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Protein

Glutathione reductase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei224 – 2241NADPBy similarity
Binding sitei230 – 2301NADPBy similarity
Active sitei462 – 4621Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi54 – 6310FADBy 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

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

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 – 2›2ChloroplastSequence Analysis
Chaini3 – 489487Glutathione reductase, chloroplasticPRO_0000030283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi63 ↔ 68Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

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.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. Aono M., Fujiyama K., Sano T., Tanaka K.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. New Asia.
    Tissue: Leaf.

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: March 4, 2015
This is version 92 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

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.