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Protein

Glutathione reductase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 3 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)DescriptionActionsGraphical viewLength
Binding sitei224NADPBy similarity1
Binding sitei230NADPBy similarity1
Active sitei462Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi54 – 63FADBy similarity10

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase, chloroplastic (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei‹1 – 2ChloroplastSequence analysis›2
ChainiPRO_00000302833 – 489Glutathione reductase, chloroplasticAdd BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi63 ↔ 68Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ43154.

Structurei

3D structure databases

ProteinModelPortaliQ43154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006324. Glut-diS_reduct.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. 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.

Q43154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EDNHSTVEDD AANYDFDLFV IGAGSGGVRA ARFSANLGAK VGICELPFHP
60 70 80 90 100
ISSEVIGGVG GTCVIRGCVP KKILVYGASF GGELEDAKNY GWELNEKIDF
110 120 130 140 150
NWKKLLQKKT DEIIRLNNIY KRLLSNAGVK LYEGEGKIVG PNEVQVTQLD
160 170 180 190 200
GTKLSYSAKH ILIATGSRAQ RPNIPGQELA ITSDEALSLE EFPKRVVILG
210 220 230 240 250
GGYISVEFAS IWRGMGADVN LCFRKELPLR GFDDEMRAAV ARNLEGRGVN
260 270 280 290 300
VHPRTTLTEL VKTDGGVVAR TDHGEEIEAD VVLFATGRSP NTKRLNLEAL
310 320 330 340 350
GVELDRTGAV KVDEYSRTSV PSIWAIGDVT NRMNLTPVAL MEGTCFAKTV
360 370 380 390 400
FGGQNSKPDY SNIACAVFSI PPLAVVGLSE EQAIEQASGD ILVFTSSFNP
410 420 430 440 450
MKNTISGRQE KTIMKLVVDA ETDKVLGASM CGPDAAEIMQ GIAIALKFGA
460 470 480
TKAQFDSTVG IHPSAAEEFV TMREPSRRVP GAGKPKTNL
Length:489
Mass (Da):52,611
Last modified:November 1, 1997 - v1
Checksum:i970FC5B079A72CCD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37870 mRNA. Translation: BAA07108.1.
PIRiT09151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37870 mRNA. Translation: BAA07108.1.
PIRiT09151.

3D structure databases

ProteinModelPortaliQ43154.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ43154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006324. Glut-diS_reduct.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSHRP_SPIOL
AccessioniPrimary (citable) accession number: Q43154
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 5, 2016
This is version 98 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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.