Reviewed, UniProtKB/Swiss-Prot P78965 (GSHR_SCHPO)

Names and origin

Protein names

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

Gene names

Name:	pgr1
ORF Names:	SPBC17A3.07, pi039

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	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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	CytoplasmBy similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Ref.1 Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	mitochondrion Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Ref.1 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 – 464	464	Glutathione reductase		PRO_0000067970
Regions
	Nucleotide binding	37 – 46	10	FAD By similarity
Sites
	Active site	453	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	46 ↔ 51		Redox-active By similarity
Experimental info
	Sequence conflict	184	1	V → VV in AAC49809. Ref.1
	Sequence conflict	419 – 424	6	LHLVGD → PTFSWR in AAC49809. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P78965-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 2BFFEFD363A3F173	FASTA	464	49,999
	10 20 30 40 50 60 MAPISKVFDY LVIGGGSGGL ASARRAAKHG AKVALIEASG RLGGTCVNYG CVPKKIMWNI 70 80 90 100 110 120 ADLVAKMKTA KQNGFPNSQL GSFDWGMIKR KRDAYIGRLN GIYERNVNKD GVAYISGHAS 130 140 150 160 170 180 FVSPTEVAVD MNDGSGTQVF SAKYILIAVG GHPIWPSHIP GAEYGIDSDG FFELESQPKR 190 200 210 220 230 240 VAIVGAGYIA VELAGVFAAL GTETHMFIRQ SKFLRKFDPI ISDGIMDHFQ HIGINVHTNS 250 260 270 280 290 300 LEFKKVEKLP SGELCIHQQD GSTFNVDTLL WAIGRAPKIQ GLRLEKAGVK TLPNGIIIAD 310 320 330 340 350 360 TYQRTNVPTV LSLGDVCGKL ELTPVAIAAG RRLSDRLFGG IKDAHLDYEE VPSVVFAHPE 370 380 390 400 410 420 AGTIGLTEQE AIDKYGESQI KVYNTKFNGL NYSMVEQEDK VPTTYKLVCA GPLQKVVGLH 430 440 450 460 LVGDFSAEIL QGFGVAIKMG ATKSDFDSCV AIHPTSAEEL VTLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, expression, and regulation of the pgr1(+) gene encoding glutathione reductase absolutely required for the growth of Schizosaccharomyces pombe." Lee J., Dawes I.W., Roe J.-H. J. Biol. Chem. 272:23042-23049(1997) [PubMed: 9287302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment." Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M. Yeast 16:71-80(2000) [PubMed: 10620777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"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	U63845 Genomic DNA. Translation: AAC49809.1. AB004537 Genomic DNA. Translation: BAA21419.1. CU329671 Genomic DNA. Translation: CAB51766.1.
PIR	T39699.
RefSeq	NP_595589.1.
3D structure databases
HSSP	HSSP built from PDB template 1ALG based on UniProtKB P00390.
ModBase	Search...
Genome annotation databases
GeneID	2540156.
KEGG	spo:SPBC17A3.07.
NMPDR	fig|4896.1.peg.1455.
Organism-specific databases
GeneDB_Spombe	SPBC17A3.07.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003627-MON.
Gene expression databases
ArrayExpress	P78965.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glut_reduct_1. IPR000815. Hg_reductase. IPR001100. Pyr_nuc-diS_OxRdtase. 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. PR00411. PNDRDTASEI.
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...

Entry information

Entry name

GSHR_SCHPO

Accession

Primary (citable) accession number: P78965
Secondary accession number(s): O13631

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2001
Last modified:	November 25, 2008
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)