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Q60151

- GSHR_STRTR

UniProt

Q60151 - GSHR_STRTR

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Protein

Glutathione reductase

Gene

gor

Organism
Streptococcus thermophilus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Maintains high levels of reduced glutathione in the cytosol.By similarity

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
Active sitei439 – 4391Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429FADBy 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 (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:gor
OrganismiStreptococcus thermophilus
Taxonomic identifieri1308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Glutathione reductasePRO_0000067979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 47Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ60151.
SMRiQ60151. Positions 3-450.
ModBaseiSearch...
MobiDBiSearch...

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.
IPR006322. Glutathione_Rdtase_euk/bac.
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.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60151-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKEYDYIVI GGGSGGIASA NRAAMHGAKV ILFEGKEVGG TCVNVGCVPK
60 70 80 90 100
KVMWYGAQVA ETLHRYAGEY GFDVTINNFD FATLKANRQA YIDRIHGSFE
110 120 130 140 150
RGFDSNGVER VYEYARFVDP HTVEVAGELY TAPHILIATG GHPLYPNIPG
160 170 180 190 200
SEYGITSDGF FELDEVPKRT AVIGAGYIAV EVAGVLNALG SDTHLFVRKD
210 220 230 240 250
RPLRTFDKDI IDVLVDEMAK SGPTLHMHAN ATEVVKNADD SLTISFDNEE
260 270 280 290 300
TITVDCLIWA VGRAANTSGF GLEKTGVELT ERGNIYSDEF ENTSVPGIYA
310 320 330 340 350
LGDVTGKLDL TPVAVKAGRQ LSERLFNNKV DAKLDYTDVA TVVFSHPAIG
360 370 380 390 400
AIGLTEEKAI AKYGAENIKV YKSSFTPMYT ALGDNRQLST MKLVTLGEDE
410 420 430 440 450
KIIGLHGIGY GVDEMIQGFS VAIKMGATKA DFDNTVAIHP TGSEEFVTMR
Length:450
Mass (Da):48,712
Last modified:November 1, 1996 - v1
Checksum:i6A0DA46BEA828804
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27672 Genomic DNA. Translation: AAB00353.1.
Z29494 Genomic DNA. Translation: CAA82630.1.
PIRiS41386.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27672 Genomic DNA. Translation: AAB00353.1 .
Z29494 Genomic DNA. Translation: CAA82630.1 .
PIRi S41386.

3D structure databases

ProteinModelPortali Q60151.
SMRi Q60151. Positions 3-450.
ModBasei Search...
MobiDBi 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.
IPR006322. Glutathione_Rdtase_euk/bac.
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 TIGR01421. gluta_reduc_1. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNRZ368."
    Pebay M., Holl A.-C., Simonet J.-M., Decaris B.
    Res. Microbiol. 146:371-383(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CNRZ 368.

Entry informationi

Entry nameiGSHR_STRTR
AccessioniPrimary (citable) accession number: Q60151
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 93 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3