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Q8T137

- GSHR_DICDI

UniProt

Q8T137 - GSHR_DICDI

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Protein

Glutathione reductase

Gene

gsr

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Maintains high levels of reduced glutathione in the cytosol.1 Publication

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 sitei454 – 4541Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 509FADBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell redox homeostasis Source: dictyBase
  2. culmination involved in sorocarp development Source: dictyBase
  3. glutathione metabolic process Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:gsr
ORF Names:DDB_G0272754
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 2, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0272754. gsr.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. intracellular Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Glutathione reductasePRO_0000327610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 55Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8T137.

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB_0231410.

Structurei

3D structure databases

ProteinModelPortaliQ8T137.
SMRiQ8T137. Positions 6-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
InParanoidiQ8T137.
KOiK00383.
OMAiTERYEAT.
PhylomeDBiQ8T137.

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.

Q8T137-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSTNHFTYL VLGAGSGGIA SARRAAKHLN AKGNGDRIGI VEVTRPGGTC
60 70 80 90 100
VNVGCVPKKV MWNTSFIKEM INAAPSYGFD FGGQQVKFNW PTIKKARDEY
110 120 130 140 150
IKRLNGIYDS NLAKDNIVRI NGYGRFSGPK EIQVNGANGE KYTADHILIA
160 170 180 190 200
AGGRPTVPDV PGKELGITSD GFFELEDLPK STLVVGAGYI AVELAGVLHS
210 220 230 240 250
LGSETTMVIR QKQFLRTFDE MLHTTLLKQM TDDGVKFVTE ASIKSLERDV
260 270 280 290 300
DGKRIIATTN AGVKLPPVEC VIWAIGRVPN TDDLGIDKAG IQLTEQSGFI
310 320 330 340 350
KVDEFQNTNV PGVHAVGDIC GNFLLTPVAI AAGRRLSERL FNGKSDLKFE
360 370 380 390 400
YENVATVVFS HPPIGTVGLT EQEAITKYGT ENIKCYNTSF INMFYSVQVH
410 420 430 440 450
KVRTSMKLVC LGKEEKVIGL HIIGDGCDEI IQGFAVAVKM GCTKWDLDNT
460
CAIHPTSAEE LVTMV
Length:465
Mass (Da):50,483
Last modified:June 1, 2003 - v2
Checksum:iE89CAF09AEA6A771
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000008 Genomic DNA. Translation: EAL71014.1.
RefSeqiXP_644939.1. XM_639847.1.

Genome annotation databases

EnsemblProtistsiDDB0231410; DDB0231410; DDB_G0272754.
GeneIDi8618618.
KEGGiddi:DDB_G0272754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000008 Genomic DNA. Translation: EAL71014.1 .
RefSeqi XP_644939.1. XM_639847.1.

3D structure databases

ProteinModelPortali Q8T137.
SMRi Q8T137. Positions 6-464.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 44689.DDB_0231410.

Proteomic databases

PRIDEi Q8T137.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi DDB0231410 ; DDB0231410 ; DDB_G0272754 .
GeneIDi 8618618.
KEGGi ddi:DDB_G0272754.

Organism-specific databases

dictyBasei DDB_G0272754. gsr.

Phylogenomic databases

eggNOGi COG1249.
InParanoidi Q8T137.
KOi K00383.
OMAi TERYEAT.
PhylomeDBi Q8T137.

Miscellaneous databases

PROi Q8T137.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  2. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  3. "Reduced glutathione levels affect the culmination and cell fate decision in Dictyostelium discoideum."
    Choi C.-H., Kim B.-J., Jeong S.-Y., Lee C.-H., Kim J.-S., Park S.-J., Yim H.-S., Kang S.-O.
    Dev. Biol. 295:523-533(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGSHR_DICDI
AccessioniPrimary (citable) accession number: Q8T137
Secondary accession number(s): Q558X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3