URE2_YEAST
ID URE2_YEAST Reviewed; 354 AA.
AC P23202; D6W0W3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Transcriptional regulator URE2;
DE AltName: Full=Disulfide reductase;
DE EC=1.8.4.-;
DE AltName: Full=Glutathione peroxidase;
DE EC=1.11.1.9;
GN Name=URE2; OrderedLocusNames=YNL229C; ORFNames=N1165;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=1990286; DOI=10.1128/mcb.11.2.822-832.1991;
RA Coschigano P.W., Magasanik B.;
RT "The URE2 gene product of Saccharomyces cerevisiae plays an important role
RT in the cellular response to the nitrogen source and has homology to
RT glutathione s-transferases.";
RL Mol. Cell. Biol. 11:822-832(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14085 / CBS 3093 / IFO 1997 / NRRL Y-12657,
RC ATCC 9804 / CBS 400 / DSM 70478 / IFO 0210 / JCM 2220, Boots, CBS 2087,
RC CBS 4734, CBS 5112, CBS 5287, CBS 7957,
RC Chevalieri / ATCC 10604 / CBS 405 / IFO 0258 / NRRL Y-1546, Fleischmann,
RC McPhie Sourdough, SAF, Sigma 1278B, Wyeast#1007, YJM 143, YJM 280, YJM 320,
RC YJM 326, and YJM 415;
RX PubMed=12177423; DOI=10.1073/pnas.162349599;
RA Edskes H.K., Wickner R.B.;
RT "Conservation of a portion of the S. cerevisiae Ure2p prion domain that
RT interacts with the full-length protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16384-16391(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP PRION FORMATION.
RX PubMed=7909170; DOI=10.1126/science.7909170;
RA Wickner R.B.;
RT "[URE3] as an altered URE2 protein: evidence for a prion analog in
RT Saccharomyces cerevisiae.";
RL Science 264:566-569(1994).
RN [7]
RP DOMAIN PRION.
RX PubMed=7569955; DOI=10.1126/science.270.5233.93;
RA Masison D.C., Wickner R.B.;
RT "Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in
RT prion-containing cells.";
RL Science 270:93-95(1995).
RN [8]
RP FUNCTION.
RX PubMed=8755910; DOI=10.1128/jb.178.15.4734-4736.1996;
RA Blinder D., Coschigano P.W., Magasanik B.;
RT "Interaction of the GATA factor Gln3p with the nitrogen regulator Ure2p in
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 178:4734-4736(1996).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10604478; DOI=10.1038/45287;
RA Beck T., Hall M.N.;
RT "The TOR signalling pathway controls nuclear localization of nutrient-
RT regulated transcription factors.";
RL Nature 402:689-692(1999).
RN [10]
RP FUNCTION.
RX PubMed=10799523; DOI=10.1074/jbc.275.19.14408;
RA Cunningham T.S., Andhare R., Cooper T.G.;
RT "Nitrogen catabolite repression of DAL80 expression depends on the relative
RT levels of Gat1p and Ure2p production in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:14408-14414(2000).
RN [11]
RP PRION FORMATION, AND PRION CURING.
RX PubMed=11073991; DOI=10.1128/mcb.20.23.8916-8922.2000;
RA Moriyama H., Edskes H.K., Wickner R.B.;
RT "[URE3] prion propagation in Saccharomyces cerevisiae: requirement for
RT chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.";
RL Mol. Cell. Biol. 20:8916-8922(2000).
RN [12]
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 [13]
RP FUNCTION.
RX PubMed=15371425; DOI=10.1074/jbc.m406612200;
RA Bai M., Zhou J.M., Perrett S.;
RT "The yeast prion protein Ure2 shows glutathione peroxidase activity in both
RT native and fibrillar forms.";
RL J. Biol. Chem. 279:50025-50030(2004).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ALA-122 AND ASN-124.
RX PubMed=19321443; DOI=10.1074/jbc.m901189200;
RA Zhang Z.R., Perrett S.;
RT "Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a
RT native-like dimer within fibrils.";
RL J. Biol. Chem. 284:14058-14067(2009).
RN [16]
RP INTERACTION WITH NNK1.
RX PubMed=20489023; DOI=10.1126/science.1176495;
RA Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA Nesvizhskii A.I., Tyers M.;
RT "A global protein kinase and phosphatase interaction network in yeast.";
RL Science 328:1043-1046(2010).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 95-354 IN COMPLEX WITH
RP GLUTATHIONE AND INHIBITORS.
RX PubMed=11695904; DOI=10.1021/bi011007b;
RA Bousset L., Belrhali H., Melki R., Morera S.;
RT "Crystal structures of the yeast prion Ure2p functional region in complex
RT with glutathione and related compounds.";
RL Biochemistry 40:13564-13573(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 97-354.
RX PubMed=11171973; DOI=10.1073/pnas.98.4.1459;
RA Umland T.C., Taylor K.L., Rhee S., Wickner R.B., Davies D.R.;
RT "The crystal structure of the nitrogen regulation fragment of the yeast
RT prion protein Ure2p.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1459-1464(2001).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-353.
RX PubMed=11342133; DOI=10.1016/s0969-2126(00)00553-0;
RA Bousset L., Belrhali H., Janin J., Melki R., Morera S.;
RT "Structure of the globular region of the prion protein Ure2 from the yeast
RT Saccharomyces cerevisiae.";
RL Structure 9:39-46(2001).
RN [21]
RP STRUCTURE BY NMR OF 10-39.
RX PubMed=16060675; DOI=10.1021/bi050724t;
RA Chan J.C., Oyler N.A., Yau W.M., Tycko R.;
RT "Parallel beta-sheets and polar zippers in amyloid fibrils formed by
RT residues 10-39 of the yeast prion protein Ure2p.";
RL Biochemistry 44:10669-10680(2005).
RN [22]
RP STRUCTURE BY NMR OF 1-89, AND DOMAIN PRION.
RX PubMed=17953455; DOI=10.1021/bi700826b;
RA Baxa U., Wickner R.B., Steven A.C., Anderson D.E., Marekov L.N., Yau W.M.,
RA Tycko R.;
RT "Characterization of beta-sheet structure in Ure2p(1-89) yeast prion
RT fibrils by solid-state nuclear magnetic resonance.";
RL Biochemistry 46:13149-13162(2007).
CC -!- FUNCTION: Plays an important role in nitrogen catabolite repression.
CC Down-regulates the expression of many genes involved in nitrogen
CC utilization by inhibiting the GATA transcriptional activators GLN3 and
CC GAT1. Under good nitrogen conditions, binds to the phosphorylated forms
CC of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing
CC transcription of genes expressed upon nitrogen limitation. Is also an
CC atypical glutaredoxin without a catalytical cysteine residue. Has
CC glutathione peroxidase and thiol:disulfide oxidoreductase activities in
CC both native and fibrillar form. Also shows insulin disulfide reductase
CC and dehydroascorbic acid reductase (DHAR) activities.
CC {ECO:0000269|PubMed:10604478, ECO:0000269|PubMed:10799523,
CC ECO:0000269|PubMed:15371425, ECO:0000269|PubMed:19321443,
CC ECO:0000269|PubMed:1990286, ECO:0000269|PubMed:8755910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC Evidence={ECO:0000269|PubMed:19321443};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for bis-(2-hydroxyethyl) disulfide (HEDS)
CC {ECO:0000269|PubMed:19321443};
CC Note=kcat is 1.2 sec(-1) with bis-(2-hydroxyethyl) disulfide (HEDS)
CC as substrate.;
CC -!- SUBUNIT: Homodimer. Interacts with NNK1. {ECO:0000269|PubMed:11695904,
CC ECO:0000269|PubMed:20489023}.
CC -!- INTERACTION:
CC P23202; P18494: GLN3; NbExp=2; IntAct=EBI-20138, EBI-7657;
CC P23202; P36003: NNK1; NbExp=4; IntAct=EBI-20138, EBI-9796;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10604478}.
CC -!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is
CC unstructured in its native, soluble form, and which forms a parallel
CC in-register beta-sheet in its amyloid form.
CC {ECO:0000269|PubMed:17953455, ECO:0000269|PubMed:7569955}.
CC -!- MISCELLANEOUS: [URE3] is the prion form of URE2. [URE3] is the result
CC of a conformational change of the cellular URE2 protein that becomes
CC self-propagating and infectious. This conformational change generates a
CC form of URE2 that assembles into amyloid fibrils. [URE3]-aggregates
CC sequester soluble URE2, which then fails to retain GLN3 in the
CC cytoplasm, resulting in GLN3 activation and consequently derepression
CC of genes that are required for utilization of poor nirogen sources
CC (PubMed:7909170). [URE3] can be cured by GdnHCl and by deletion of the
CC molecular chaperone HSP104, which is required for [URE3] propagation
CC (PubMed:11073991). {ECO:0000305|PubMed:11073991,
CC ECO:0000305|PubMed:7909170}.
CC -!- MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Mad yeast disease - Issue 47
CC of June 2004;
CC URL="https://web.expasy.org/spotlight/back_issues/047";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M35268; AAA35201.1; -; Genomic_DNA.
DR EMBL; AF525174; AAM93167.1; -; Genomic_DNA.
DR EMBL; AF525175; AAM93168.1; -; Genomic_DNA.
DR EMBL; AF525176; AAM93169.1; -; Genomic_DNA.
DR EMBL; AF525177; AAM93170.1; -; Genomic_DNA.
DR EMBL; AF525178; AAM93171.1; -; Genomic_DNA.
DR EMBL; AF525179; AAM93172.1; -; Genomic_DNA.
DR EMBL; AF525180; AAM93173.1; -; Genomic_DNA.
DR EMBL; AF525181; AAM93174.1; -; Genomic_DNA.
DR EMBL; AF525182; AAM93175.1; -; Genomic_DNA.
DR EMBL; AF525183; AAM93176.1; -; Genomic_DNA.
DR EMBL; AF525184; AAM93177.1; -; Genomic_DNA.
DR EMBL; AF525185; AAM93178.1; -; Genomic_DNA.
DR EMBL; AF525186; AAM93179.1; -; Genomic_DNA.
DR EMBL; AF525187; AAM93180.1; -; Genomic_DNA.
DR EMBL; AF525188; AAM93181.1; -; Genomic_DNA.
DR EMBL; AF525189; AAM93182.1; -; Genomic_DNA.
DR EMBL; AF525190; AAM93183.1; -; Genomic_DNA.
DR EMBL; AF525191; AAM93184.1; -; Genomic_DNA.
DR EMBL; AF525192; AAM93185.1; -; Genomic_DNA.
DR EMBL; Z69381; CAA93369.1; -; Genomic_DNA.
DR EMBL; Z71505; CAA96134.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10329.1; -; Genomic_DNA.
DR PIR; A39609; A39609.
DR RefSeq; NP_014170.1; NM_001183067.1.
DR PDB; 1G6W; X-ray; 2.50 A; A/B/C/D=94-354.
DR PDB; 1G6Y; X-ray; 2.80 A; A/B=94-354.
DR PDB; 1HQO; X-ray; 2.30 A; A/B=97-354.
DR PDB; 1JZR; X-ray; 2.90 A; A/B/C/D=95-354.
DR PDB; 1K0A; X-ray; 2.50 A; A/B=95-354.
DR PDB; 1K0B; X-ray; 2.50 A; A/B/C/D=95-354.
DR PDB; 1K0C; X-ray; 2.50 A; A/B/C/D=95-354.
DR PDB; 1K0D; X-ray; 2.20 A; A/B/C/D=95-354.
DR PDBsum; 1G6W; -.
DR PDBsum; 1G6Y; -.
DR PDBsum; 1HQO; -.
DR PDBsum; 1JZR; -.
DR PDBsum; 1K0A; -.
DR PDBsum; 1K0B; -.
DR PDBsum; 1K0C; -.
DR PDBsum; 1K0D; -.
DR AlphaFoldDB; P23202; -.
DR BMRB; P23202; -.
DR SMR; P23202; -.
DR BioGRID; 35609; 347.
DR DIP; DIP-1308N; -.
DR IntAct; P23202; 33.
DR MINT; P23202; -.
DR STRING; 4932.YNL229C; -.
DR MoonProt; P23202; -.
DR iPTMnet; P23202; -.
DR MaxQB; P23202; -.
DR PaxDb; P23202; -.
DR PRIDE; P23202; -.
DR EnsemblFungi; YNL229C_mRNA; YNL229C; YNL229C.
DR GeneID; 855492; -.
DR KEGG; sce:YNL229C; -.
DR SGD; S000005173; URE2.
DR VEuPathDB; FungiDB:YNL229C; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_14_1_1; -.
DR InParanoid; P23202; -.
DR OMA; KFFQNQP; -.
DR BioCyc; YEAST:YNL229C-MON; -.
DR EvolutionaryTrace; P23202; -.
DR PRO; PR:P23202; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P23202; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IMP:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0032447; P:protein urmylation; IMP:SGD.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IMP:SGD.
DR GO; GO:0010044; P:response to aluminum ion; IMP:SGD.
DR DisProt; DP00353; -.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017298; Ure2.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PIRSF; PIRSF037861; Prion_URE2; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amyloid; Cytoplasm; Nitrate assimilation;
KW Oxidoreductase; Prion; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..354
FT /note="Transcriptional regulator URE2"
FT /id="PRO_0000186013"
FT DOMAIN 112..196
FT /note="GST N-terminal"
FT DOMAIN 205..354
FT /note="GST C-terminal"
FT REGION 2..89
FT /note="Prion domain (PrD)"
FT REGION 22..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:11695904"
FT BINDING 151
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:11695904"
FT BINDING 164..165
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 180..181
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT MOD_RES 2
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 122
FT /note="A->S: Reduces glutaredoxin activity."
FT /evidence="ECO:0000269|PubMed:19321443"
FT MUTAGEN 124
FT /note="N->A,V: Abolishes glutaredoxin activity."
FT /evidence="ECO:0000269|PubMed:19321443"
FT MUTAGEN 313
FT /note="F->S: Destroys protein function."
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1K0D"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:1K0D"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1K0D"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1K0D"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1K0D"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:1K0D"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 206..222
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:1K0D"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1G6W"
FT HELIX 242..271
FT /evidence="ECO:0007829|PDB:1K0D"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1K0B"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:1G6W"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1G6W"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1G6W"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1G6W"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:1K0D"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:1K0D"
SQ SEQUENCE 354 AA; 40271 MW; 2C628976034B0F1C CRC64;
MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN SSSNNNNVQN
NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS RITKFFQEQP LEGYTLFSHR
SAPNGFKVAI VLSELGFHYN TIFLDFNLGE HRAPEFVSVN PNARVPALID HGMDNLSIWE
SGAILLHLVN KYYKETGNPL LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK
IASAVERYTD EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW
LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA LRGE
