Reviewed, UniProtKB/Swiss-Prot Q54UU8 (TRXB_DICDI)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase
    EC=1.8.1.9

Gene names

Name:	trrA
ORF Names:	DDB_G0280815

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from direct assay. Source: dictyBase culmination during sorocarp development Inferred from mutant phenotype. Source: dictyBase oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phagocytosis Inferred from mutant phenotype. Source: dictyBase removal of superoxide radicals Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro membrane fraction Inferred from direct assay. Source: dictyBase
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activity Inferred from direct assay. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 319	319	Thioredoxin reductase		PRO_0000318657
Regions
	Nucleotide binding	36 – 48	13	FAD By similarity
	Nucleotide binding	289 – 298	10	FAD By similarity
Amino acid modifications
	Disulfide bond	144 ↔ 147		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54UU8-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: A03B2A592B189957	FASTA	319	34,208
	10 20 30 40 50 60 MSTEKIQKVV IIGSGPAGHT AGIYAGRARL EPLMFEGFMA GGVAAGGQLT TTTEIENFPG 70 80 90 100 110 120 FPIDISGSEL MDKMREQNIK CGTTIETKTI SKVDLKQRPF TIYVEDEEDK PIKAQSIIIA 130 140 150 160 170 180 TGATAKRMGV PGETEFWSKG VSACAVCDGA LPIYRNKHLV VVGGGDTAAE EATFLTHFAS 190 200 210 220 230 240 KVTLLVRRNV MRASKAMQQK VFSNPKIEVL WDTTLVEIKG EKSVTSVGIY NSETKVSSNL 250 260 270 280 290 300 DAQGLFYAIG HTPNSAFLNG QLNTDETGYI ITQPGSTKTN VEGVFACGDV QDKVYRQAIT 310 AAGNGCMAAL DCERFLSSL

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000038 Genomic DNA. Translation: EAL67065.1.
RefSeq	XP_641039.1.
3D structure databases
HSSP	HSSP built from PDB template 1VDC based on UniProtKB Q39243.
SMR	Q54UU8. Positions 5-317.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54UU8.
Genome annotation databases
GeneID	8622741.
KEGG	ddi:DDB_0231235.
Organism-specific databases
dictyBase	DDB_G0280815. trrA.
Phylogenomic databases
eggNOG	KOG0404.
HOGENOM	HBG669726.
OMA	GTEIITE.
PhylomeDB	Q54UU8.
Enzyme and pathway databases
BRENDA	1.8.1.9. 424.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR005982. Thioredox_Rdtase. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00469. PNDRDTASEII.
TIGRFAMs	TIGR01292. TRX_reduct. 1 hit.
PROSITE	PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXB_DICDI

Accession

Primary (citable) accession number: Q54UU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)