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NADPH-dependent methylglyoxal reductase GRE2 (EC 1.1.1.283) (3-methylbutanal reductase) (EC 1.1.1.265) (Genes de respuesta a estres protein 2) (Isovaleraldehyde reductase)

 GRE2_YEAST              Reviewed;         342 AA.
Q12068; D6W1R9;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=NADPH-dependent methylglyoxal reductase GRE2;
EC=1.1.1.283 {ECO:0000269|PubMed:12722185, ECO:0000269|PubMed:16999827, ECO:0000269|PubMed:3896793};
AltName: Full=3-methylbutanal reductase;
EC=1.1.1.265 {ECO:0000269|PubMed:16999827};
AltName: Full=Genes de respuesta a estres protein 2;
AltName: Full=Isovaleraldehyde reductase;
Name=GRE2; OrderedLocusNames=YOL151W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8553699; DOI=10.1002/yea.320111308;
Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J.,
Lafuente M.J., Gancedo C., Arino J.;
"DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
chromosome XV containing seven new open reading frames.";
Yeast 11:1281-1288(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=3896793; DOI=10.1111/j.1432-1033.1985.tb09151.x;
Murata K., Fukuda Y., Simosaka M., Watanabe K., Saikusa T., Kimura A.;
"Metabolism of 2-oxoaldehyde in yeasts. Purification and
characterization of NADPH-dependent methylglyoxal-reducing enzyme from
Saccharomyces cerevisiae.";
Eur. J. Biochem. 151:631-636(1985).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12722185; DOI=10.1002/yea.979;
Chen C.N., Porubleva L., Shearer G., Svrakic M., Holden L.G.,
Dover J.L., Johnston M., Chitnis P.R., Kohl D.H.;
"Associating protein activities with their genes: rapid identification
of a gene encoding a methylglyoxal reductase in the yeast
Saccharomyces cerevisiae.";
Yeast 20:545-554(2003).
[7]
INDUCTION.
PubMed=10407268;
DOI=10.1002/(SICI)1097-0061(199907)15:10A<879::AID-YEA428>3.0.CO;2-Q;
Garay-Arroyo A., Covarrubias A.A.;
"Three genes whose expression is induced by stress in Saccharomyces
cerevisiae.";
Yeast 15:879-892(1999).
[8]
INDUCTION.
PubMed=10347154; DOI=10.1074/jbc.274.23.16040;
Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J.,
Toledano M.B.;
"Yap1 and Skn7 control two specialized oxidative stress response
regulons in yeast.";
J. Biol. Chem. 274:16040-16046(1999).
[9]
INDUCTION.
PubMed=11401713; DOI=10.1046/j.1365-2958.2001.02384.x;
Rep M., Proft M., Remize F., Tamas M., Serrano R., Thevelein J.M.,
Hohmann S.;
"The Saccharomyces cerevisiae Sko1p transcription factor mediates HOG
pathway-dependent osmotic regulation of a set of genes encoding
enzymes implicated in protection from oxidative damage.";
Mol. Microbiol. 40:1067-1083(2001).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
FUNCTION.
PubMed=16598690; DOI=10.1002/yea.1363;
Warringer J., Blomberg A.;
"Involvement of yeast YOL151W/GRE2 in ergosterol metabolism.";
Yeast 23:389-398(2006).
[13]
FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=16999827; DOI=10.1111/j.1567-1364.2006.00151.x;
Hauser M., Horn P., Tournu H., Hauser N.C., Hoheisel J.D., Brown A.J.,
Dickinson J.R.;
"A transcriptome analysis of isoamyl alcohol-induced filamentation in
yeast reveals a novel role for Gre2p as isovaleraldehyde reductase.";
FEMS Yeast Res. 7:84-92(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[15]
BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
PubMed=20111861; DOI=10.1007/s00253-010-2442-5;
Choi Y.H., Choi H.J., Kim D., Uhm K.N., Kim H.K.;
"Asymmetric synthesis of (S)-3-chloro-1-phenyl-1-propanol using
Saccharomyces cerevisiae reductase with high enantioselectivity.";
Appl. Microbiol. Biotechnol. 87:185-193(2010).
[16]
BIOTECHNOLOGY, AND MUTAGENESIS OF ASN-9.
PubMed=20480039; DOI=10.3390/ijms11041735;
Katzberg M., Skorupa-Parachin N., Gorwa-Grauslund M.F., Bertau M.;
"Engineering cofactor preference of ketone reducing biocatalysts: A
mutagenesis study on a gamma-diketone reductase from the yeast
Saccharomyces cerevisiae serving as an example.";
Int. J. Mol. Sci. 11:1735-1758(2010).
[17]
BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY,
SUBUNIT, AND SUBSTRATE SPECIFICITY.
PubMed=20237665; DOI=10.1039/b920869k;
Muller M., Katzberg M., Bertau M., Hummel W.;
"Highly efficient and stereoselective biosynthesis of (2S,5S)-
hexanediol with a dehydrogenase from Saccharomyces cerevisiae.";
Org. Biomol. Chem. 8:1540-1550(2010).
[18]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP,
BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
PubMed=24879127; DOI=10.1016/j.bbapap.2014.05.008;
Guo P.C., Bao Z.Z., Ma X.X., Xia Q., Li W.F.;
"Structural insights into the cofactor-assisted substrate recognition
of yeast methylglyoxal/isovaleraldehyde reductase Gre2.";
Biochim. Biophys. Acta 1844:1486-1492(2014).
-!- FUNCTION: Catalyzes the irreversible reduction of the cytotoxic
compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde as
an alternative to detoxification of MG by glyoxalase I GLO1. MG is
synthesized via a bypath of glycolysis from dihydroxyacetone
phosphate and is believed to play a role in cell cycle regulation
and stress adaptation. Also catalyzes the reduction of 3-
methylbutanal to 3-methylbutanol. Acts as a suppressor of 3-
methylbutanol-induced filamentation by modulating the levels of 3-
methylbutanal, the signal to which cells respond by filamentation.
Also involved in ergosterol metabolism.
{ECO:0000269|PubMed:12722185, ECO:0000269|PubMed:16598690,
ECO:0000269|PubMed:16999827, ECO:0000269|PubMed:3896793}.
-!- CATALYTIC ACTIVITY: (S)-lactaldehyde + NADP(+) = 2-oxopropanal +
NADPH. {ECO:0000269|PubMed:12722185, ECO:0000269|PubMed:16999827,
ECO:0000269|PubMed:3896793}.
-!- CATALYTIC ACTIVITY: 3-methylbutanol + NAD(P)(+) = 3-methylbutanal
+ NAD(P)H. {ECO:0000269|PubMed:16999827}.
-!- ENZYME REGULATION: Activated by glutathione.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.88 mM for methylglyoxal {ECO:0000269|PubMed:3896793};
KM=1.54 mM for phenylglyoxal {ECO:0000269|PubMed:3896793};
KM=0.14 mM for 3-methylbutanal {ECO:0000269|PubMed:24879127};
KM=0.192 mM for 3-chloro-1-phenyl-1-propanol
{ECO:0000269|PubMed:20111861, ECO:0000269|PubMed:20237665};
KM=4.33 mM for 2,5-hexanedione {ECO:0000269|PubMed:20111861,
ECO:0000269|PubMed:20237665};
KM=10.48 mM for (2S,5S)-hexanediol {ECO:0000269|PubMed:20111861,
ECO:0000269|PubMed:20237665};
KM=0.112 mM for NADPH {ECO:0000269|PubMed:20111861,
ECO:0000269|PubMed:20237665};
Note=kcat is 31.3 min(-1) with 3-chloro-1-phenyl-1-propanol as
substrate and 29.1 min(-1) for NADPH.;
pH dependence:
Optimum pH is 7 for 2,5-hexanedione reduction, and 10 for the
reverse reaction. {ECO:0000269|PubMed:20111861,
ECO:0000269|PubMed:20237665};
Temperature dependence:
Optimum temperature is 40 degrees Celsius for 3-chloro-1-phenyl-
1-propanol reduction, and 54 degrees Celsius for 2,5-hexanedione
reduction, and 30 degrees Celsius for the reverse reaction.
{ECO:0000269|PubMed:20111861, ECO:0000269|PubMed:20237665};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20237665}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- INDUCTION: Repressed by SKO1. During osmotic stress, this
repression is relieved. Induced by transcription factor YAP1
during oxidative stress, and induced by ionic and heat stress.
Induced by isoamylalcohol. {ECO:0000269|PubMed:10347154,
ECO:0000269|PubMed:10407268, ECO:0000269|PubMed:11401713,
ECO:0000269|PubMed:16999827}.
-!- PTM: The N-terminus is blocked.
-!- DISRUPTION PHENOTYPE: Causes hyperfilamentation, probably due to
the elevated levels of 3-methylbutanal in the mutant.
{ECO:0000269|PubMed:16999827}.
-!- BIOTECHNOLOGY: Used as a biocatalyst, because the enzyme accepts a
broad range of substrates including aliphatic and aromatic
ketones, chloroketones, diketones as well as beta-ketoesters which
are reduced with high stereoselectivity.
{ECO:0000269|PubMed:20111861, ECO:0000269|PubMed:20480039}.
-!- MISCELLANEOUS: Present with 5458 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: 'De respuesta a estres' means stress response in
Spanish.
-!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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EMBL; Z48239; CAA88277.1; -; Genomic_DNA.
EMBL; Z74893; CAA99172.1; -; Genomic_DNA.
EMBL; AY558040; AAS56366.1; -; Genomic_DNA.
EMBL; BK006948; DAA10635.1; -; Genomic_DNA.
PIR; S60386; S60386.
RefSeq; NP_014490.1; NM_001183405.1.
PDB; 4PVC; X-ray; 2.00 A; A/B=1-342.
PDB; 4PVD; X-ray; 2.40 A; A/B/C/D=1-342.
PDBsum; 4PVC; -.
PDBsum; 4PVD; -.
ProteinModelPortal; Q12068; -.
SMR; Q12068; -.
BioGrid; 34267; 55.
DIP; DIP-2645N; -.
IntAct; Q12068; 1.
MINT; MINT-425047; -.
STRING; 4932.YOL151W; -.
iPTMnet; Q12068; -.
MaxQB; Q12068; -.
PRIDE; Q12068; -.
EnsemblFungi; YOL151W; YOL151W; YOL151W.
GeneID; 854014; -.
KEGG; sce:YOL151W; -.
EuPathDB; FungiDB:YOL151W; -.
SGD; S000005511; GRE2.
GeneTree; ENSGT00390000002618; -.
HOGENOM; HOG000167998; -.
InParanoid; Q12068; -.
KO; K17741; -.
OMA; HTYNEAD; -.
OrthoDB; EOG092C3RD2; -.
BioCyc; MetaCyc:YOL151W-MONOMER; -.
BioCyc; YEAST:YOL151W-MONOMER; -.
PRO; PR:Q12068; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
GO; GO:0046568; F:3-methylbutanol:NAD(P) oxidoreductase activity; IMP:SGD.
GO; GO:0043892; F:methylglyoxal reductase (NADPH-dependent) activity; IDA:SGD.
GO; GO:0008204; P:ergosterol metabolic process; IMP:SGD.
GO; GO:0030447; P:filamentous growth; IMP:SGD.
GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01073; 3Beta_HSD; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; NADP; Nucleus;
Oxidoreductase; Phosphoprotein; Reference proteome.
CHAIN 1 342 NADPH-dependent methylglyoxal reductase
GRE2.
/FTId=PRO_0000215576.
NP_BIND 7 12 NADP. {ECO:0000269|PubMed:24879127}.
NP_BIND 57 58 NADP. {ECO:0000269|PubMed:24879127}.
ACT_SITE 169 169 Proton donor.
{ECO:0000305|PubMed:24879127}.
BINDING 32 32 NADP. {ECO:0000269|PubMed:24879127}.
BINDING 36 36 NADP. {ECO:0000269|PubMed:24879127}.
BINDING 165 165 NADP. {ECO:0000269|PubMed:24879127}.
BINDING 169 169 NADP. {ECO:0000269|PubMed:24879127}.
BINDING 199 199 NADP; via amide nitrogen.
{ECO:0000269|PubMed:24879127}.
BINDING 216 216 NADP. {ECO:0000269|PubMed:24879127}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 9 9 N->E: Alters cofactor preference of the
enzyme to be able to use as well NAD
instead of NADP.
{ECO:0000269|PubMed:20480039}.
STRAND 3 6 {ECO:0000244|PDB:4PVC}.
TURN 7 9 {ECO:0000244|PDB:4PVC}.
HELIX 11 22 {ECO:0000244|PDB:4PVC}.
STRAND 27 33 {ECO:0000244|PDB:4PVC}.
HELIX 34 43 {ECO:0000244|PDB:4PVC}.
STRAND 50 54 {ECO:0000244|PDB:4PVC}.
TURN 61 64 {ECO:0000244|PDB:4PVC}.
HELIX 65 71 {ECO:0000244|PDB:4PVC}.
TURN 72 74 {ECO:0000244|PDB:4PVC}.
STRAND 77 80 {ECO:0000244|PDB:4PVC}.
STRAND 89 91 {ECO:0000244|PDB:4PVC}.
HELIX 92 95 {ECO:0000244|PDB:4PVC}.
HELIX 97 114 {ECO:0000244|PDB:4PVC}.
TURN 116 118 {ECO:0000244|PDB:4PVC}.
STRAND 121 125 {ECO:0000244|PDB:4PVC}.
HELIX 128 130 {ECO:0000244|PDB:4PVC}.
HELIX 134 136 {ECO:0000244|PDB:4PVC}.
STRAND 143 145 {ECO:0000244|PDB:4PVC}.
HELIX 156 159 {ECO:0000244|PDB:4PVC}.
HELIX 161 182 {ECO:0000244|PDB:4PVC}.
TURN 183 186 {ECO:0000244|PDB:4PVC}.
STRAND 190 196 {ECO:0000244|PDB:4PVC}.
STRAND 198 201 {ECO:0000244|PDB:4PVC}.
HELIX 206 210 {ECO:0000244|PDB:4PVC}.
HELIX 215 224 {ECO:0000244|PDB:4PVC}.
STRAND 236 241 {ECO:0000244|PDB:4PVC}.
HELIX 242 254 {ECO:0000244|PDB:4PVC}.
TURN 257 260 {ECO:0000244|PDB:4PVC}.
STRAND 262 265 {ECO:0000244|PDB:4PVC}.
STRAND 268 271 {ECO:0000244|PDB:4PVC}.
HELIX 272 282 {ECO:0000244|PDB:4PVC}.
TURN 284 289 {ECO:0000244|PDB:4PVC}.
TURN 299 301 {ECO:0000244|PDB:4PVC}.
STRAND 307 309 {ECO:0000244|PDB:4PVC}.
HELIX 311 317 {ECO:0000244|PDB:4PVC}.
HELIX 324 338 {ECO:0000244|PDB:4PVC}.
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


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BMF BLVRB Gene biliverdin reductase B (flavin reductase (NADPH))
EIAAB11124 7-dehydrocholesterol reductase,7-DHC reductase,D7SR,DHCR7,Homo sapiens,Human,Putative sterol reductase SR-2,Sterol Delta(7)-reductase
EIAAB13217 ANG1,Another new gene 1 protein,C-14 sterol reductase,Delta(14)-sterol reductase,Delta-14-SR,Homo sapiens,Human,Putative sterol reductase SR-1,Sterol C14-reductase,TM7SF2,Transmembrane 7 superfamily m
EIAAB05625 3-oxoacyl-[acyl-carrier-protein] reductase,Bos taurus,Bovine,Carbonyl reductase family member 4,CBR4,Quinone reductase CBR4
EIAAB05628 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Quinone reductase CBR4,Rat,Rattus norvegicus
EIAAB05627 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,Cbr4,Mouse,Mus musculus,Quinone reductase CBR4
EIAAB05626 3-oxoacyl-[acyl-carrier-protein] reductase,Carbonyl reductase family member 4,CBR4,Homo sapiens,Human,Quinone reductase CBR4
EIAAB11126 7-dehydrocholesterol reductase,7-DHC reductase,Bos taurus,Bovine,DHCR7,Sterol Delta(7)-reductase


 

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