Q03835 (GLRX3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Monothiol glutaredoxin-3

Gene names

Name:	GRX3
Ordered Locus Names:	YDR098C
ORF Names:	YD8557.05C

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	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters By similarity. Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit Probable. Ref.5
Subunit structure	Homodimer. Heterodimer with FRA2. Ref.5
Miscellaneous	Present with 11000 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the glutaredoxin family. Monothiol subfamily. Contains 1 glutaredoxin domain. Contains 1 thioredoxin domain.

Ontologies

Keywords
Domain	Redox-active center
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from mutant phenotype. Source: SGD cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular iron ion homeostasis Inferred from genetic interaction. Source: SGD cellular response to oxidative stress Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay Ref.4. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AFT1	P22149	4	EBI-22178,EBI-2332
BUD32	P53323	3	EBI-22178,EBI-3809

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 285

285

Monothiol glutaredoxin-3

PRO_0000102249

Regions

Domain

30 – 145

116

Thioredoxin

Domain

186 – 285

100

Glutaredoxin

Sites

Metal binding

211

1

Iron-sulfur (2Fe-2S); shared with dimeric partner By similarity

Secondary structure

1

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285

Helix Strand Turn

Details...

Beta strand

38 – 41

4

Helix

44 – 51

8

Turn

52 – 54

3

Beta strand

60 – 65

6

Helix

72 – 84

13

Helix

86 – 88

3

Beta strand

91 – 97

7

Turn

98 – 100

3

Helix

102 – 107

6

Beta strand

112 – 119

8

Beta strand

124 – 128

5

Helix

133 – 147

15

Sequences

	Sequence		Length	Mass (Da)
	Q03835 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5C97FFC38192E904	FASTA	285	32,481
	10 20 30 40 50 60 MCSFQVPSAF SFNYTSYCYK RHQARYYTAA KLFQEMPVIE INDQEQFTYL TTTAAGDKLI 70 80 90 100 110 120 VLYFHTSWAE PCKALKQVFE AISNEPSNSN VSFLSIDADE NSEISELFEI SAVPYFIIIH 130 140 150 160 170 180 KGTILKELSG ADPKEYVSLL EDCKNSVNSG SSQTHTMENA NVNEGSHNDE DDDDEEEEEE 190 200 210 220 230 240 TEEQINARLT KLVNAAPVML FMKGSPSEPK CGFSRQLVGI LREHQVRFGF FDILRDESVR 250 260 270 280 QNLKKFSEWP TFPQLYINGE FQGGLDIIKE SLEEDPDFLQ HALQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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].
[4]	"Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis." Kumanovics A., Chen O.S., Li L., Bagley D., Adkins E.M., Lin H., Dingra N.N., Outten C.E., Keller G., Winge D., Ward D.M., Kaplan J. J. Biol. Chem. 283:10276-10286(2008) [PubMed: 18281282] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FRA2.
[5]	"The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation." Li H., Mapolelo D.T., Dingra N.N., Naik S.G., Lees N.S., Hoffman B.M., Riggs-Gelasco P.J., Huynh B.H., Johnson M.K., Outten C.E. Biochemistry 48:9569-9581(2009) [PubMed: 19715344] [Abstract] Cited for: FUNCTION, SUBUNIT, MASS SPECTROMETRY, INTERACTION WITH FRA2.
[6]	"Structure of the thioredoxin-like domain of yeast glutaredoxin 3." Gibson L.M., Dingra N.N., Outten C.E., Lebioda L. Acta Crystallogr. D 64:927-932(2008) [PubMed: 18703840] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 37-148.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z47746 Genomic DNA. Translation: CAA87672.1.
BK006938 Genomic DNA. Translation: DAA11943.1.

PIR

S51247.

RefSeq

NP_010383.1. NM_001180406.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3D6I	X-ray	1.50	A/B	37-148	[»]

ProteinModelPortal

Q03835.

SMR

Q03835. Positions 37-148, 185-284.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1350N.

IntAct

Q03835. 8 interactions.

MINT

MINT-402040.

STRING

Q03835.

Proteomic databases

PeptideAtlas

Q03835.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR098C; YDR098C; YDR098C.

GeneID

851672.

KEGG

sce:YDR098C.

NMPDR

fig|4932.3.peg.1129.

Organism-specific databases

CYGD

YDR098c.

SGD

S000002505. GRX3.

Phylogenomic databases

eggNOG

fuNOG04169.

GeneTree

EFGT00050000001289.

HOGENOM

HBG327968.

OMA

MIFMKGD.

OrthoDB

EOG4SBJ76.

Gene expression databases

ArrayExpress

Q03835.

Genevestigator

Q03835.

GermOnline

YDR098C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.

PANTHER

PTHR10293. Glutredox-rel. 1 hit.

Pfam

PF00462. Glutaredoxin. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 2 hits.

PROSITE

PS51354. GLUTAREDOXIN_2. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

969295.

Entry information

Entry name

GLRX3_YEAST

Accession

Primary (citable) accession number: Q03835
Secondary accession number(s): D6VS83

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program