Reviewed, UniProtKB/Swiss-Prot Q6HA23 (GSHR_KLULA)

Names and origin

Protein names

Recommended name:
    Glutathione reductase
      Short name=GRase
      Short name=GR
    EC=1.8.1.7

Gene names

Name:	GLR1
Ordered Locus Names:	KLLA0E24112g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
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 By similarity.
Catalytic activity	2 glutathione + NADP+ = glutathione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond By similarity.
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
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro 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 – 484	484	Glutathione reductase		PRO_0000067968
Regions
	Nucleotide binding	52 – 60	9	FAD By similarity
Sites
	Active site	473	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	60 ↔ 65		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HA23-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: CEE24F6377CC0ECB	FASTA	484	53,378
	10 20 30 40 50 60 MSIRNTINRI IIRRNMSDSI RHYDYLVIGG GSGGVASSRR AASYGAKTLL IEAKAMGGTC 70 80 90 100 110 120 VNKGCVPKKV MWYASDLATR IGHAHSYNLF EDLPLTKENL TFNWPEFKKK RDAYIHRLNG 130 140 150 160 170 180 IYERNLTKEG VDYVYGWASF TVDGKVQVKK ADNCTETYTA DHILVATGGK PIYPAKIPGY 190 200 210 220 230 240 DYGVSSDEFF ELEDQPKKVV VVGAGYIGVE IAGVFNGLGS DSHLVIRGET VLRKFDDCIQ 250 260 270 280 290 300 ETVTDTYIKE GVNIHKSSNV TKVEKDESTG KLNIQLDTGK NIDNVDSLIW TIGRRSLLGL 310 320 330 340 350 360 GLENIGVKLD AKEQIVVDEY QNSSVKNVYS LGDVVGKVEL TPVAIAAGRK LSNRLFGPEK 370 380 390 400 410 420 FKNQKQDYEN VPSVVFSHPE AGSIGLSERE AIEKFGKDNV KVYNSKFNAM YYAMMEEKDK 430 440 450 460 470 480 TPTRYKLVCT GEEEKVVGLH IIGDSSAEIL QGFGVAIKMG ATKADFDSCV AIHPTSAEEL VTLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two nuclear genes encoding glutathione and thioredoxin reductases from the yeast Kluyveromyces lactis." Tarrio N., Diaz Prado S., Cerdan M.E., Gonzales Siso M.I. Biochim. Biophys. Acta 1678:170-175(2004) [PubMed: 15157744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ504414 Genomic DNA. Translation: CAD43213.1. CR382125 Genomic DNA. Translation: CAH00123.1.
RefSeq	XP_455036.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2894346.
KEGG	kla:KLLA0E24112g.
Phylogenomic databases
HOGENOM	Q6HA23.
OMA	Q6HA23. EFQNTSR.
Enzyme and pathway databases
BRENDA	1.8.1.7. 74088.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glut_reduct_1. IPR000815. Hg_reductase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01421. gluta_reduc_1. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHR_KLULA

Accession

Primary (citable) accession number: Q6HA23
Secondary accession number(s): Q6CM03

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)