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UniProtKB/Swiss-Prot entry P78965


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GSHR_SCHPO
Primary accession number P78965
Secondary accession number O13631
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 78)
Name and origin of the protein
Protein name Glutathione reductase
Synonyms GRase
GR
EC 1.8.1.7
Gene name
Name: pgr1
ORFNames: SPBC17A3.07, pi039
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1074/jbc.272.37.23042; PubMed=9287302 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J., Dawes I.W., Roe J.-H.;
"Isolation, expression, and regulation of the pgr1(+) gene encoding glutathione reductase absolutely required for the growth of Schizosaccharomyces pombe.";
J. Biol. Chem. 272:23042-23049(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1002/(SICI)1097-0061(20000115)16:1<71::AID-YEA505>3.0.CO;2-5; PubMed=10620777 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
Yeast 16:71-80(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U63845; AAC49809.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB004537; BAA21419.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAB51766.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39699; T39699.
RefSeq NP_595589.1; -.
3D structure databases
HSSP P00390; 1ALG. [HSSP ENTRY / PDB]
ModBase P78965.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-003627-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC17A3.07; -.
Gene expression databases
ArrayExpress P78965; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from GeneDB_SPombe).
GO:0004362; Molecular function: glutathione-disulfide reductase activity (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006749; Biological process: glutathione metabolic process (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006979; Biological process: response to oxidative stress (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01421; gluta_reduc_1; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
BLOCKS P78965.
ProtoNet P78965.
Genome annotation databases
GeneID 2540156; -.
KEGG spo:SPBC17A3.07; -.
NMPDR fig|4896.1.peg.1455; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   464  464     Glutathione reductase. PRO_0000067970
NP_BIND   37    46  10     FAD (By similarity). 
ACT_SITE   453   453        Proton acceptor (By similarity). 
DISULFID   46    51        Redox-active (By similarity). 
CONFLICT   184   184        V -> VV (in Ref. 1; AAC49809). 
CONFLICT   419   424        LHLVGD -> PTFSWR (in Ref. 1; AAC49809). 
Sequence information
Length: 464 AA [This is the length of the unprocessed precursor] Molecular weight: 49999 Da [This is the MW of the unprocessed precursor] CRC64: 2BFFEFD363A3F173 [This is a checksum on the sequence]
        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 

P78965 in FASTA format

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