Q6C5H4 (GSHR_YARLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	GLR1
Ordered Locus Names:	YALI0E18029g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide 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 – 470	470	Glutathione reductase		PRO_0000067971
Regions
	Nucleotide binding	36 – 44	9	FAD By similarity
Sites
	Active site	459	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	44 ↔ 49		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6C5H4 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: B9E4760F181DD143	FASTA	470	51,302
	10 20 30 40 50 60 MASIPHYDYL VIGGGSGGVA SARRAASYGA KTLLIEGKAL GGTCVNVGCV PKKVMWNASD 70 80 90 100 110 120 LAGRIRQAKE YGFPDVDPKY ADNFDWSGFK AKRDAYVKRL NGIYERNLQK EGVEYVFGWA 130 140 150 160 170 180 TLYKQEGQEF PLVHVKSDDG NTKLYSAKKI MIATGGKPRL PDVPGAEYGI DSDGFFALET 190 200 210 220 230 240 QPKRVAVVGG GYIGVELAGV FHGLNSETTL FCRGQTVLRA FDIMIQDTIT DYYVKEGINV 250 260 270 280 290 300 LKGSGVKKIV KKDNGELLVT YEQDGAEKDI TLDSLIWTIG REPLKDTLNL GEFGIKTNKR 310 320 330 340 350 360 GYIEVDEYQR SSVDNIYSLG DVCGKVELTP MAIAAGRKLS NRLFGPTEFK NQKQDYTDVP 370 380 390 400 410 420 SAVFSHPEVG SIGITEAAAK EQYGEENVKV YTSKFVAMYY AMLEEKAPTA YKLVCAGKDE 430 440 450 460 470 KVVGLHIVGA DSAEILQGFG VAIRMGATKA DFDNVVAIHP TSAEELVTMR

References

[1]

"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: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382131 Genomic DNA. Translation: CAG79681.1.
RefSeq	XP_504088.1. XM_504088.1.
3D structure databases
ProteinModelPortal	Q6C5H4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6C5H4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2911696.
GenomeReviews	Gene locus YALI0E18029g in contig CR382131_GR.
KEGG	yli:YALI0E18029g.
Phylogenomic databases
eggNOG	fuNOG04327.
HOGENOM	HBG515043.
OMA	KVVGLHM.
OrthoDB	EOG415KNX.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KO	K00383.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01421. Gluta_reduc_1. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHR_YARLI

Accession

Primary (citable) accession number: Q6C5H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	August 16, 2004
Last modified:	December 14, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program