569; SRX1.
DR VEuPathDB; FungiDB:YKL086W; -.
DR eggNOG; KOG3388; Eukaryota.
DR GeneTree; ENSGT00390000007832; -.
DR HOGENOM; CLU_124532_1_1_1; -.
DR InParanoid; P36077; -.
DR OMA; CHRFAAY; -.
DR BioCyc; YEAST:G3O-31879-MON; -.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:P36077; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36077; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR016692; Sulfiredoxin.
DR PANTHER; PTHR21348; PTHR21348; 1.
DR Pfam; PF02195; ParBc; 1.
DR PIRSF; PIRSF017267; Sulfiredoxin; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 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
