GRE2_YEAST
ID GRE2_YEAST Reviewed; 342 AA.
AC Q12068; D6W1R9;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=NADPH-dependent methylglyoxal reductase GRE2;
DE EC=1.1.1.283 {ECO:0000269|PubMed:12722185, ECO:0000269|PubMed:16999827, ECO:0000269|PubMed:3896793};
DE AltName: Full=3-methylbutanal reductase;
DE EC=1.1.1.265 {ECO:0000269|PubMed:16999827};
DE AltName: Full=Genes de respuesta a estres protein 2;
DE AltName: Full=Isovaleraldehyde reductase;
GN Name=GRE2; OrderedLocusNames=YOL151W;
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=ATCC 96604 / S288c / FY1679;
RX PubMed=8553699; DOI=10.1002/yea.320111308;
RA Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J.,
RA Gancedo C., Arino J.;
RT "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
RT chromosome XV containing seven new open reading frames.";
RL Yeast 11:1281-1288(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3896793; DOI=10.1111/j.1432-1033.1985.tb09151.x;
RA Murata K., Fukuda Y., Simosaka M., Watanabe K., Saikusa T., Kimura A.;
RT "Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization
RT of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces
RT cerevisiae.";
RL Eur. J. Biochem. 151:631-636(1985).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12722185; DOI=10.1002/yea.979;
RA Chen C.N., Porubleva L., Shearer G., Svrakic M., Holden L.G., Dover J.L.,
RA Johnston M., Chitnis P.R., Kohl D.H.;
RT "Associating protein activities with their genes: rapid identification of a
RT gene encoding a methylglyoxal reductase in the yeast Saccharomyces
RT cerevisiae.";
RL Yeast 20:545-554(2003).
RN [7]
RP INDUCTION.
RX PubMed=10407268;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<879::aid-yea428>3.0.co;2-q;
RA Garay-Arroyo A., Covarrubias A.A.;
RT "Three genes whose expression is induced by stress in Saccharomyces
RT cerevisiae.";
RL Yeast 15:879-892(1999).
RN [8]
RP INDUCTION.
RX PubMed=10347154; DOI=10.1074/jbc.274.23.16040;
RA Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J.,
RA Toledano M.B.;
RT "Yap1 and Skn7 control two specialized oxidative stress response regulons
RT in yeast.";
RL J. Biol. Chem. 274:16040-16046(1999).
RN [9]
RP INDUCTION.
RX PubMed=11401713; DOI=10.1046/j.1365-2958.2001.02384.x;
RA Rep M., Proft M., Remize F., Tamas M., Serrano R., Thevelein J.M.,
RA Hohmann S.;
RT "The Saccharomyces cerevisiae Sko1p transcription factor mediates HOG
RT pathway-dependent osmotic regulation of a set of genes encoding enzymes
RT implicated in protection from oxidative damage.";
RL Mol. Microbiol. 40:1067-1083(2001).
RN [10]
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 [11]
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 [12]
RP FUNCTION.
RX PubMed=16598690; DOI=10.1002/yea.1363;
RA Warringer J., Blomberg A.;
RT "Involvement of yeast YOL151W/GRE2 in ergosterol metabolism.";
RL Yeast 23:389-398(2006).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16999827; DOI=10.1111/j.1567-1364.2006.00151.x;
RA Hauser M., Horn P., Tournu H., Hauser N.C., Hoheisel J.D., Brown A.J.,
RA Dickinson J.R.;
RT "A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast
RT reveals a novel role for Gre2p as isovaleraldehyde reductase.";
RL FEMS Yeast Res. 7:84-92(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP 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 BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RX PubMed=20111861; DOI=10.1007/s00253-010-2442-5;
RA Choi Y.H., Choi H.J., Kim D., Uhm K.N., Kim H.K.;
RT "Asymmetric synthesis of (S)-3-chloro-1-phenyl-1-propanol using
RT Saccharomyces cerevisiae reductase with high enantioselectivity.";
RL Appl. Microbiol. Biotechnol. 87:185-193(2010).
RN [16]
RP BIOTECHNOLOGY, AND MUTAGENESIS OF ASN-9.
RX PubMed=20480039; DOI=10.3390/ijms11041735;
RA Katzberg M., Skorupa-Parachin N., Gorwa-Grauslund M.F., Bertau M.;
RT "Engineering cofactor preference of ketone reducing biocatalysts: A
RT mutagenesis study on a gamma-diketone reductase from the yeast
RT Saccharomyces cerevisiae serving as an example.";
RL Int. J. Mol. Sci. 11:1735-1758(2010).
RN [17]
RP BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBUNIT, AND SUBSTRATE SPECIFICITY.
RX PubMed=20237665; DOI=10.1039/b920869k;
RA Muller M., Katzberg M., Bertau M., Hummel W.;
RT "Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol
RT with a dehydrogenase from Saccharomyces cerevisiae.";
RL Org. Biomol. Chem. 8:1540-1550(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
RX PubMed=24879127; DOI=10.1016/j.bbapap.2014.05.008;
RA Guo P.C., Bao Z.Z., Ma X.X., Xia Q., Li W.F.;
RT "Structural insights into the cofactor-assisted substrate recognition of
RT yeast methylglyoxal/isovaleraldehyde reductase Gre2.";
RL Biochim. Biophys. Acta 1844:1486-1492(2014).
CC -!- FUNCTION: Catalyzes the irreversible reduction of the cytotoxic
CC compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde as an
CC alternative to detoxification of MG by glyoxalase I GLO1. MG is
CC synthesized via a bypath of glycolysis from dihydroxyacetone phosphate
CC and is believed to play a role in cell cycle regulation and stress
CC adaptation. Also catalyzes the reduction of 3-methylbutanal to 3-
CC methylbutanol. Acts as a suppressor of 3-methylbutanol-induced
CC filamentation by modulating the levels of 3-methylbutanal, the signal
CC to which cells respond by filamentation. Also involved in ergosterol
CC metabolism. {ECO:0000269|PubMed:12722185, ECO:0000269|PubMed:16598690,
CC ECO:0000269|PubMed:16999827, ECO:0000269|PubMed:3896793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactaldehyde + NADP(+) = H(+) + methylglyoxal + NADPH;
CC Xref=Rhea:RHEA:21748, ChEBI:CHEBI:15378, ChEBI:CHEBI:17158,
CC ChEBI:CHEBI:18041, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.283; Evidence={ECO:0000269|PubMed:12722185,
CC ECO:0000269|PubMed:16999827, ECO:0000269|PubMed:3896793};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanol + NADP(+) = 3-methylbutanal + H(+) + NADPH;
CC Xref=Rhea:RHEA:18525, ChEBI:CHEBI:15378, ChEBI:CHEBI:15837,
CC ChEBI:CHEBI:16638, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.265; Evidence={ECO:0000269|PubMed:16999827};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanol + NAD(+) = 3-methylbutanal + H(+) + NADH;
CC Xref=Rhea:RHEA:18529, ChEBI:CHEBI:15378, ChEBI:CHEBI:15837,
CC ChEBI:CHEBI:16638, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.265; Evidence={ECO:0000269|PubMed:16999827};
CC -!- ACTIVITY REGULATION: Activated by glutathione.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.88 mM for methylglyoxal {ECO:0000269|PubMed:3896793};
CC KM=1.54 mM for phenylglyoxal {ECO:0000269|PubMed:3896793};
CC KM=0.14 mM for 3-methylbutanal {ECO:0000269|PubMed:24879127};
CC KM=0.192 mM for 3-chloro-1-phenyl-1-propanol
CC {ECO:0000269|PubMed:20111861, ECO:0000269|PubMed:20237665};
CC KM=4.33 mM for 2,5-hexanedione {ECO:0000269|PubMed:20111861,
CC ECO:0000269|PubMed:20237665};
CC KM=10.48 mM for (2S,5S)-hexanediol {ECO:0000269|PubMed:20111861,
CC ECO:0000269|PubMed:20237665};
CC KM=0.112 mM for NADPH {ECO:0000269|PubMed:20111861,
CC ECO:0000269|PubMed:20237665};
CC Note=kcat is 31.3 min(-1) with 3-chloro-1-phenyl-1-propanol as
CC substrate and 29.1 min(-1) for NADPH.;
CC pH dependence:
CC Optimum pH is 7 for 2,5-hexanedione reduction, and 10 for the reverse
CC reaction. {ECO:0000269|PubMed:20111861, ECO:0000269|PubMed:20237665};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius for 3-chloro-1-phenyl-1-
CC propanol reduction, and 54 degrees Celsius for 2,5-hexanedione
CC reduction, and 30 degrees Celsius for the reverse reaction.
CC {ECO:0000269|PubMed:20111861, ECO:0000269|PubMed:20237665};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20237665}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Repressed by SKO1. During osmotic stress, this repression is
CC relieved. Induced by transcription factor YAP1 during oxidative stress,
CC and induced by ionic and heat stress. Induced by isoamylalcohol.
CC {ECO:0000269|PubMed:10347154, ECO:0000269|PubMed:10407268,
CC ECO:0000269|PubMed:11401713, ECO:0000269|PubMed:16999827}.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISRUPTION PHENOTYPE: Causes hyperfilamentation, probably due to the
CC elevated levels of 3-methylbutanal in the mutant.
CC {ECO:0000269|PubMed:16999827}.
CC -!- BIOTECHNOLOGY: Used as a biocatalyst, because the enzyme accepts a
CC broad range of substrates including aliphatic and aromatic ketones,
CC chloroketones, diketones as well as beta-ketoesters which are reduced
CC with high stereoselectivity. {ECO:0000269|PubMed:20111861,
CC ECO:0000269|PubMed:20480039}.
CC -!- MISCELLANEOUS: Present with 5458 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: 'De respuesta a estres' means stress response in
CC Spanish.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; Z48239; CAA88277.1; -; Genomic_DNA.
DR EMBL; Z74893; CAA99172.1; -; Genomic_DNA.
DR EMBL; AY558040; AAS56366.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10635.1; -; Genomic_DNA.
DR PIR; S60386; S60386.
DR RefSeq; NP_014490.1; NM_001183405.1.
DR PDB; 4PVC; X-ray; 2.00 A; A/B=1-342.
DR PDB; 4PVD; X-ray; 2.40 A; A/B/C/D=1-342.
DR PDBsum; 4PVC; -.
DR PDBsum; 4PVD; -.
DR AlphaFoldDB; Q12068; -.
DR SMR; Q12068; -.
DR BioGRID; 34267; 60.
DR DIP; DIP-2645N; -.
DR IntAct; Q12068; 1.
DR MINT; Q12068; -.
DR STRING; 4932.YOL151W; -.
DR iPTMnet; Q12068; -.
DR MaxQB; Q12068; -.
DR PaxDb; Q12068; -.
DR PRIDE; Q12068; -.
DR EnsemblFungi; YOL151W_mRNA; YOL151W; YOL151W.
DR GeneID; 854014; -.
DR KEGG; sce:YOL151W; -.
DR SGD; S000005511; GRE2.
DR VEuPathDB; FungiDB:YOL151W; -.
DR eggNOG; KOG1502; Eukaryota.
DR GeneTree; ENSGT00940000176317; -.
DR HOGENOM; CLU_007383_9_2_1; -.
DR InParanoid; Q12068; -.
DR OMA; ATIWIDV; -.
DR BioCyc; MetaCyc:YOL151W-MON; -.
DR BioCyc; YEAST:YOL151W-MON; -.
DR BRENDA; 1.1.1.265; 984.
DR BRENDA; 1.1.1.283; 984.
DR SABIO-RK; Q12068; -.
DR PRO; PR:Q12068; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12068; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0052676; F:3-methylbutanol:NAD oxidoreductase activity; IEA:RHEA.
DR GO; GO:0046568; F:3-methylbutanol:NAD(P) oxidoreductase activity; IMP:SGD.
DR GO; GO:0052675; F:3-methylbutanol:NADP oxidoreductase activity; IEA:RHEA.
DR GO; GO:0043892; F:methylglyoxal reductase (NADPH-dependent) activity; IDA:SGD.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0008204; P:ergosterol metabolic process; IMP:SGD.
DR GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..342
FT /note="NADPH-dependent methylglyoxal reductase GRE2"
FT /id="PRO_0000215576"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:24879127"
FT BINDING 7..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT BINDING 32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT BINDING 57..58
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT BINDING 199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT BINDING 216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24879127"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 9
FT /note="N->E: Alters cofactor preference of the enzyme to be
FT able to use as well NAD instead of NADP."
FT /evidence="ECO:0000269|PubMed:20480039"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 161..182
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 284..289
FT /evidence="ECO:0007829|PDB:4PVC"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:4PVC"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:4PVC"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:4PVC"
SQ SEQUENCE 342 AA; 38170 MW; 84DC286AAD8C88D2 CRC64;
MSVFVSGANG FIAQHIVDLL LKEDYKVIGS ARSQEKAENL TEAFGNNPKF SMEVVPDISK
LDAFDHVFQK HGKDIKIVLH TASPFCFDIT DSERDLLIPA VNGVKGILHS IKKYAADSVE
RVVLTSSYAA VFDMAKENDK SLTFNEESWN PATWESCQSD PVNAYCGSKK FAEKAAWEFL
EENRDSVKFE LTAVNPVYVF GPQMFDKDVK KHLNTSCELV NSLMHLSPED KIPELFGGYI
DVRDVAKAHL VAFQKRETIG QRLIVSEARF TMQDVLDILN EDFPVLKGNI PVGKPGSGAT
HNTLGATLDN KKSKKLLGFK FRNLKETIDD TASQILKFEG RI
