Monothiol glutaredoxin-3 (Q03835)

Identification
NameMonothiol glutaredoxin-3
SynonymsNot Available
Gene NameGRX3
Enzyme ClassNot Available
Biological Properties
General FunctionPosttranslational modification, protein turnover, chaperones
Specific FunctionMonothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. 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)
Cellular LocationNot Available
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
GO Classification
Function
catalytic activity
oxidoreductase activity
electron carrier activity
oxidoreductase activity, acting on a sulfur group of donors
disulfide oxidoreductase activity
protein disulfide oxidoreductase activity
Process
cellular process
cellular homeostasis
cell redox homeostasis
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>858 bp ATGTGTTCTTTTCAGGTTCCATCTGCATTTTCTTTTAACTACACCTCGTACTGTTATAAA CGCCACCAAGCAAGATATTACACAGCAGCAAAACTTTTTCAGGAAATGCCTGTTATTGAA ATTAACGATCAAGAGCAATTTACTTACCTAACTACCACTGCGGCCGGCGACAAGTTAATC GTGCTTTATTTCCATACCAGTTGGGCAGAACCATGCAAAGCATTAAAGCAGGTTTTTGAG GCCATTAGTAATGAGCCTTCCAATTCCAACGTCTCTTTCTTATCCATTGATGCGGACGAA AACTCGGAAATTTCAGAACTTTTTGAAATCTCAGCTGTTCCATATTTTATCATAATTCAC AAAGGGACAATCTTAAAAGAATTATCCGGCGCGGATCCAAAGGAGTATGTGTCTTTATTA GAAGACTGCAAGAACTCAGTCAATTCCGGATCATCACAAACTCATACTATGGAAAATGCA AACGTAAATGAGGGGAGTCATAATGATGAAGACGATGACGACGAAGAAGAGGAAGAAGAA ACTGAGGAGCAAATAAACGCTAGATTGACTAAATTGGTCAATGCCGCGCCGGTAATGTTA TTTATGAAGGGGAGCCCCTCTGAACCTAAATGCGGGTTTTCGAGACAACTTGTGGGTATC TTGAGAGAACATCAAGTAAGATTTGGCTTCTTTGATATATTAAGAGACGAATCTGTTAGA CAAAACTTGAAAAAGTTTTCTGAATGGCCAACTTTCCCTCAACTTTATATAAATGGGGAG TTTCAAGGCGGTTTAGACATTATCAAGGAATCCTTGGAGGAAGACCCTGATTTTTTGCAG CATGCTCTCCAATCTTAA
Protein Properties
Pfam Domain Function
Protein Residues285
Protein Molecular Weight32480.80078
Protein Theoretical pI4.26
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Monothiol glutaredoxin-3 MCSFQVPSAFSFNYTSYCYKRHQARYYTAAKLFQEMPVIEINDQEQFTYLTTTAAGDKLI VLYFHTSWAEPCKALKQVFEAISNEPSNSNVSFLSIDADENSEISELFEISAVPYFIIIH KGTILKELSGADPKEYVSLLEDCKNSVNSGSSQTHTMENANVNEGSHNDEDDDDEEEEEE TEEQINARLTKLVNAAPVMLFMKGSPSEPKCGFSRQLVGILREHQVRFGFFDILRDESVR QNLKKFSEWPTFPQLYINGEFQGGLDIIKESLEEDPDFLQHALQS
References
External Links
ResourceLink
Saccharomyces Genome Database GRX3
Uniprot IDQ03835
Uniprot NameGLRX3_YEAST
GenBank Gene IDZ47746
Genebank Protein ID633632
General Reference
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, 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., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • 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. (2009). "The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation." Biochemistry 48:9569-9581.19715344
  • Gibson, L. M., Dingra, N. N., Outten, C. E., Lebioda, L. (2008). "Structure of the thioredoxin-like domain of yeast glutaredoxin 3." Acta Crystallogr D Biol Crystallogr 64:927-932.18703840