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Reviewed, UniProtKB/Swiss-Prot P48638 (GSHR_ANASP)

Last modified November 25, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutathione reductase
      Short name=GRase
      Short name=GR
    EC=1.8.1.7
Gene names
Name: gor
Ordered Locus Names: all4968
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activity

2 glutathione + NADP(+) = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Glutathione reductase
PRO_0000067973

Regions

Nucleotide binding34 – 429FAD By similarity

Sites

Active site4481Proton acceptor By similarity

Amino acid modifications

Disulfide bond42 ↔ 47Redox-active By similarity

Experimental info

Sequence conflict2341E → Q in CAA61856. Ref.1
Sequence conflict3401R → L in CAA61856. Ref.1
Sequence conflict3611V → L in CAA61856. Ref.1
Sequence conflict3721L → H in CAA61856. Ref.1
Sequence conflict381 – 3833RTR → AP in CAA61856. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48638-1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 29C1F06CE2195888

FASTA45949,478
        10         20         30         40         50         60 
MTFDYDLFVI GAGSGGLAAS KRAASYGAKV AIAENDLVGG TCVIRGCVPK KLMVYGSHFP 

        70         80         90        100        110        120 
ALFEDAAGYG WQVGKAELNW EHFITSIDKE VRRLSQLHIS FLEKAGVELI SGRATLVDNH 

       130        140        150        160        170        180 
TVEVGERKFT ADKILIAVGG RPIKPELPGM EYGITSNEIF HLKTQPKHIA IIGSGYIGTE 

       190        200        210        220        230        240 
FAGIMRGLGS QVTQITRGDK ILKGFDEDIR TEIQEGMTNH GIRIIPKNVV TAIEQVPEGL 

       250        260        270        280        290        300 
KISLSGEDQE PIIADVFLVA TGRVPNVDGL GLENAGVDVV DSSIEGPGYS TMNAIAVNEY 

       310        320        330        340        350        360 
SQTSQPNIYA VGDVTDRLNL TPVAIGEGRA FADSEFGNNR REFSHETIAT AVFSNPQAST 

       370        380        390        400        410        420 
VGLTEAEARA KLGDDAVTIY RTRFRPMYHS FTGKQERIMM KLVVDTKTDK VLGAHMVGEN 

       430        440        450 
AAEIIQGVAI AVKMGATKKD FDATVGIHPS SAEEFVTMR 

« Hide

References

« Hide 'large scale' references
[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: 7559423] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

X89712 Genomic DNA. Translation: CAA61856.1.
BA000019 Genomic DNA. Translation: BAB76667.1.
PIRAH2426.
I39477.
RefSeqNP_489008.1.

3D structure databases

HSSPHSSP built from PDB template 1ONF based on UniProtKB Q94655.
ModBaseSearch...

Genome annotation databases

GeneID1108569.
GenomeReviewsGene locus all4968 in contig BA000019_GR.
KEGGana:all4968.
NMPDRfig|103690.1.peg.5275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP48638.

Enzyme and pathway databases

BioCycNSP103690:ALL4968-MON.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006324. Glut_reduct_pln.
IPR000815. Hg_reductase.
IPR001100. Pyr_nuc-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
PR00411. PNDRDTASEI.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01424. gluta_reduc_2. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHR_ANASP
AccessionPrimary (citable) accession number: P48638
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2002
Last modified: November 25, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents