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Protein

Glutathione reductase

Gene

pgr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei453 – 4531Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 4610FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. glutathione-disulfide reductase activity Source: PomBase
  3. NADP binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to menadione Source: PomBase
  3. cellular response to oxidative stress Source: PomBase
  4. glutathione metabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiREACT_210617. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_219607. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:pgr1
ORF Names:pi039, SPBC17A3.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC17A3.07.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Glutathione reductasePRO_0000067970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 51Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP78965.
PaxDbiP78965.

Interactioni

Protein-protein interaction databases

BioGridi276692. 1 interaction.
MINTiMINT-4691707.
STRINGi4896.SPBC17A3.07-1.

Structurei

3D structure databases

ProteinModelPortaliP78965.
SMRiP78965. Positions 6-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiP78965.
KOiK00383.
OMAiHKEPTVY.
OrthoDBiEOG79W9F2.
PhylomeDBiP78965.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78965-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPISKVFDY LVIGGGSGGL ASARRAAKHG AKVALIEASG RLGGTCVNYG
60 70 80 90 100
CVPKKIMWNI ADLVAKMKTA KQNGFPNSQL GSFDWGMIKR KRDAYIGRLN
110 120 130 140 150
GIYERNVNKD GVAYISGHAS FVSPTEVAVD MNDGSGTQVF SAKYILIAVG
160 170 180 190 200
GHPIWPSHIP GAEYGIDSDG FFELESQPKR VAIVGAGYIA VELAGVFAAL
210 220 230 240 250
GTETHMFIRQ SKFLRKFDPI ISDGIMDHFQ HIGINVHTNS LEFKKVEKLP
260 270 280 290 300
SGELCIHQQD GSTFNVDTLL WAIGRAPKIQ GLRLEKAGVK TLPNGIIIAD
310 320 330 340 350
TYQRTNVPTV LSLGDVCGKL ELTPVAIAAG RRLSDRLFGG IKDAHLDYEE
360 370 380 390 400
VPSVVFAHPE AGTIGLTEQE AIDKYGESQI KVYNTKFNGL NYSMVEQEDK
410 420 430 440 450
VPTTYKLVCA GPLQKVVGLH LVGDFSAEIL QGFGVAIKMG ATKSDFDSCV
460
AIHPTSAEEL VTLV
Length:464
Mass (Da):49,999
Last modified:January 11, 2001 - v2
Checksum:i2BFFEFD363A3F173
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841V → VV in AAC49809. (PubMed:9287302)Curated
Sequence conflicti419 – 4246LHLVGD → PTFSWR in AAC49809. (PubMed:9287302)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63845 Genomic DNA. Translation: AAC49809.1.
AB004537 Genomic DNA. Translation: BAA21419.1.
CU329671 Genomic DNA. Translation: CAB51766.1.
PIRiT39699.
RefSeqiNP_595589.1. NM_001021485.2.

Genome annotation databases

EnsemblFungiiSPBC17A3.07.1; SPBC17A3.07.1:pep; SPBC17A3.07.
GeneIDi2540156.
KEGGispo:SPBC17A3.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63845 Genomic DNA. Translation: AAC49809.1.
AB004537 Genomic DNA. Translation: BAA21419.1.
CU329671 Genomic DNA. Translation: CAB51766.1.
PIRiT39699.
RefSeqiNP_595589.1. NM_001021485.2.

3D structure databases

ProteinModelPortaliP78965.
SMRiP78965. Positions 6-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276692. 1 interaction.
MINTiMINT-4691707.
STRINGi4896.SPBC17A3.07-1.

Proteomic databases

MaxQBiP78965.
PaxDbiP78965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC17A3.07.1; SPBC17A3.07.1:pep; SPBC17A3.07.
GeneIDi2540156.
KEGGispo:SPBC17A3.07.

Organism-specific databases

PomBaseiSPBC17A3.07.

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiP78965.
KOiK00383.
OMAiHKEPTVY.
OrthoDBiEOG79W9F2.
PhylomeDBiP78965.

Enzyme and pathway databases

ReactomeiREACT_210617. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_219607. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi20801291.
PROiP78965.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiGSHR_SCHPO
AccessioniPrimary (citable) accession number: P78965
Secondary accession number(s): O13631
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: January 7, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.