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Protein

Glutathione reductase, chloroplastic

Gene

GOR

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 sitei283 – 2831NADPBy similarity
Binding sitei289 – 2891NADPBy similarity
Active sitei521 – 5211Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi118 – 12710FADBy 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. 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

BRENDAi1.8.1.7. 3645.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase, chloroplastic (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:GOR
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei‹1 – 66›66Chloroplast1 PublicationAdd
BLAST
Chaini67 – 557491Glutathione reductase, chloroplasticPRO_0000030284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi127 ↔ 132Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP80461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

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: Fragment.

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

P80461-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ATSLSTPKLS TTLSSPTLHS LLYKHKFSLL SLSNPIKPLH FNFLTHSRST
60 70 80 90 100
PSSLSCTRRR FTAPRAESSN GADAPRHYDF DLFTIGAGSG GVRASRFASN
110 120 130 140 150
FGASVAVCEL PFSTISSDST GGVGGTCVLR GCVPKKLLVY ASKYSHEFEE
160 170 180 190 200
SCGFGWNYDV EPRFDWSTLI ANKNAELQRL TGIYKNILKN AGVTLIEGRG
210 220 230 240 250
KVVDPHTVDV DGKLYSAKNI LISVGGRPFI PDIPGSEYAI DSDAALDLPT
260 270 280 290 300
KPNKIAIVGG GYIALEFAGI FNGLKSEVHV FIRQKKVLRG FDEEIRDFVG
310 320 330 340 350
EQMSLRGIEF HTEESPQAIV KSADGSLSLK TSRGTVEGFS HIMFATGRRP
360 370 380 390 400
NTKNLGLETV GVKMTKNGAI EVDEYSRTSV PSIWAVGDVT DRINLTPVAL
410 420 430 440 450
MEGGALAKTI FAHEPTKPDY RNVPAAVFSQ PPIGQVGLME EQAIKEFGDV
460 470 480 490 500
DVYTANFRPL KATISGLPDR VFMKLIVCAK TSKVLGLHMC GDDAPEIVQG
510 520 530 540 550
FAIAVKAGLT KADFDATVGI HPTSAEEFVT MRTPTRKVRS SPSEGKAEHD

IKAAAGV
Length:557
Mass (Da):60,035
Last modified:October 1, 1996 - v1
Checksum:i79813D1C6AA1D784
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76293 mRNA. Translation: CAA53925.1.
PIRiS38908.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76293 mRNA. Translation: CAA53925.1.
PIRiS38908.

3D structure databases

ProteinModelPortaliP80461.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.8.1.7. 3645.

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

  1. "Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme."
    Creissen G.P., Mullineaux P.M.
    Planta 197:422-425(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Willows R.D., Kannangara G.C., Svendsen I.
    Submitted (MAY-1995) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 67-74.
    Tissue: Leaf.

Entry informationi

Entry nameiGSHRP_TOBAC
AccessioniPrimary (citable) accession number: P80461
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 99 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

Direct protein sequencing

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.