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P48638

- GSHR_NOSS1

UniProt

P48638 - GSHR_NOSS1

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Protein

Glutathione reductase

Gene

gor

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Maintains high levels of reduced glutathione in the cytosol.

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 sitei448 – 4481Proton 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
Ordered Locus Names:all4968
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000002483: Chromosome

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 – 459459Glutathione reductasePRO_0000067973Add
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

Protein-protein interaction databases

STRINGi103690.all4968.

Structurei

3D structure databases

ProteinModelPortaliP48638.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
KOiK00383.
OMAiANVEANC.
OrthoDBiEOG6QCD6D.

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.

P48638-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTFDYDLFVI GAGSGGLAAS KRAASYGAKV AIAENDLVGG TCVIRGCVPK
60 70 80 90 100
KLMVYGSHFP ALFEDAAGYG WQVGKAELNW EHFITSIDKE VRRLSQLHIS
110 120 130 140 150
FLEKAGVELI SGRATLVDNH TVEVGERKFT ADKILIAVGG RPIKPELPGM
160 170 180 190 200
EYGITSNEIF HLKTQPKHIA IIGSGYIGTE FAGIMRGLGS QVTQITRGDK
210 220 230 240 250
ILKGFDEDIR TEIQEGMTNH GIRIIPKNVV TAIEQVPEGL KISLSGEDQE
260 270 280 290 300
PIIADVFLVA TGRVPNVDGL GLENAGVDVV DSSIEGPGYS TMNAIAVNEY
310 320 330 340 350
SQTSQPNIYA VGDVTDRLNL TPVAIGEGRA FADSEFGNNR REFSHETIAT
360 370 380 390 400
AVFSNPQAST VGLTEAEARA KLGDDAVTIY RTRFRPMYHS FTGKQERIMM
410 420 430 440 450
KLVVDTKTDK VLGAHMVGEN AAEIIQGVAI AVKMGATKKD FDATVGIHPS

SAEEFVTMR
Length:459
Mass (Da):49,478
Last modified:January 23, 2002 - v2
Checksum:i29C1F06CE2195888
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341E → Q in CAA61856. (PubMed:7559423)Curated
Sequence conflicti340 – 3401R → L in CAA61856. (PubMed:7559423)Curated
Sequence conflicti361 – 3611V → L in CAA61856. (PubMed:7559423)Curated
Sequence conflicti372 – 3721L → H in CAA61856. (PubMed:7559423)Curated
Sequence conflicti381 – 3833RTR → AP in CAA61856. (PubMed:7559423)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89712 Genomic DNA. Translation: CAA61856.1.
BA000019 Genomic DNA. Translation: BAB76667.1.
PIRiAH2426.
I39477.
RefSeqiNP_489008.1. NC_003272.1.
WP_010999094.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB76667; BAB76667; BAB76667.
GeneIDi1108569.
KEGGiana:all4968.
PATRICi22780609. VBINosSp37423_5746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89712 Genomic DNA. Translation: CAA61856.1 .
BA000019 Genomic DNA. Translation: BAB76667.1 .
PIRi AH2426.
I39477.
RefSeqi NP_489008.1. NC_003272.1.
WP_010999094.1. NC_003272.1.

3D structure databases

ProteinModelPortali P48638.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 103690.all4968.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB76667 ; BAB76667 ; BAB76667 .
GeneIDi 1108569.
KEGGi ana:all4968.
PATRICi 22780609. VBINosSp37423_5746.

Phylogenomic databases

eggNOGi COG1249.
HOGENOMi HOG000276712.
KOi K00383.
OMAi ANVEANC.
OrthoDBi EOG6QCD6D.

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

« Hide 'large scale' publications
  1. "Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120."
    Jiang F., Hellman U., Sroga G.E., Bergman B., Mannervik B.
    J. Biol. Chem. 270:22882-22889(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.

Entry informationi

Entry nameiGSHR_NOSS1
AccessioniPrimary (citable) accession number: P48638
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2002
Last modified: November 26, 2014
This is version 108 of the entry and version 2 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3