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Q873E8

- GSHR_NEUCR

UniProt

Q873E8 - GSHR_NEUCR

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Protein
Glutathione reductase
Gene
gtr-1, glr1, B10C3.130, NCU03339
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Maintains high levels of reduced glutathione in the cytosol By similarity.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

Binds 1 FAD per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei457 – 4571Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 469FAD By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to oxidative stress Source: EnsemblFungi
  3. glutathione metabolic process Source: InterPro
  4. protein glutathionylation Source: EnsemblFungi
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:gtr-1
Synonyms:glr1
ORF Names:B10C3.130, NCU03339
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 6, Linkage Group II

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. mitochondrion Source: EnsemblFungi
  2. nucleus Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Glutathione reductase
PRO_0000067969Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU03339.1.

Structurei

3D structure databases

ProteinModelPortaliQ873E8.
SMRiQ873E8. Positions 6-468.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
KOiK00383.
OMAiGTNSDGF.
OrthoDBiEOG79W9F2.

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.

Q873E8-1 [UniParc]FASTAAdd to Basket

« Hide

MAPISRETDF LVIGGGSGGI ATARAAAGKY GIKSMVVEGK RLGGTCVNVG    50
CVPKKVTFYA ALVAETIHQA KDYGFSVEQT APFDWPTFKQ KRDAYVARLN 100
GIYERNLAND KVEYVHGWAK LLSPNSVEVT LDDGTKSVVN AKKILIAVGG 150
NPTIPPHIPG SEYGTNSDGF FDIDTLPKKV ALVGAGYIAV EFAGMLNALG 200
VETHLFIRHD TFLRSFDPMI QQVSVKEYER IGVKVHKKSQ LTSVQKDAAG 250
KLAINFKEGE GEQSISDVDH LIWAVGRTPA VEGLGLDKAG VKTNEKGYIE 300
VDEYQNTSTE NIYAVGDVCG QVELTPVAIA AGRKLAARLF GPEEFRTLKL 350
NYDNVPSVVF AHPEIGSIGL TEPEAVAKYG AENLKIYKSS FTAMYYAMMK 400
PEDKAPTAYK LICAGPEEKV VGLHIIGLGS GEILQGFGVA VNMGATKADF 450
DNCVAIHPTS AEELVTLK 468
Length:468
Mass (Da):50,313
Last modified:June 1, 2003 - v1
Checksum:iA3802C1A7DC0B479
GO

Sequence cautioni

The sequence ESA43520.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence ESA43521.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX284749 Genomic DNA. Translation: CAD70360.1.
CM002237 Genomic DNA. Translation: ESA43520.1. Different initiation.
CM002237 Genomic DNA. Translation: ESA43521.1. Different initiation.
RefSeqiXP_956448.1. XM_951355.1.
UniGeneiNcr.16209.

Genome annotation databases

EnsemblFungiiEFNCRT00000002546; EFNCRP00000002546; EFNCRG00000002543.
GeneIDi3872613.
KEGGincr:NCU03339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX284749 Genomic DNA. Translation: CAD70360.1 .
CM002237 Genomic DNA. Translation: ESA43520.1 . Different initiation.
CM002237 Genomic DNA. Translation: ESA43521.1 . Different initiation.
RefSeqi XP_956448.1. XM_951355.1.
UniGenei Ncr.16209.

3D structure databases

ProteinModelPortali Q873E8.
SMRi Q873E8. Positions 6-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5141.NCU03339.1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000002546 ; EFNCRP00000002546 ; EFNCRG00000002543 .
GeneIDi 3872613.
KEGGi ncr:NCU03339.

Phylogenomic databases

eggNOGi COG1249.
HOGENOMi HOG000276712.
KOi K00383.
OMAi GTNSDGF.
OrthoDBi EOG79W9F2.

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

  1. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  2. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiGSHR_NEUCR
AccessioniPrimary (citable) accession number: Q873E8
Secondary accession number(s): Q1K529, V5IP83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 80 of the entry and version 1 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 By similarity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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