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Protein

Glutathione reductase, chloroplastic

Gene

EMB2360

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Maintains high levels of reduced glutathione in the chloroplast.

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
Binding sitei291 – 2911NADPBy similarity
Binding sitei297 – 2971NADPBy similarity
Active sitei529 – 5291Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi126 – 13510FADBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. detoxification of mercury ion Source: InterPro
  3. glutathione metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2390-MONOMER.
ReactomeiREACT_294404. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_298517. PPARA activates gene expression.
REACT_333313. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase, chloroplastic (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Alternative name(s):
Protein EMBRYO DEFECTIVE 2360
Gene namesi
Name:EMB2360
Ordered Locus Names:At3g54660
ORF Names:T5N23_20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G54660.

Subcellular locationi

Plastidchloroplast Curated

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
  3. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7474ChloroplastSequence AnalysisAdd
BLAST
Chaini75 – 565491Glutathione reductase, chloroplasticPRO_0000030280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi135 ↔ 140Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP42770.
PRIDEiP42770.

Expressioni

Gene expression databases

ExpressionAtlasiP42770. baseline and differential.
GenevestigatoriP42770.

Interactioni

Protein-protein interaction databases

IntActiP42770. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP42770.
SMRiP42770. Positions 86-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiP42770.
KOiK00383.
OMAiVIGHNED.
PhylomeDBiP42770.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. 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]
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.
TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42770-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTPKLTST ISSSSPSLQF LCKKLPIAIH LPSSSSSSFL SLPKTLTSLY
60 70 80 90 100
SLRPRIALLS NHRYYHSRRF SVCASTDNGA ESDRHYDFDL FTIGAGSGGV
110 120 130 140 150
RASRFATSFG ASAAVCELPF STISSDTAGG VGGTCVLRGC VPKKLLVYAS
160 170 180 190 200
KYSHEFEDSH GFGWKYETEP SHDWTTLIAN KNAELQRLTG IYKNILSKAN
210 220 230 240 250
VKLIEGRGKV IDPHTVDVDG KIYTTRNILI AVGGRPFIPD IPGKEFAIDS
260 270 280 290 300
DAALDLPSKP KKIAIVGGGY IALEFAGIFN GLNCEVHVFI RQKKVLRGFD
310 320 330 340 350
EDVRDFVGEQ MSLRGIEFHT EESPEAIIKA GDGSFSLKTS KGTVEGFSHV
360 370 380 390 400
MFATGRKPNT KNLGLENVGV KMAKNGAIEV DEYSQTSVPS IWAVGDVTDR
410 420 430 440 450
INLTPVALME GGALAKTLFQ NEPTKPDYRA VPCAVFSQPP IGTVGLTEEQ
460 470 480 490 500
AIEQYGDVDV YTSNFRPLKA TLSGLPDRVF MKLIVCANTN KVLGVHMCGE
510 520 530 540 550
DSPEIIQGFG VAVKAGLTKA DFDATVGVHP TAAEEFVTMR APTRKFRKDS
560
SEGKASPEAK TAAGV
Length:565
Mass (Da):60,852
Last modified:November 1, 1995 - v1
Checksum:i29C2CD0E68ED4E4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14049 mRNA. Translation: BAA03137.1.
D89620 Genomic DNA. Translation: BAA19653.1.
AL138650 Genomic DNA. Translation: CAB77586.1.
CP002686 Genomic DNA. Translation: AEE79262.1.
PIRiT47625.
RefSeqiNP_191026.1. NM_115323.3.
UniGeneiAt.21776.

Genome annotation databases

EnsemblPlantsiAT3G54660.1; AT3G54660.1; AT3G54660.
GeneIDi824631.
KEGGiath:AT3G54660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14049 mRNA. Translation: BAA03137.1.
D89620 Genomic DNA. Translation: BAA19653.1.
AL138650 Genomic DNA. Translation: CAB77586.1.
CP002686 Genomic DNA. Translation: AEE79262.1.
PIRiT47625.
RefSeqiNP_191026.1. NM_115323.3.
UniGeneiAt.21776.

3D structure databases

ProteinModelPortaliP42770.
SMRiP42770. Positions 86-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP42770. 1 interaction.

Proteomic databases

PaxDbiP42770.
PRIDEiP42770.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G54660.1; AT3G54660.1; AT3G54660.
GeneIDi824631.
KEGGiath:AT3G54660.

Organism-specific databases

GeneFarmi2285. 251.
TAIRiAT3G54660.

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiP42770.
KOiK00383.
OMAiVIGHNED.
PhylomeDBiP42770.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2390-MONOMER.
ReactomeiREACT_294404. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_298517. PPARA activates gene expression.
REACT_333313. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiP42770.

Gene expression databases

ExpressionAtlasiP42770. baseline and differential.
GenevestigatoriP42770.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. 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]
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.
TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: cv. Columbia.
  2. Kubo A.
    Submitted (OCT-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.
    , 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiGSHRP_ARATH
AccessioniPrimary (citable) accession number: P42770
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.