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P78965

- GSHR_SCHPO

UniProt

P78965 - GSHR_SCHPO

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Protein
Glutathione reductase
Gene
pgr1, pi039, SPBC17A3.07
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - 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

Binds 1 FAD per subunit By similarity.

Sites

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

Regions

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

GO - Molecular functioni

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

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 reductase
PRO_0000067970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 51Redox-active By 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.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
KOiK00383.
OMAiLMRFKRT.
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

MAPISKVFDY LVIGGGSGGL ASARRAAKHG AKVALIEASG RLGGTCVNYG    50
CVPKKIMWNI ADLVAKMKTA KQNGFPNSQL GSFDWGMIKR KRDAYIGRLN 100
GIYERNVNKD GVAYISGHAS FVSPTEVAVD MNDGSGTQVF SAKYILIAVG 150
GHPIWPSHIP GAEYGIDSDG FFELESQPKR VAIVGAGYIA VELAGVFAAL 200
GTETHMFIRQ SKFLRKFDPI ISDGIMDHFQ HIGINVHTNS LEFKKVEKLP 250
SGELCIHQQD GSTFNVDTLL WAIGRAPKIQ GLRLEKAGVK TLPNGIIIAD 300
TYQRTNVPTV LSLGDVCGKL ELTPVAIAAG RRLSDRLFGG IKDAHLDYEE 350
VPSVVFAHPE AGTIGLTEQE AIDKYGESQI KVYNTKFNGL NYSMVEQEDK 400
VPTTYKLVCA GPLQKVVGLH LVGDFSAEIL QGFGVAIKMG ATKSDFDSCV 450
AIHPTSAEEL VTLV 464
Length:464
Mass (Da):49,999
Last modified:January 11, 2001 - v2
Checksum:i2BFFEFD363A3F173
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841V → VV in AAC49809. 1 Publication
Sequence conflicti419 – 4246LHLVGD → PTFSWR in AAC49809. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U63845 Genomic DNA. Translation: AAC49809.1 .
AB004537 Genomic DNA. Translation: BAA21419.1 .
CU329671 Genomic DNA. Translation: CAB51766.1 .
PIRi T39699.
RefSeqi NP_595589.1. NM_001021485.2.

3D structure databases

ProteinModelPortali P78965.
SMRi P78965. Positions 6-463.
ModBasei Search...

Protein-protein interaction databases

BioGridi 276692. 1 interaction.
MINTi MINT-4691707.
STRINGi 4896.SPBC17A3.07-1.

Proteomic databases

MaxQBi P78965.
PaxDbi P78965.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC17A3.07.1 ; SPBC17A3.07.1:pep ; SPBC17A3.07 .
GeneIDi 2540156.
KEGGi spo:SPBC17A3.07.

Organism-specific databases

PomBasei SPBC17A3.07.

Phylogenomic databases

eggNOGi COG1249.
HOGENOMi HOG000276712.
KOi K00383.
OMAi LMRFKRT.
OrthoDBi EOG79W9F2.
PhylomeDBi P78965.

Enzyme and pathway databases

Reactomei REACT_210617. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_219607. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi 20801291.
PROi P78965.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01421. gluta_reduc_1. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 129 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

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