Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione reductase

Gene

gtr-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 4 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

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

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

Regions

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

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. glutathione-disulfide reductase activity Source: UniProtKB-EC
  3. mercury (II) reductase activity Source: InterPro
  4. mercury ion binding Source: InterPro
  5. NADP binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to hydrogen peroxide Source: EnsemblFungi
  3. cellular response to menadione Source: EnsemblFungi
  4. detoxification of mercury ion Source: InterPro
  5. glutathione metabolic process Source: EnsemblFungi
  6. 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 Componenti: Chromosome 6, Linkage Group II

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Glutathione reductasePRO_0000067969Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU03339.1.

Structurei

3D structure databases

ProteinModelPortaliQ873E8.
SMRiQ873E8. Positions 6-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiQ873E8.
KOiK00383.
OMAiHKEPTVY.
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

        10         20         30         40         50
MAPISRETDF LVIGGGSGGI ATARAAAGKY GIKSMVVEGK RLGGTCVNVG
60 70 80 90 100
CVPKKVTFYA ALVAETIHQA KDYGFSVEQT APFDWPTFKQ KRDAYVARLN
110 120 130 140 150
GIYERNLAND KVEYVHGWAK LLSPNSVEVT LDDGTKSVVN AKKILIAVGG
160 170 180 190 200
NPTIPPHIPG SEYGTNSDGF FDIDTLPKKV ALVGAGYIAV EFAGMLNALG
210 220 230 240 250
VETHLFIRHD TFLRSFDPMI QQVSVKEYER IGVKVHKKSQ LTSVQKDAAG
260 270 280 290 300
KLAINFKEGE GEQSISDVDH LIWAVGRTPA VEGLGLDKAG VKTNEKGYIE
310 320 330 340 350
VDEYQNTSTE NIYAVGDVCG QVELTPVAIA AGRKLAARLF GPEEFRTLKL
360 370 380 390 400
NYDNVPSVVF AHPEIGSIGL TEPEAVAKYG AENLKIYKSS FTAMYYAMMK
410 420 430 440 450
PEDKAPTAYK LICAGPEEKV VGLHIIGLGS GEILQGFGVA VNMGATKADF
460
DNCVAIHPTS AEELVTLK
Length:468
Mass (Da):50,313
Last modified:May 31, 2003 - v1
Checksum:iA3802C1A7DC0B479
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ873E8.
SMRiQ873E8. Positions 6-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU03339.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiQ873E8.
KOiK00383.
OMAiHKEPTVY.
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]
ProtoNetiSearch...

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(2002) [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(2002) [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 10, 2004
Last sequence update: May 31, 2003
Last modified: March 31, 2015
This is version 86 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

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.