Reviewed, UniProtKB/Swiss-Prot P42770 (GSHRP_ARATH)

Names and origin

Protein names

Recommended name:
    Glutathione reductase, chloroplastic
      Short name=GRase
      Short name=GR
    EC=1.8.1.7
Alternative name(s):
    Protein EMBRYO DEFECTIVE 2360

Gene names

Name:	EMB2360
Ordered Locus Names:	At3g54660
ORF Names:	T5N23_20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Maintains high levels of reduced glutathione in the chloroplast.
Catalytic activity	2 glutathione + NADP+ = glutathione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Plastid › chloroplast Potential.
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	Chloroplast Plastid
Domain	Redox-active center Transit peptide
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	chloroplast stroma Inferred from direct assay. Source: TAIR mitochondrion Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from direct assay. Source: TAIR 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
	Transit peptide	1 – 74	74	Chloroplast Potential
	Chain	75 – 565	491	Glutathione reductase, chloroplastic		PRO_0000030280
Regions
	Nucleotide binding	126 – 135	10	FAD By similarity
Sites
	Active site	529	1	Proton acceptor By similarity
	Binding site	291	1	NADP By similarity
	Binding site	297	1	NADP By similarity
Amino acid modifications
	Disulfide bond	135 ↔ 140		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42770-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 29C2CD0E68ED4E4A	FASTA	565	60,852
	10 20 30 40 50 60 MASTPKLTST ISSSSPSLQF LCKKLPIAIH LPSSSSSSFL SLPKTLTSLY SLRPRIALLS 70 80 90 100 110 120 NHRYYHSRRF SVCASTDNGA ESDRHYDFDL FTIGAGSGGV RASRFATSFG ASAAVCELPF 130 140 150 160 170 180 STISSDTAGG VGGTCVLRGC VPKKLLVYAS KYSHEFEDSH GFGWKYETEP SHDWTTLIAN 190 200 210 220 230 240 KNAELQRLTG IYKNILSKAN VKLIEGRGKV IDPHTVDVDG KIYTTRNILI AVGGRPFIPD 250 260 270 280 290 300 IPGKEFAIDS DAALDLPSKP KKIAIVGGGY IALEFAGIFN GLNCEVHVFI RQKKVLRGFD 310 320 330 340 350 360 EDVRDFVGEQ MSLRGIEFHT EESPEAIIKA GDGSFSLKTS KGTVEGFSHV MFATGRKPNT 370 380 390 400 410 420 KNLGLENVGV KMAKNGAIEV DEYSQTSVPS IWAVGDVTDR INLTPVALME GGALAKTLFQ 430 440 450 460 470 480 NEPTKPDYRA VPCAVFSQPP IGTVGLTEEQ AIEQYGDVDV YTSNFRPLKA TLSGLPDRVF 490 500 510 520 530 540 MKLIVCANTN KVLGVHMCGE DSPEIIQGFG VAVKAGLTKA DFDATVGVHP TAAEEFVTMR 550 560 APTRKFRKDS SEGKASPEAK TAAGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure and properties of glutathione reductase from Arabidopsis thaliana." Kubo A., Sano T., Saji H., Tanaka K., Kondo N., Tanaka K. Plant Cell Physiol. 34:1259-1266(1993) Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Columbia.
[2]	Kubo A. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D14049 mRNA. Translation: BAA03137.1. D89620 Genomic DNA. Translation: BAA19653.1. AL138650 Genomic DNA. Translation: CAB77586.1.
IPI	IPI00546267.
PIR	T47625.
RefSeq	NP_191026.1.
UniGene	At.21776
3D structure databases
HSSP	HSSP built from PDB template 1GER based on UniProtKB P06715.
ModBase	Search...
Proteomic databases
PRIDE	P42770.
Genome annotation databases
GeneID	824631.
GenomeReviews	Gene locus AT3G54660 in contig BA000014_GR.
KEGG	ath:AT3G54660.
Organism-specific databases
GeneFarm	2285. 251.
TAIR	At3g54660.
Phylogenomic databases
OMA	P42770. LHISFLE.
Enzyme and pathway databases
BRENDA	1.8.1.7. 302.
Gene expression databases
ArrayExpress	P42770.
GermOnline	AT3G54660. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006324. Glut_reduct_pln. 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.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01424. gluta_reduc_2. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHRP_ARATH

Accession

Primary (citable) accession number: P42770

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)