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P30635

- GSHR_CAEEL

UniProt

P30635 - GSHR_CAEEL

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Protein
Probable glutathione reductase 2
Gene
trxr-2, ZK637.10
Organism
Caenorhabditis elegans
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 sitei476 – 4761Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi58 – 6710FAD 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
  4. thioredoxin-disulfide reductase activity Source: WormBase

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. oxidation-reduction process Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glutathione reductase 2 (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:trxr-2
ORF Names:ZK637.10
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome III

Organism-specific databases

WormBaseiZK637.10; CE15373; WBGene00014028; trxr-2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Probable glutathione reductase 2
PRO_0000067958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 72Redox-active By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP30635.

Interactioni

Protein-protein interaction databases

STRINGi6239.ZK637.10.

Structurei

3D structure databases

ProteinModelPortaliP30635.
SMRiP30635. Positions 18-496.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOGENOMiHOG000276712.
InParanoidiP30635.
KOiK00383.
OMAiGLSCSKR.
PhylomeDBiP30635.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[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.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30635-1 [UniParc]FASTAAdd to Basket

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MLLSTFKRHL PIRRLFSSNK FDLIVIGAGS GGLSCSKRAA DLGANVALID    50
AVEPTPHGHS WGIGGTCANV GCIPKKLMHQ AAIVGKELKH ADKYGWNGID 100
QEKIKHDWNV LSKNVNDRVK ANNWIYRVQL NQKKINYFNA YAEFVDKDKI 150
VITGTDKNKT KNFLSAPNVV ISTGLRPKYP NIPGAELGIT SDDLFTLASV 200
PGKTLIVGGG YVALECAGFL SAFNQNVEVL VRSIPLKGFD RDCVHFVMEH 250
LKTTGVKVKE HVEVERVEAV GSKKKVTFTG NGGVEEYDTV IWAAGRVPNL 300
KSLNLDNAGV RTDKRSGKIL ADEFDRASCN GVYAVGDIVQ DRQELTPLAI 350
QSGKLLADRL FSNSKQIVRF DGVATTVFTP LELSTVGLTE EEAIQKHGED 400
SIEVFHSHFT PFEYVVPQNK DSGFCYVKAV CTRDESQKIL GLHFVGPNAA 450
EVIQGYAVAF RVGISMSDLQ NTIAIHPCSS EEFVKLHITK RSGQDPRTQG 500
CCG 503
Length:503
Mass (Da):55,046
Last modified:November 1, 1997 - v2
Checksum:iCE2385C9ACBD9AD2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11115 Genomic DNA. Translation: CAA77459.1.
PIRiD88542.
S15798.
RefSeqiNP_498971.1. NM_066570.4.
UniGeneiCel.9538.

Genome annotation databases

EnsemblMetazoaiZK637.10.1; ZK637.10.1; WBGene00014028.
ZK637.10.2; ZK637.10.2; WBGene00014028.
GeneIDi176259.
KEGGicel:CELE_ZK637.10.
UCSCiZK637.10. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11115 Genomic DNA. Translation: CAA77459.1 .
PIRi D88542.
S15798.
RefSeqi NP_498971.1. NM_066570.4.
UniGenei Cel.9538.

3D structure databases

ProteinModelPortali P30635.
SMRi P30635. Positions 18-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6239.ZK637.10.

Proteomic databases

PaxDbi P30635.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai ZK637.10.1 ; ZK637.10.1 ; WBGene00014028 .
ZK637.10.2 ; ZK637.10.2 ; WBGene00014028 .
GeneIDi 176259.
KEGGi cel:CELE_ZK637.10.
UCSCi ZK637.10. c. elegans.

Organism-specific databases

CTDi 40475.
WormBasei ZK637.10 ; CE15373 ; WBGene00014028 ; trxr-2.

Phylogenomic databases

eggNOGi COG1249.
GeneTreei ENSGT00390000007578.
HOGENOMi HOG000276712.
InParanoidi P30635.
KOi K00383.
OMAi GLSCSKR.
PhylomeDBi P30635.

Miscellaneous databases

NextBioi 891814.
PROi P30635.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[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 TIGR01438. TGR. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiGSHR_CAEEL
AccessioniPrimary (citable) accession number: P30635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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