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P42770 (GSHRP_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutathione reductase, chloroplastic

Short name=GR
Short name=GRase
EC=1.8.1.7
Alternative name(s):
Protein EMBRYO DEFECTIVE 2360
Gene names
Name:EMB2360
Ordered Locus Names:At3g54660
ORF Names:T5N23_20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Maintains high levels of reduced glutathione in the chloroplast.

Catalytic activity

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subcellular location

Plastidchloroplast Potential.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7474Chloroplast Potential
Chain75 – 565491Glutathione reductase, chloroplastic
PRO_0000030280

Regions

Nucleotide binding126 – 13510FAD By similarity

Sites

Active site5291Proton acceptor By similarity
Binding site2911NADP By similarity
Binding site2971NADP By similarity

Amino acid modifications

Disulfide bond135 ↔ 140Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P42770 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 29C2CD0E68ED4E4A

FASTA56560,852
        10         20         30         40         50         60 
MASTPKLTST ISSSSPSLQF LCKKLPIAIH LPSSSSSSFL SLPKTLTSLY SLRPRIALLS 

        70         80         90        100        110        120 
NHRYYHSRRF SVCASTDNGA ESDRHYDFDL FTIGAGSGGV RASRFATSFG ASAAVCELPF 

       130        140        150        160        170        180 
STISSDTAGG VGGTCVLRGC VPKKLLVYAS KYSHEFEDSH GFGWKYETEP SHDWTTLIAN 

       190        200        210        220        230        240 
KNAELQRLTG IYKNILSKAN VKLIEGRGKV IDPHTVDVDG KIYTTRNILI AVGGRPFIPD 

       250        260        270        280        290        300 
IPGKEFAIDS DAALDLPSKP KKIAIVGGGY IALEFAGIFN GLNCEVHVFI RQKKVLRGFD 

       310        320        330        340        350        360 
EDVRDFVGEQ MSLRGIEFHT EESPEAIIKA GDGSFSLKTS KGTVEGFSHV MFATGRKPNT 

       370        380        390        400        410        420 
KNLGLENVGV KMAKNGAIEV DEYSQTSVPS IWAVGDVTDR INLTPVALME GGALAKTLFQ 

       430        440        450        460        470        480 
NEPTKPDYRA VPCAVFSQPP IGTVGLTEEQ AIEQYGDVDV YTSNFRPLKA TLSGLPDRVF 

       490        500        510        520        530        540 
MKLIVCANTN KVLGVHMCGE DSPEIIQGFG VAVKAGLTKA DFDATVGVHP TAAEEFVTMR 

       550        560 
APTRKFRKDS SEGKASPEAK TAAGV 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure and properties of glutathione reductase from Arabidopsis thaliana."
Kubo A., Sano T., Saji H., Tanaka K., Kondo N., Tanaka K.
Plant Cell Physiol. 34:1259-1266(1993)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Columbia.
[2]Kubo A.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14049 mRNA. Translation: BAA03137.1.
D89620 Genomic DNA. Translation: BAA19653.1.
AL138650 Genomic DNA. Translation: CAB77586.1.
CP002686 Genomic DNA. Translation: AEE79262.1.
PIRT47625.
RefSeqNP_191026.1. NM_115323.3.
UniGeneAt.21776.

3D structure databases

ProteinModelPortalP42770.
SMRP42770. Positions 86-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP42770. 1 interaction.

Proteomic databases

PaxDbP42770.
PRIDEP42770.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G54660.1; AT3G54660.1; AT3G54660.
GeneID824631.
KEGGath:AT3G54660.

Organism-specific databases

GeneFarm2285. 251.
TAIRAT3G54660.

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276712.
InParanoidP42770.
KOK00383.
OMALAKTLFQ.
PhylomeDBP42770.

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-2390-MONOMER.

Gene expression databases

GenevestigatorP42770.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006324. Glut-diS_reduct.
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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01424. gluta_reduc_2. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP42770.

Entry information

Entry nameGSHRP_ARATH
AccessionPrimary (citable) accession number: P42770
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names