Reviewed, UniProtKB/Swiss-Prot P11804 (GSHR_SPISP)

Names and origin

Protein names	Recommended name:     Glutathione reductase       Short name=GRase       Short name=GR     EC=1.8.1.7
Organism	Spirulina sp.
Taxonomic identifier	1157 [NCBI]
Taxonomic lineage	Bacteria › Cyanobacteria › Oscillatoriales › Spirulina

Protein attributes

Sequence length	58 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glutathione-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›58	›58	Glutathione reductase		PRO_0000067978
Regions
	Nucleotide binding	5 – 13	9	FAD By similarity
Amino acid modifications
	Disulfide bond	13 ↔ 18		Redox-active
Experimental info
	Non-adjacent residues	21 – 22	2
	Non-adjacent residues	43 – 44	2
	Non-terminal residue	1	1
	Non-terminal residue	58	1

Sequences

	Sequence		Length	Mass (Da)
	P11804-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: B2C2A050EF55B5EF	FASTA	58	5,952
	10 20 30 40 50 VAIAENSVVG GTCVIRGCVP KLTLTGDDTE PLIVDALLCA TGRTTQSNIF AVGDCTDR

References

[1]

"Isolation and sequence studies of cysteinyl peptides from Spirulina glutathione reductase: comparison of active site cysteine peptides with those of other flavoprotein disulfide oxidoreductases." Cui J.-Y., Wakabayashi S., Wada K., Fukuyama K., Matsubara H. J. Biochem. 105:390-394(1989) [PubMed: 2499573] [Abstract] Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.

Cross-references

Sequence databases
PIR	PX0017.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR012999. Pyr_OxRdtase_I_AS. [Graphical view]
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHR_SPISP

Accession

Primary (citable) accession number: P11804

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 4, 2008
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)