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P48639

- GSHR_BURCE

UniProt

P48639 - GSHR_BURCE

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Protein
Glutathione reductase
Gene
gor
Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

Binds 1 FAD per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei435 – 4351Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 439FAD 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

GO - Biological processi

  1. 2,4,5-trichlorophenoxyacetic acid catabolic process Source: UniProtKB-UniPathway
  2. cell redox homeostasis Source: InterPro
  3. glutathione metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

UniPathwayiUPA00686.

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

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Glutathione reductase
PRO_0000067974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 48Redox-active By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP48639.

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP48639.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

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.

P48639-1 [UniParc]FASTAAdd to Basket

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MQKYDFDLFV IGAGSGGVRA ARIAAGHGAK VAIAEEYRFG GTCVIRGCVP    50
KKLLMYASQY GQGFEDAAGF GWHSAATSHS WTSLIAAKDA EIARLEGVYQ 100
RLIENANVEI FKGRAQIAGP NRVTVTGASV SARTILIATG ARPVMPPVAG 150
ANLMITSDDV FDLPVGPPRI AIIGGGYIAC EFAGIFNGLG RHVVQLHRGS 200
QVLRGFDDEL REHLGDELKK SGIDLRLGVD VVAVERQRGA LSVQLTTGDA 250
MEVDAVMAAT GRLPNTWGLG LETVDVGLDQ NGAIKVDEYS RTSSPGIYAV 300
GDVTNRLNLT PVAIHEGHAF ADTVFGGKAL PTEHENVPFA VFSQPQAASV 350
GLSEAQARDR YSNVEIYGSA FRPMRAALSG RDEKALVKLV VNGSNDRVVG 400
AHIVGADAAE IIQGIAVAIK ARATKADFDA TLGVHPTLAE EFVTLRNRR 449
Length:449
Mass (Da):47,541
Last modified:February 1, 1996 - v1
Checksum:i402FCC6E7A8D6720
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19883 Genomic DNA. Translation: AAC43334.1.
PIRiI40178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19883 Genomic DNA. Translation: AAC43334.1 .
PIRi I40178.

3D structure databases

ProteinModelPortali P48639.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P48639.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00686 .

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. "Sequence analysis of a gene cluster involved in metabolism of 2,4,5-trichlorophenoxyacetic acid by Burkholderia cepacia AC1100."
    Daubaras D.L., Hershberger C.D., Kitano K., Chakrabarty A.M.
    Appl. Environ. Microbiol. 61:1279-1289(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: AC1100.

Entry informationi

Entry nameiGSHR_BURCE
AccessioniPrimary (citable) accession number: P48639
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 16, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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