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P27456

- GSHRP_PEA

UniProt

P27456 - GSHRP_PEA

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Protein
Glutathione reductase, chloroplastic/mitochondrial
Gene
GR, GOR1
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

Binds 1 FAD per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei277 – 2771NADP By similarity
Binding sitei283 – 2831NADP By similarity
Active sitei515 – 5151Proton acceptor By similarity

Regions

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

GO - Molecular functioni

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

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6060Chloroplast and mitochondrion Reviewed prediction
Add
BLAST
Chaini61 – 552492Glutathione reductase, chloroplastic/mitochondrial
PRO_0000030281Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP27456.

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

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MNQAMATPLS LSCCSPTLTR STLFFTKTFP FSRSFSTPLP LSTKTLISLS    50
PPHRTFAVRA ESQNGADPAR QYDFDLFTIG AGSGGVRASR FASNFGASSA 100
VCELPFSTIS SDTTGGVGGT CVIRGCVPKK LLVYASKFSH EFEESNGFGW 150
RYDSEPKHDW SSLIANKNAE LQRLTGIYKN TLKNAGVKLI EGRGKIVDAH 200
TVDVDGKLYS AKHILVSVGG RPFIPDIPGK EYAIDSDAAL DLPSKPQKIA 250
IVGGGYIALE FAGIFNGLKS EVHVFIRQKK VLRGFDEEIR DFVAENMALR 300
GIEFHTEESP VAITKAADGS LSLKTNKGTE EGFSHIMFAT GRSPNTKDLG 350
LESVGVKVAK DGSIEVDEYS QTSVPSIWAI GDATNRVNLT PVALMEGVAL 400
AKTLFQNEPT KPDYRAIPSA VFSQPPIGGV GLTEEQAAEQ YGDIDVFTAN 450
FRPMKATLSG LPDRVFMKLI VSAETNVVLG LHMCGEDAAE IAQGFAVGIK 500
AGLTKADFDA TVGIHPTAAE EFVTMRTPTR KVRKNQASQG KSDSKAKAVA 550
GS 552
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60373 mRNA. Translation: CAA42921.1. Different initiation.
X90996 Genomic DNA. Translation: CAA62482.1.
PIRiS18973.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60373 mRNA. Translation: CAA42921.1 . Different initiation.
X90996 Genomic DNA. Translation: CAA62482.1 .
PIRi S18973.

3D structure databases

ProteinModelPortali P27456.
ModBasei 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: June 11, 2014
This is version 102 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

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