Reviewed, UniProtKB/Swiss-Prot Q25861 (TRXR_PLAF5)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase
      Short name=TrxR
    EC=1.8.1.9

Gene names

Name:	TR
Synonyms:	GR

Organism

Plasmodium falciparum (isolate FCH-5)

Taxonomic identifier

132416 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer.
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.
Caution	Was originally (Ref.1) thought to be a glutathione reductase.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro thioredoxin-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 – 541	541	Thioredoxin reductase		PRO_0000067986
Regions
	Nucleotide binding	71 – 88	18	FAD By similarity
Sites
	Active site	509	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	88 ↔ 93		Redox-active By similarity
Experimental info
	Sequence conflict	49 – 51	3	GGP → AGS in CAA58583. Ref.2
	Sequence conflict	512 – 517	6	DAESFM → AAEELS Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q25861-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5449D50D7BA5BD9D	FASTA	541	59,686
	10 20 30 40 50 60 MCKDKNEKKN YEHVNANEKN GYLASEKNEL TKNKVEEHTY DYDYVVIGGG PGGMASAKEA 70 80 90 100 110 120 AAHGARVLLF DYVKPSSQGT KWGIGGTCVN VGCVPKKLMH YAGHMGSIFK LDSKAYGWKF 130 140 150 160 170 180 DNLKHDWKKL VTTVQSHIRS LNFSYMTGLR SSKVKYINGL AKLKDKNTVS YYLKGDLSKE 190 200 210 220 230 240 ETVTGKYILI ATGCRPHIPD DVEGAKELSI TSDDIFSLKK DPGKTLVVGA SYVALECSGF 250 260 270 280 290 300 LNSLGYDVTV AVRSIVLRGF DQQCAVKVKL YMEEQGVMFK NGILPKKLTK MDDKILVEFS 310 320 330 340 350 360 DKTSELYDTV LYAIGRKGDI DGLNLESLNM NVNKSNNKII ADHLSCTNIP SIFAVGDVAE 370 380 390 400 410 420 NVPELAPVAI KAGEILARRL FKDSDEIMDY SYIPTSIYTP IEYGACGYSE EKAYELYGKS 430 440 450 460 470 480 NVEVFLQEFN NLEISAVHRQ KHIRAQKDEY DLDVSSTCLA KLVCLKNEDN RVIGFHYVGP 490 500 510 520 530 540 NAGEVTQGMA LALRLKVKKK DFDNCIGIHP TDAESFMNLF VTISSGLSYA AKGGCGGGKC G

References

[1]	"Plasmodium falciparum glutathione reductase exhibits sequence similarities with the human host enzyme in the core structure but differs at the ligand-binding sites." Mueller S., Becker K., Bergmann B., Schirmer R.H., Walter R.D. Mol. Biochem. Parasitol. 74:11-18(1995) [PubMed: 8719241] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Recombinant putative glutathione reductase of Plasmodium falciparum exhibits thioredoxin reductase activity." Mueller S., Gilberger T.-W., Faerber P.M., Becker K., Schirmer R.H., Walter R.D. Mol. Biochem. Parasitol. 80:215-219(1996) [PubMed: 8892299] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 47-517, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X87095 mRNA. Translation: CAA60574.1. X83603 Genomic DNA. Translation: CAA58583.1.
PIR	S57658.
3D structure databases
HSSP	HSSP built from PDB template 1ONF based on UniProtKB Q94655.
ModBase	Search...
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR006338. Thioredoxin/glutathione_Rdtase. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF23. Reduct_Se. 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. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXR_PLAF5

Accession

Primary (citable) accession number: Q25861
Secondary accession number(s): Q25864

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	September 22, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)