P25373 (GLRX1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaredoxin-1

Alternative name(s):
Glutathione-dependent oxidoreductase 1

Gene names

Name:	GRX1
Ordered Locus Names:	YCL035C
ORF Names:	YCL35C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	110 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Ref.3 Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity.
Induction	In response to heat shock and osmotic stress. Ref.3 Ref.4
Miscellaneous	Present with 3030 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.
Biophysicochemical properties	Kinetic parameters: KM=0.88 mM for H2O2 Ref.5 Ref.6 KM=0.52 mM for cumene hydroperoxide KM=0.37 mM for tert-butyl hydroperoxide KM=4.2 mM for 1-chloro-2,4-dinitrobenzene KM=1.3 mM for 1,2-dichloro-4-nitrobenzene Vmax=110 µmol/min/mg enzyme for H2O2 Vmax=32.5 µmol/min/mg enzyme for cumene hydroperoxide Vmax=7.5 µmol/min/mg enzyme for tert-butyl hydroperoxide

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from mutant phenotype. Source: SGD cellular response to oxidative stress Inferred from mutant phenotype Ref.3. Source: SGD electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW protein glutathionylation Inferred from genetic interaction. Source: SGD transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro glutathione peroxidase activity Inferred from direct assay Ref.6. Source: SGD glutathione transferase activity Inferred from direct assay Ref.6. Source: SGD protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 110

110

Glutaredoxin-1

PRO_0000141613

Regions

Domain

7 – 110

104

Glutaredoxin

Amino acid modifications

Disulfide bond

27 ↔ 30

Redox-active By similarity

Secondary structure

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110

Helix Strand Turn

Details...

Helix

4 – 15

12

Beta strand

17 – 23

7

Helix

28 – 38

11

Helix

45 – 47

3

Beta strand

48 – 52

5

Helix

53 – 55

3

Helix

59 – 70

12

Beta strand

77 – 80

4

Beta strand

83 – 87

5

Helix

88 – 96

9

Helix

100 – 104

5

Turn

105 – 107

3

Sequences

	Sequence		Length	Mass (Da)
	P25373 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 8E69BC80BF40F2DD	FASTA	110	12,380
	10 20 30 40 50 60 MVSQETIKHV KDLIAENEIF VASKTYCPYC HAALNTLFEK LKVPRSKVLV LQLNDMKEGA 70 80 90 100 110 DIQAALYEIN GQRTVPNIYI NGKHIGGNDD LQELRETGEL EELLEPILAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species." Luikenhuis S., Perrone G., Dawes I.W., Grant C.M. Mol. Biol. Cell 9:1081-1091(1998) [PubMed: 9571241] [Abstract] Cited for: FUNCTION, INDUCTION.
[4]	"Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae." Grant C.M., Luikenhuis S., Beckhouse A., Soderbergh M., Dawes I.W. Biochim. Biophys. Acta 1490:33-42(2000) [PubMed: 10786615] [Abstract] Cited for: INDUCTION.
[5]	"The yeast glutaredoxins are active as glutathione peroxidases." Collinson E.J., Wheeler G.L., Garrido E.O., Avery A.M., Avery S.V., Grant C.M. J. Biol. Chem. 277:16712-16717(2002) [PubMed: 11875065] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"Role of yeast glutaredoxins as glutathione S-transferases." Collinson E.J., Grant C.M. J. Biol. Chem. 278:22492-22497(2003) [PubMed: 12684511] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59720 Genomic DNA. Translation: CAA42381.1.
BK006937 Genomic DNA. Translation: DAA07449.1.

PIR

S19363.

RefSeq

NP_009895.1. NM_001178680.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JAC	X-ray	2.02	A	1-110	[»]
2JAD	X-ray	2.70	A	1-110	[»]
3C1R	X-ray	2.00	A	1-110	[»]
3C1S	X-ray	2.50	A	1-110	[»]

ProteinModelPortal

P25373.

SMR

P25373. Positions 1-92.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5646N.

IntAct

P25373. 3 interactions.

MINT

MINT-556392.

STRING

P25373.

Proteomic databases

PeptideAtlas

P25373.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YCL035C; YCL035C; YCL035C.

GeneID

850322.

KEGG

sce:YCL035C.

NMPDR

fig|4932.3.peg.615.

Organism-specific databases

CYGD

YCL035c.

SGD

S000000540. GRX1.

Phylogenomic databases

eggNOG

fuNOG12136.

GeneTree

EFGT00050000002871.

HOGENOM

HBG728471.

OMA

IAENEIF.

OrthoDB

EOG4V1B9J.

Gene expression databases

ArrayExpress

P25373.

Genevestigator

P25373.

GermOnline

YCL035C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

KO

K03676.

Pfam

PF00462. Glutaredoxin. 1 hit.
[Graphical view]

PRINTS

PR00160. GLUTAREDOXIN.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR02180. GRX_euk. 1 hit.

PROSITE

PS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

965736.

Entry information

Entry name

GLRX1_YEAST

Accession

Primary (citable) accession number: P25373
Secondary accession number(s): D6VQY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	December 14, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program