[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8774709 [NCBI, ExPASy, EBI, Israel, Japan] Faerber P.M., Becker K., Mueller S.; "Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum."; Eur. J. Biochem. 239:655-661(1996).
[2]	PROTEIN SEQUENCE OF 2-16, AND CHARACTERIZATION. PubMed=8631352 [NCBI, ExPASy, EBI, Israel, Japan] Krauth-Siegel R.L., Muller J.G., Lottspeich F., Schirmer R.H.; "Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria."; Eur. J. Biochem. 235:345-350(1996).

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).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X93462; CAA63747.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1ONF; X-ray; 2.60 A; A=1-500.

[ExPASy / RCSB / EBI]

PDBsum

1ONF; -.

ModBase

Q94655.

Ontologies

GO:0004362;	Molecular function: glutathione-disulfide reductase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 500`	`499`	`Glutathione reductase.`	`PRO_0000067959`
`NP_BIND`	`32 40`	`9`	`FAD (By similarity).`
`ACT_SITE`	`485 485`		`Proton acceptor (By similarity).`
`DISULFID`	`40 45`		`Redox-active (By similarity).`
`STRAND`	`3 8`	`6`
`HELIX`	`12 23`	`12`
`STRAND`	`28 35`	`8`
`HELIX`	`38 42`	`5`
`HELIX`	`45 63`	`19`
`HELIX`	`64 67`	`4`
`STRAND`	`69 75`	`7`
`HELIX`	`77 101`	`25`
`STRAND`	`105 109`	`5`
`STRAND`	`142 147`	`6`
`HELIX`	`161 163`	`3`
`HELIX`	`167 170`	`4`
`STRAND`	`177 182`	`6`
`HELIX`	`186 196`	`11`
`TURN`	`197 199`	`3`
`STRAND`	`201 205`	`5`
`STRAND`	`207 211`	`5`
`HELIX`	`217 229`	`13`
`STRAND`	`233 235`	`3`
`STRAND`	`240 247`	`8`
`STRAND`	`251 255`	`5`
`STRAND`	`260 269`	`10`
`TURN`	`276 279`	`4`
`TURN`	`283 286`	`4`
`STRAND`	`289 292`	`4`
`STRAND`	`294 296`	`3`
`STRAND`	`303 309`	`7`
`STRAND`	`314 316`	`3`
`HELIX`	`354 369`	`16`
`STRAND`	`383 385`	`3`
`STRAND`	`391 395`	`5`
`HELIX`	`398 404`	`7`
`HELIX`	`407 409`	`3`
`STRAND`	`410 417`	`8`
`HELIX`	`420 422`	`3`
`HELIX`	`429 431`	`3`
`STRAND`	`435 442`	`8`
`TURN`	`443 446`	`4`
`STRAND`	`447 455`	`9`
`HELIX`	`458 470`	`13`
`HELIX`	`475 479`	`5`
`HELIX`	`491 494`	`4`

Sequence information

Length: 500 AA [This is the length of the unprocessed precursor]

Molecular weight: 56561 Da [This is the MW of the unprocessed precursor]

CRC64: AB2299144002FCD3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVYDLIVIGG GSGGMAAARR AARHNAKVAL VEKSRLGGTC VNVGCVPKKI MFNAASVHDI 

        70         80         90        100        110        120 
LENSRHYGFD TKFSFNLPLL VERRDKYIQR LNNIYRQNLS KDKVDLYEGT ASFLSENRIL 

       130        140        150        160        170        180 
IKGTKDNNNK DNGPLNEEIL EGRNILIAVG NKPVFPPVKG IENTISSDEF FNIKESKKIG 

       190        200        210        220        230        240 
IVGSGYIAVE LINVIKRLGI DSYIFARGNR ILRKFDESVI NVLENDMKKN NINIVTFADV 

       250        260        270        280        290        300 
VEIKKVSDKN LSIHLSDGRI YEHFDHVIYC VGRSPDTENL KLEKLNVETN NNYIVVDENQ 

       310        320        330        340        350        360 
RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEERYLNKK ENVTEDIFYN VQLTPVAINA 

       370        380        390        400        410        420 
GRLLADRLFL KKTRKTNYKL IPTVIFSHPP IGTIGLSEEA AIQIYGKENV KIYESKFTNL 

       430        440        450        460        470        480 
FFSVYDIEPE LKEKTYLKLV CVGKDELIKG LHIIGLNADE IVQGFAVALK MNATKKDFDE 

       490        500 
TIPIHPTAAE EFLTLQPWMK

Q94655 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools