Reviewed, UniProtKB/Swiss-Prot P41921 (GSHR_YEAST)

Names and origin

Protein names

Recommended name:
    Glutathione reductase
      Short name=GRase
      Short name=GR
    EC=1.8.1.7

Gene names

Name:	GLR1
Ordered Locus Names:	YPL091W
ORF Names:	LPG17W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Maintains high levels of reduced glutathione in the cytosol.
Catalytic activity	2 glutathione + NADP+ = glutathione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond. Present with 7600 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Ref.1 Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-7920,EBI-7920
ATG19	P35193	1	EBI-7920,EBI-29291
CYS4	P32582	1	EBI-7920,EBI-4167
RNR2	P09938	1	EBI-7920,EBI-15240
SSA2	P10592	1	EBI-7920,EBI-8603
TPS3	P38426	1	EBI-7920,EBI-19448
VMA5	P31412	1	EBI-7920,EBI-20260

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 483

483

Glutathione reductase

PRO_0000067972

Regions

Nucleotide binding

53 – 61

9

FAD By similarity

Sites

Active site

472

1

Proton acceptor By similarity

Amino acid modifications

Modified residue

475

1

Phosphoserine Ref.5

Disulfide bond

61 ↔ 66

Redox-active By similarity

Experimental info

Sequence conflict

315

1

Q → E in BAA07109. Ref.3

Sequence conflict

428

1

C → G in BAA07109. Ref.3

Secondary structure

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483

Helix Strand Turn

Details...

Beta strand

23 – 29

7

Helix

33 – 44

12

Beta strand

49 – 55

7

Helix

59 – 64

6

Helix

66 – 82

17

Turn

83 – 89

7

Helix

98 – 100

3

Helix

105 – 129

25

Beta strand

132 – 141

10

Beta strand

147 – 154

8

Beta strand

157 – 166

10

Beta strand

170 – 172

3

Helix

181 – 183

3

Helix

187 – 192

6

Beta strand

198 – 203

6

Helix

207 – 218

12

Beta strand

222 – 226

5

Beta strand

228 – 232

5

Helix

238 – 251

14

Beta strand

254 – 256

3

Beta strand

261 – 266

6

Beta strand

273 – 277

5

Beta strand

282 – 291

10

Beta strand

295 – 297

3

Helix

303 – 306

4

Beta strand

329 – 331

3

Helix

333 – 335

3

Helix

342 – 357

16

Helix

360 – 362

3

Beta strand

374 – 376

3

Beta strand

382 – 386

5

Helix

389 – 396

8

Helix

398 – 400

3

Beta strand

401 – 408

8

Helix

411 – 415

5

Beta strand

422 – 429

8

Turn

430 – 433

4

Beta strand

434 – 442

9

Helix

445 – 457

13

Helix

462 – 466

5

Helix

476 – 480

5

Sequences

	Sequence		Length	Mass (Da)
	P41921-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 203BBB770120504A	FASTA	483	53,441
	10 20 30 40 50 60 MLSATKQTFR SLQIRTMSTN TKHYDYLVIG GGSGGVASAR RAASYGAKTL LVEAKALGGT 70 80 90 100 110 120 CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH LTFNWPEFKQ KRDAYVHRLN 130 140 150 160 170 180 GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ KRDNTTEVYS ANHILVATGG KAIFPENIPG 190 200 210 220 230 240 FELGTDSDGF FRLEEQPKKV VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI 250 260 270 280 290 300 QNTITDHYVK EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG 310 320 330 340 350 360 MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR KLSNRLFGPE 370 380 390 400 410 420 KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN IKVYNSKFTA MYYAMLSEKS 430 440 450 460 470 480 PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ GFGVAIKMGA TKADFDNCVA IHPTSAEELV TMR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase." Collinson L.P., Dawes I.W. Gene 156:123-127(1995) [PubMed: 7737505] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-483.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Aono M., Nakajima N. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 20-483.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L35342 Genomic DNA. Translation: AAA92575.1.
U43281 Genomic DNA. Translation: AAB68208.1.
D37871 mRNA. Translation: BAA07109.1.

PIR

S61975.

RefSeq

NP_015234.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HQM	X-ray	2.40	A/B	17-483	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4020N.

IntAct

P41921. 8 interactions.

2-D gel databases

COMPLUYEAST-2DPAGE

P41921.

Proteomic databases

PeptideAtlas

P41921.

Genome annotation databases

Ensembl

YPL091W. Saccharomyces cerevisiae. [Contig view]

GeneID

856014.

GenomeReviews

Gene locus YPL091W in contig U00094_GR.

KEGG

sce:YPL091W.

NMPDR

fig|4932.3.peg.6367.

Organism-specific databases

CYGD

YPL091w.

SGD

S000006012. GLR1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P41921.

OMA

P41921. EFQNTSR.

Enzyme and pathway databases

BRENDA

1.8.1.7. 250.

Gene expression databases

GermOnline

YPL091W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glut_reduct_1.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00945. HGRDTASE.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01421. gluta_reduc_1. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

980908.

Entry information

Entry name

GSHR_YEAST

Accession

Primary (citable) accession number: P41921

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)