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Reviewed, UniProtKB/Swiss-Prot P42770 (GSHRP_ARATH)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutathione reductase, chloroplastic
      Short name=GRase
      Short name=GR
    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) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

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
P42770-1 [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: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

D14049 mRNA. Translation: BAA03137.1.
D89620 Genomic DNA. Translation: BAA19653.1.
AL138650 Genomic DNA. Translation: CAB77586.1.
IPIIPI00546267.
PIRT47625.
RefSeqNP_191026.1.
UniGeneAt.21776

3D structure databases

HSSPHSSP built from PDB template 1GER based on UniProtKB P06715.
ModBaseSearch...

Proteomic databases

PRIDEP42770.

Genome annotation databases

GeneID824631.
GenomeReviewsGene locus AT3G54660 in contig BA000014_GR.
KEGGath:AT3G54660.

Organism-specific databases

GeneFarm2285. 251.
TAIRAt3g54660.

Phylogenomic databases

OMAP42770. LHISFLE.

Enzyme and pathway databases

BRENDA1.8.1.7. 302.

Gene expression databases

ArrayExpressP42770.
GermOnlineAT3G54660. Arabidopsis thaliana.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006324. Glut_reduct_pln.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01424. gluta_reduc_2. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents