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Protein

Glutathione reductase

Gene

gor

Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Miscellaneous

The active site is a redox-active disulfide bond.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Pathwayi: (2,4,5-trichlorophenoxy)acetate degradation

This protein is involved in the pathway (2,4,5-trichlorophenoxy)acetate degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway (2,4,5-trichlorophenoxy)acetate degradation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei435Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 43FADBy similarity9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

UniPathwayi
UPA00686

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:gor
OrganismiBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifieri292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000679741 – 449Glutathione reductaseAdd BLAST449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi43 ↔ 48Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP48639

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP48639
SMRiP48639
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 3 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006324 Glut-diS_reduct
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit
PIRSFiPIRSF000350 Mercury_reductase_MerA, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit
TIGRFAMsiTIGR01424 gluta_reduc_2, 1 hit
PROSITEiView protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 1 hit

Sequencei

Sequence statusi: Complete.

P48639-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQKYDFDLFV IGAGSGGVRA ARIAAGHGAK VAIAEEYRFG GTCVIRGCVP
60 70 80 90 100
KKLLMYASQY GQGFEDAAGF GWHSAATSHS WTSLIAAKDA EIARLEGVYQ
110 120 130 140 150
RLIENANVEI FKGRAQIAGP NRVTVTGASV SARTILIATG ARPVMPPVAG
160 170 180 190 200
ANLMITSDDV FDLPVGPPRI AIIGGGYIAC EFAGIFNGLG RHVVQLHRGS
210 220 230 240 250
QVLRGFDDEL REHLGDELKK SGIDLRLGVD VVAVERQRGA LSVQLTTGDA
260 270 280 290 300
MEVDAVMAAT GRLPNTWGLG LETVDVGLDQ NGAIKVDEYS RTSSPGIYAV
310 320 330 340 350
GDVTNRLNLT PVAIHEGHAF ADTVFGGKAL PTEHENVPFA VFSQPQAASV
360 370 380 390 400
GLSEAQARDR YSNVEIYGSA FRPMRAALSG RDEKALVKLV VNGSNDRVVG
410 420 430 440
AHIVGADAAE IIQGIAVAIK ARATKADFDA TLGVHPTLAE EFVTLRNRR
Length:449
Mass (Da):47,541
Last modified:February 1, 1996 - v1
Checksum:i402FCC6E7A8D6720
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19883 Genomic DNA Translation: AAC43334.1
PIRiI40178

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19883 Genomic DNA Translation: AAC43334.1
PIRiI40178

3D structure databases

ProteinModelPortaliP48639
SMRiP48639
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP48639

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00686

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 3 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006324 Glut-diS_reduct
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit
PIRSFiPIRSF000350 Mercury_reductase_MerA, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit
TIGRFAMsiTIGR01424 gluta_reduc_2, 1 hit
PROSITEiView protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGSHR_BURCE
AccessioniPrimary (citable) accession number: P48639
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 28, 2018
This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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