Q43154 (GSHRP_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glutathione reductase, chloroplastic Short name=GR Short name=GRase EC=1.8.1.7
Organism	Spinacia oleracea (Spinach)
Taxonomic identifier	3562 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	489 AA.
Sequence status	Fragment.
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.
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
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	chloroplast 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
	Transit peptide	‹1 – 2	›2	Chloroplast Potential
	Chain	3 – 489	487	Glutathione reductase, chloroplastic		PRO_0000030283
Regions
	Nucleotide binding	54 – 63	10	FAD By similarity
Sites
	Active site	462	1	Proton acceptor By similarity
	Binding site	224	1	NADP By similarity
	Binding site	230	1	NADP By similarity
Amino acid modifications
	Disulfide bond	63 ↔ 68		Redox-active By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q43154 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 970FC5B079A72CCD	FASTA	489	52,611
	10 20 30 40 50 60 EDNHSTVEDD AANYDFDLFV IGAGSGGVRA ARFSANLGAK VGICELPFHP ISSEVIGGVG 70 80 90 100 110 120 GTCVIRGCVP KKILVYGASF GGELEDAKNY GWELNEKIDF NWKKLLQKKT DEIIRLNNIY 130 140 150 160 170 180 KRLLSNAGVK LYEGEGKIVG PNEVQVTQLD GTKLSYSAKH ILIATGSRAQ RPNIPGQELA 190 200 210 220 230 240 ITSDEALSLE EFPKRVVILG GGYISVEFAS IWRGMGADVN LCFRKELPLR GFDDEMRAAV 250 260 270 280 290 300 ARNLEGRGVN VHPRTTLTEL VKTDGGVVAR TDHGEEIEAD VVLFATGRSP NTKRLNLEAL 310 320 330 340 350 360 GVELDRTGAV KVDEYSRTSV PSIWAIGDVT NRMNLTPVAL MEGTCFAKTV FGGQNSKPDY 370 380 390 400 410 420 SNIACAVFSI PPLAVVGLSE EQAIEQASGD ILVFTSSFNP MKNTISGRQE KTIMKLVVDA 430 440 450 460 470 480 ETDKVLGASM CGPDAAEIMQ GIAIALKFGA TKAQFDSTVG IHPSAAEEFV TMREPSRRVP GAGKPKTNL

References

[1]	Aono M., Fujiyama K., Sano T., Tanaka K. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. New Asia. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D37870 mRNA. Translation: BAA07108.1.
PIR	T09151.
3D structure databases
ProteinModelPortal	Q43154.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006324. Glut-diS_reduct. 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]
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	TIGR01424. gluta_reduc_2. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHRP_SPIOL

Accession

Primary (citable) accession number: Q43154

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	March 6, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program