Reviewed, UniProtKB/Swiss-Prot O36032 (GLRX1_SCHPO)

Names and origin

Protein names

Recommended name:
    Glutaredoxin-1

Gene names

Name:	grx1
ORF Names:	SPAC4F10.20

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	101 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function

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 some disulfides in a coupled system with glutathione reductase. Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions. It transfers reducing equivalents to cytosolic protein and nonprotein disulfides By similarity.

Sequence similarities

Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Redox-active center
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to stress Inferred from expression pattern. Source: GeneDB_SPombe electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW response to zinc ion Inferred from mutant phenotype. Source: GeneDB_SPombe transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro 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 – 101	101	Glutaredoxin-1		PRO_0000141610
Regions
	Domain	5 – 101	97	Glutaredoxin
Amino acid modifications
	Disulfide bond	25 ↔ 28		Redox-active By similarity
Experimental info
	Sequence conflict	52	1	N → D in AAF19628. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O36032-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 30557E19BF33E9BB	FASTA	101	11,261
	10 20 30 40 50 60 MSSVESFVDS AVADNDVVVF AKSYCPYCHA TEKVIADKKI KAQVYQIDLM NNGDEIQSYL 70 80 90 100 LKKTGQRTVP NIFIHQKHVG GNSDFQALFK KGELDSLFNT A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"S.pombe glutaredoxin." Kawamukai M. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of cDNA encoding thioltransferase (glutaredoxin) from Schizosaccharomyces pombe." Kim H.-G., Cho Y.-W., Park E.-H., Lim C.-J. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Isolation and expression of the genomic DNA encoding thioltransferase (Glutaredoxin) from Schizosaccharomyces pombe." Cho Y.-W., Kim H.-G., Lim C.-J. Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB015167 mRNA. Translation: BAA28750.1. AF121275 mRNA. Translation: AAD25391.1. AF192764 Genomic DNA. Translation: AAF19628.1. CU329670 Genomic DNA. Translation: CAB11722.1.
PIR	T38824.
RefSeq	NP_594763.1.
3D structure databases
HSSP	HSSP built from PDB template 1JHB based on UniProtKB P35754.
ModBase	Search...
Genome annotation databases
GeneID	2543556.
KEGG	spo:SPAC4F10.20.
NMPDR	fig|4896.1.peg.4733.
Organism-specific databases
GeneDB_Spombe	SPAC4F10.20.
Phylogenomic databases
OMA	O36032. QAKWAFD.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002839-MON.
Gene expression databases
ArrayExpress	O36032.
Family and domain databases
InterPro	IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR014025. Glutaredoxin_sub. IPR011899. GRX_euk. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00462. Glutaredoxin. 1 hit. [Graphical view]
PRINTS	PR00160. GLUTAREDOXIN.
TIGRFAMs	TIGR02180. GRX_euk. 1 hit.
PROSITE	PS00195. GLUTAREDOXIN_1. 1 hit. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLRX1_SCHPO

Accession

Primary (citable) accession number: O36032
Secondary accession number(s): Q9US58

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)