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P27456

- GSHRP_PEA

UniProt

P27456 - GSHRP_PEA

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Protein

Glutathione reductase, chloroplastic/mitochondrial

Gene

GR

Organism
Pisum sativum (Garden pea)
Status
Reviewed - 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 sitei277 – 2771NADPBy similarity
Binding sitei283 – 2831NADPBy similarity
Active sitei515 – 5151Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi112 – 12110FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. glutathione-disulfide reductase activity Source: UniProtKB-EC
  3. NADP binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. 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/mitochondrial (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Alternative name(s):
GOR1
Gene namesi
Name:GR
Synonyms:GOR1
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

Plastidchloroplast 1 Publication. Mitochondrion 1 Publication
Note: The majority of the protein is found in chloroplast, with only 3% in mitochondria.

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
  2. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6060Chloroplast and mitochondrionSequence AnalysisAdd
BLAST
Chaini61 – 552492Glutathione reductase, chloroplastic/mitochondrialPRO_0000030281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi121 ↔ 126Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP27456.
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: Complete.

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

P27456-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNQAMATPLS LSCCSPTLTR STLFFTKTFP FSRSFSTPLP LSTKTLISLS
60 70 80 90 100
PPHRTFAVRA ESQNGADPAR QYDFDLFTIG AGSGGVRASR FASNFGASSA
110 120 130 140 150
VCELPFSTIS SDTTGGVGGT CVIRGCVPKK LLVYASKFSH EFEESNGFGW
160 170 180 190 200
RYDSEPKHDW SSLIANKNAE LQRLTGIYKN TLKNAGVKLI EGRGKIVDAH
210 220 230 240 250
TVDVDGKLYS AKHILVSVGG RPFIPDIPGK EYAIDSDAAL DLPSKPQKIA
260 270 280 290 300
IVGGGYIALE FAGIFNGLKS EVHVFIRQKK VLRGFDEEIR DFVAENMALR
310 320 330 340 350
GIEFHTEESP VAITKAADGS LSLKTNKGTE EGFSHIMFAT GRSPNTKDLG
360 370 380 390 400
LESVGVKVAK DGSIEVDEYS QTSVPSIWAI GDATNRVNLT PVALMEGVAL
410 420 430 440 450
AKTLFQNEPT KPDYRAIPSA VFSQPPIGGV GLTEEQAAEQ YGDIDVFTAN
460 470 480 490 500
FRPMKATLSG LPDRVFMKLI VSAETNVVLG LHMCGEDAAE IAQGFAVGIK
510 520 530 540 550
AGLTKADFDA TVGIHPTAAE EFVTMRTPTR KVRKNQASQG KSDSKAKAVA

GS
Length:552
Mass (Da):59,108
Last modified:August 1, 1992 - v1
Checksum:i690D1058AE4168BC
GO

Sequence cautioni

The sequence CAA42921.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60373 mRNA. Translation: CAA42921.1. Different initiation.
X90996 Genomic DNA. Translation: CAA62482.1.
PIRiS18973.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60373 mRNA. Translation: CAA42921.1 . Different initiation.
X90996 Genomic DNA. Translation: CAA62482.1 .
PIRi S18973.

3D structure databases

ProteinModelPortali P27456.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01424. gluta_reduc_2. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.)."
    Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P.M.
    Plant J. 2:129-131(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leaf.
  2. "Characterisation of a glutathione reductase gene and its genetic locus from pea (Pisum sativum L.)."
    Mullineaux P.M., Enard C., Hellens R., Creissen G.
    Planta 200:186-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Birte.
  3. "Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco."
    Creissen G.P., Reynolds H., Xue Y., Mullineaux P.M.
    Plant J. 8:167-175(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGSHRP_PEA
AccessioniPrimary (citable) accession number: P27456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 105 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