GLRX2_YEAST
ID GLRX2_YEAST Reviewed; 143 AA.
AC P17695; D6VTD4; Q6B234;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Glutaredoxin-2 {ECO:0000303|PubMed:9571241};
DE EC=1.11.1.9 {ECO:0000269|PubMed:11875065};
DE EC=2.5.1.18 {ECO:0000269|PubMed:12684511};
DE AltName: Full=Glutathione-dependent oxidoreductase 2;
DE AltName: Full=Thioltransferase {ECO:0000303|PubMed:1530649};
DE Flags: Precursor;
GN Name=GRX2; Synonyms=TTR, TTR1; OrderedLocusNames=YDR513W;
GN ORFNames=D9719.17;
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].
RC STRAIN=DMY6;
RX PubMed=1530649; DOI=10.1016/0006-291x(92)91289-3;
RA Gan Z.-R.;
RT "Cloning and sequencing of a gene encoding yeast thioltransferase.";
RL Biochem. Biophys. Res. Commun. 187:949-955(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 31-45, AND PROCESSING BY MPP.
RX PubMed=20036764; DOI=10.1016/j.bbapap.2009.12.012;
RA Porras P., McDonagh B., Pedrajas J.R., Barcena J.A., Padilla C.A.;
RT "Structure and function of yeast glutaredoxin 2 depend on postranslational
RT processing and are related to subcellular distribution.";
RL Biochim. Biophys. Acta 1804:839-845(2010).
RN [6]
RP PROTEIN SEQUENCE OF 36-141.
RX PubMed=2189409; DOI=10.1016/0006-291x(90)91120-h;
RA Gan Z.-R., Polokoff M.A., Jacobs J.W., Sardana M.K.;
RT "Complete amino acid sequence of yeast thioltransferase (glutaredoxin).";
RL Biochem. Biophys. Res. Commun. 168:944-951(1990).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=9571241; DOI=10.1091/mbc.9.5.1081;
RA Luikenhuis S., Perrone G., Dawes I.W., Grant C.M.;
RT "The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that
RT are required for protection against reactive oxygen species.";
RL Mol. Biol. Cell 9:1081-1091(1998).
RN [8]
RP INDUCTION.
RX PubMed=10786615; DOI=10.1016/s0167-4781(99)00234-1;
RA Grant C.M., Luikenhuis S., Beckhouse A., Soderbergh M., Dawes I.W.;
RT "Differential regulation of glutaredoxin gene expression in response to
RT stress conditions in the yeast Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1490:33-42(2000).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11958675; DOI=10.1042/bj20020570;
RA Pedrajas J.R., Porras P., Martinez-Galisteo E., Padilla C.A.,
RA Miranda-Vizuete A., Barcena J.A.;
RT "Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in
RT vivo and localize to different subcellular compartments.";
RL Biochem. J. 364:617-623(2002).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11875065; DOI=10.1074/jbc.m111686200;
RA Collinson E.J., Wheeler G.L., Garrido E.O., Avery A.M., Avery S.V.,
RA Grant C.M.;
RT "The yeast glutaredoxins are active as glutathione peroxidases.";
RL J. Biol. Chem. 277:16712-16717(2002).
RN [11]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12684511; DOI=10.1074/jbc.m301387200;
RA Collinson E.J., Grant C.M.;
RT "Role of yeast glutaredoxins as glutathione S-transferases.";
RL J. Biol. Chem. 278:22492-22497(2003).
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 ALTERNATIVE INITIATION.
RX PubMed=16606613; DOI=10.1074/jbc.m600790200;
RA Porras P., Padilla C.A., Krayl M., Voos W., Barcena J.A.;
RT "One single in-frame AUG codon is responsible for a diversity of
RT subcellular localizations of glutaredoxin 2 in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 281:16551-16562(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-91, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP 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).
RN [16]
RP FUNCTION.
RX PubMed=21565288; DOI=10.1016/j.jprot.2011.04.018;
RA McDonagh B., Requejo R., Fuentes-Almagro C.A., Ogueta S., Barcena J.A.,
RA Padilla C.A.;
RT "Thiol redox proteomics identifies differential targets of cytosolic and
RT mitochondrial glutaredoxin-2 isoforms in Saccharomyces cerevisiae.
RT Reversible S-glutathionylation of DHBP synthase (RIB3).";
RL J. Proteomics 74:2487-2497(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 35-143 IN COMPLEX WITH
RP GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GLUTATHIONYLATION AT
RP CYS-61, AND MUTAGENESIS OF CYS-64.
RX PubMed=18992757; DOI=10.1016/j.jmb.2008.10.055;
RA Discola K.F., de Oliveira M.A., Rosa Cussiol J.R., Monteiro G.,
RA Barcena J.A., Porras P., Padilla C.A., Guimaraes B.G., Netto L.E.;
RT "Structural aspects of the distinct biochemical properties of glutaredoxin
RT 1 and glutaredoxin 2 from Saccharomyces cerevisiae.";
RL J. Mol. Biol. 385:889-901(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 35-143 IN COMPLEX WITH
RP GLUTATHIONE, DISULFIDE BOND, MUTAGENESIS OF SER-123, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20417731; DOI=10.1016/j.bbapap.2010.04.010;
RA Li W.F., Yu J., Ma X.X., Teng Y.B., Luo M., Tang Y.J., Zhou C.Z.;
RT "Structural basis for the different activities of yeast Grx1 and Grx2.";
RL Biochim. Biophys. Acta 1804:1542-1547(2010).
CC -!- FUNCTION: Component of the glutathione system which performs several
CC activities such as glutathione-dependent oxidoreductase, glutathione
CC peroxidase and glutathione S-transferase (GST) activity
CC (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an
CC electron carrier in the glutathione-dependent synthesis of
CC deoxyribonucleotides by the enzyme ribonucleotide reductase. In
CC addition, it is also involved in reducing cytosolic protein- and non-
CC protein-disulfides in a coupled system with glutathione reductase.
CC Required for resistance to reactive oxygen species (ROS) by directly
CC reducing hydroperoxides and for the detoxification of ROS-mediated
CC damage. GRX2 is more active as an oxidoreductase than GRX1
CC (PubMed:9571241, PubMed:18992757, PubMed:20417731). Responsible for the
CC S-glutathionylation of DHBP synthase (PubMed:21565288).
CC {ECO:0000269|PubMed:11875065, ECO:0000269|PubMed:12684511,
CC ECO:0000269|PubMed:18992757, ECO:0000269|PubMed:20417731,
CC ECO:0000269|PubMed:21565288, ECO:0000269|PubMed:9571241}.
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:11875065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:12684511};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:12684511};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for H(2)O(2) {ECO:0000269|PubMed:12684511};
CC KM=2.2 mM for tert-butyl hydroperoxide {ECO:0000269|PubMed:12684511};
CC KM=0.87 mM for cumene hydroperoxide {ECO:0000269|PubMed:12684511};
CC KM=0.17 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:12684511};
CC KM=0.27 mM for 1,2-dichloro-4-nitrobenzene
CC {ECO:0000269|PubMed:12684511};
CC KM=0.9 mM for reduced glutathione {ECO:0000269|PubMed:18992757};
CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm
CC {ECO:0000269|PubMed:11958675, ECO:0000269|PubMed:16606613}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000269|PubMed:11958675, ECO:0000269|PubMed:16606613}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial {ECO:0000303|PubMed:11958675};
CC IsoId=P17695-1; Sequence=Displayed;
CC Name=Cytoplasmic {ECO:0000303|PubMed:11958675};
CC IsoId=P17695-2; Sequence=VSP_060434;
CC -!- INDUCTION: In response to exposure to reactive oxygen species (ROS) and
CC upon entry into stationary phase. {ECO:0000269|PubMed:10786615,
CC ECO:0000269|PubMed:9571241}.
CC -!- MISCELLANEOUS: Present with 31400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: It is unclear whether the long polypeptide observed in
CC mitochondria represents the immature form of the protein before
CC cleavage of the transit peptide and release of the short form into the
CC cytoplasm or whether two mature isoforms exists.
CC {ECO:0000305|PubMed:16606613, ECO:0000305|PubMed:20036764}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB23389.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S45268; AAB23389.1; ALT_INIT; Genomic_DNA.
DR EMBL; U33057; AAB64953.1; -; Genomic_DNA.
DR EMBL; AY692896; AAT92915.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12344.1; -; Genomic_DNA.
DR PIR; S69570; GDBY.
DR RefSeq; NP_010801.1; NM_001180821.1. [P17695-1]
DR PDB; 3CTF; X-ray; 2.10 A; A=35-143.
DR PDB; 3CTG; X-ray; 1.50 A; A=35-143.
DR PDB; 3D4M; X-ray; 2.05 A; A=35-143.
DR PDB; 3D5J; X-ray; 1.91 A; A/B=35-143.
DR PDBsum; 3CTF; -.
DR PDBsum; 3CTG; -.
DR PDBsum; 3D4M; -.
DR PDBsum; 3D5J; -.
DR AlphaFoldDB; P17695; -.
DR SMR; P17695; -.
DR BioGRID; 32563; 105.
DR DIP; DIP-5271N; -.
DR IntAct; P17695; 1.
DR STRING; 4932.YDR513W; -.
DR iPTMnet; P17695; -.
DR MaxQB; P17695; -.
DR PaxDb; P17695; -.
DR PRIDE; P17695; -.
DR EnsemblFungi; YDR513W_mRNA; YDR513W; YDR513W. [P17695-1]
DR GeneID; 852124; -.
DR KEGG; sce:YDR513W; -.
DR SGD; S000002921; GRX2.
DR VEuPathDB; FungiDB:YDR513W; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00940000162420; -.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; P17695; -.
DR OMA; GRTTFPQ; -.
DR BioCyc; YEAST:MON3O-490; -.
DR SABIO-RK; P17695; -.
DR EvolutionaryTrace; P17695; -.
DR PRO; PR:P17695; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P17695; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IMP:SGD.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:SGD.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IGI:SGD.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Glutathionylation; Mitochondrion;
KW Oxidoreductase; Phosphoprotein; Redox-active center; Reference proteome;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:20036764,
FT ECO:0000305|PubMed:16606613"
FT CHAIN 31..143
FT /note="Glutaredoxin-2"
FT /id="PRO_0000141612"
FT DOMAIN 41..143
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 58..63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18992757"
FT BINDING 109
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18992757"
FT BINDING 122..123
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18992757"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 61
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:18992757"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT DISULFID 61..64
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000269|PubMed:20417731"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000269|PubMed:16606613,
FT ECO:0000269|PubMed:2189409"
FT /id="VSP_060434"
FT MUTAGEN 1
FT /note="M->V: Loss of the mitochondrial isoform."
FT /evidence="ECO:0000269|PubMed:16606613"
FT MUTAGEN 35
FT /note="M->V: Loss of the cytoplasmic isoform."
FT /evidence="ECO:0000269|PubMed:16606613"
FT MUTAGEN 64
FT /note="C->S: Leads to 30 percent decreased oxidoreductase
FT activity."
FT /evidence="ECO:0000269|PubMed:18992757"
FT MUTAGEN 123
FT /note="S->D: Leads to decreased oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:20417731"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:3CTG"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3CTG"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:3CTG"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3CTG"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3CTG"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3CTG"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:3CTG"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3CTG"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3CTG"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:3CTG"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:3CTG"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:3CTG"
FT INIT_MET P17695-2:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16606613"
SQ SEQUENCE 143 AA; 15861 MW; 99A79B87695B2266 CRC64;
METNFSFDSN LIVIIIITLF ATRIIAKRFL STPKMVSQET VAHVKDLIGQ KEVFVAAKTY
CPYCKATLST LFQELNVPKS KALVLELDEM SNGSEIQDAL EEISGQKTVP NVYINGKHIG
GNSDLETLKK NGKLAEILKP VFQ
