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P48640

- GSHRP_SOYBN

UniProt

P48640 - GSHRP_SOYBN

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Protein
Glutathione reductase, chloroplastic
Gene
GR
Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - 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

Binds 1 FAD per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei269 – 2691NADP By similarity
Binding sitei275 – 2751NADP By similarity
Active sitei507 – 5071Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1139FAD 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 (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:GR
OrganismiGlycine max (Soybean) (Glycine hispida)
Taxonomic identifieri3847 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
ProteomesiUP000008827: Unplaced

Subcellular locationi

Plastidchloroplast Reviewed prediction

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 peptidei1 – 5252Chloroplast Reviewed prediction
Add
BLAST
Chaini53 – 544492Glutathione reductase, chloroplastic
PRO_0000030282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi113 ↔ 118Redox-active By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Gene expression databases

GenevestigatoriP48640.

Structurei

3D structure databases

ProteinModelPortaliP48640.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

KOiK00383.

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.

P48640-1 [UniParc]FASTAAdd to Basket

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MATSLSVSPS LSLNTLFIAK ALPLSRPSFL SLPLPKSLLS LSTRRRTFIV    50
RAESQNGRDP VPAHYDFDLF TIGAGSGGVR ARRFAANYGA SVAICELPFS 100
TISSETTGVG GTCVIRGCVP KKLLVYASKF SHEFEESNGF GWRYDSEPKH 150
DWSSFIANKN AELQRLTGIY KNILNNAGVK LIEGHGKMID PHTVDVNGKL 200
YSAKHILVAV GGRPFIPDIP GKELAIDSDA ALDLPTKPVK IAIVGGGYIA 250
LEFAGIFNGL KSEVHVFIRQ KKVLRGFDEE IRDFVEEQMS VRGIEFHTEE 300
SPQAITKSAD GSFSLKTNKG TVDGFSHIMF ATGRRPNTQN LGLESVGVKL 350
AKDGAIEVDE YSQTSVYSIW AVGDVTNRIN LTPVALMEGG ALVKTLFQDN 400
PTKPDYRAVP SAVFSQPPIG QVGLTEEQAV QQYGDIDIFT ANFRPLKATL 450
SGLPDRVFMK LVVCAKTNEV LGLHMCGEDA PEIVQGFAVA LKARLTKADF 500
DATVGIHPSA AEEFVTMRTP TRKIRKSESS EGKSGSQAKA AAGV 544
Length:544
Mass (Da):58,783
Last modified:February 1, 1996 - v1
Checksum:i7A71449EA21CE639
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11632 mRNA. Translation: AAA33962.1.
PIRiT07155.
RefSeqiNP_001238006.1. NM_001251077.1.
UniGeneiGma.32269.

Genome annotation databases

GeneIDi547793.
KEGGigmx:547793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11632 mRNA. Translation: AAA33962.1 .
PIRi T07155.
RefSeqi NP_001238006.1. NM_001251077.1.
UniGenei Gma.32269.

3D structure databases

ProteinModelPortali P48640.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 547793.
KEGGi gmx:547793.

Phylogenomic databases

KOi K00383.

Gene expression databases

Genevestigatori P48640.

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. "Soybean root nodule cDNA encoding glutathione reductase."
    Tang X., Webb M.A.
    Plant Physiol. 104:1081-1082(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Root nodule.

Entry informationi

Entry nameiGSHRP_SOYBN
AccessioniPrimary (citable) accession number: P48640
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 103 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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