Q94655 (GSHR_PLAFK) 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:

GR2

Organism

Plasmodium falciparum (isolate K1 / Thailand)

Taxonomic identifier

5839 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania) › Plasmodium falciparum

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
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	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 500

499

Glutathione reductase

PRO_0000067959

Regions

Nucleotide binding

32 – 40

9

FAD By similarity

Sites

Active site

485

1

Proton acceptor By similarity

Amino acid modifications

Disulfide bond

40 ↔ 45

Redox-active By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

500

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

12 – 23

12

Beta strand

28 – 35

8

Helix

38 – 42

5

Helix

45 – 63

19

Helix

64 – 67

4

Helix

77 – 101

25

Beta strand

105 – 109

5

Beta strand

142 – 147

6

Helix

161 – 163

3

Helix

167 – 170

4

Beta strand

177 – 182

6

Helix

186 – 196

11

Turn

197 – 199

3

Beta strand

201 – 205

5

Beta strand

207 – 211

5

Helix

217 – 229

13

Beta strand

233 – 235

3

Beta strand

240 – 247

8

Beta strand

251 – 255

5

Beta strand

260 – 269

10

Turn

276 – 279

4

Turn

283 – 286

4

Beta strand

289 – 292

4

Beta strand

294 – 296

3

Beta strand

303 – 309

7

Beta strand

314 – 316

3

Helix

354 – 369

16

Beta strand

383 – 385

3

Beta strand

391 – 395

5

Helix

398 – 404

7

Helix

407 – 409

3

Beta strand

410 – 417

8

Helix

420 – 422

3

Helix

429 – 431

3

Beta strand

435 – 442

8

Turn

443 – 446

4

Beta strand

447 – 455

9

Helix

458 – 470

13

Helix

475 – 479

5

Helix

491 – 494

4

Sequences

	Sequence		Length	Mass (Da)
	Q94655 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AB2299144002FCD3	FASTA	500	56,561
	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

References

[1]	"Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum." Faerber P.M., Becker K., Mueller S. Eur. J. Biochem. 239:655-661(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria." Krauth-Siegel R.L., Muller J.G., Lottspeich F., Schirmer R.H. Eur. J. Biochem. 235:345-350(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X93462 Genomic DNA. Translation: CAA63747.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ONF	X-ray	2.60	A	1-500	[»]

ProteinModelPortal

Q94655.

SMR

Q94655. Positions 2-496.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG1249.

Family and domain databases

Gene3D

3.30.390.30. 1 hit.

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
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.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1741261.

EvolutionaryTrace

Q94655.

Entry information

Entry name

GSHR_PLAFK

Accession

Primary (citable) accession number: Q94655

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)