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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

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei269 – 2691NADPBy similarity
Binding sitei275 – 2751NADPBy similarity
Active sitei507 – 5071Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1139FADBy 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 (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 Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252ChloroplastSequence AnalysisAdd
BLAST
Chaini53 – 544492Glutathione reductase, chloroplasticPRO_0000030282Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Expressioni

Gene expression databases

GenevestigatoriP48640.

Structurei

3D structure databases

ProteinModelPortaliP48640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

InParanoidiP48640.
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

« Hide

        10         20         30         40         50
MATSLSVSPS LSLNTLFIAK ALPLSRPSFL SLPLPKSLLS LSTRRRTFIV
60 70 80 90 100
RAESQNGRDP VPAHYDFDLF TIGAGSGGVR ARRFAANYGA SVAICELPFS
110 120 130 140 150
TISSETTGVG GTCVIRGCVP KKLLVYASKF SHEFEESNGF GWRYDSEPKH
160 170 180 190 200
DWSSFIANKN AELQRLTGIY KNILNNAGVK LIEGHGKMID PHTVDVNGKL
210 220 230 240 250
YSAKHILVAV GGRPFIPDIP GKELAIDSDA ALDLPTKPVK IAIVGGGYIA
260 270 280 290 300
LEFAGIFNGL KSEVHVFIRQ KKVLRGFDEE IRDFVEEQMS VRGIEFHTEE
310 320 330 340 350
SPQAITKSAD GSFSLKTNKG TVDGFSHIMF ATGRRPNTQN LGLESVGVKL
360 370 380 390 400
AKDGAIEVDE YSQTSVYSIW AVGDVTNRIN LTPVALMEGG ALVKTLFQDN
410 420 430 440 450
PTKPDYRAVP SAVFSQPPIG QVGLTEEQAV QQYGDIDIFT ANFRPLKATL
460 470 480 490 500
SGLPDRVFMK LVVCAKTNEV LGLHMCGEDA PEIVQGFAVA LKARLTKADF
510 520 530 540
DATVGIHPSA AEEFVTMRTP TRKIRKSESS EGKSGSQAKA AAGV
Length:544
Mass (Da):58,783
Last modified:February 1, 1996 - v1
Checksum:i7A71449EA21CE639
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 547793.
KEGGi gmx:547793.

Phylogenomic databases

InParanoidi P48640.
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: November 26, 2014
This is version 106 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