Reviewed, UniProtKB/Swiss-Prot Q8T6Z1 (TRXB_SPIBA)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase
    EC=1.8.1.9
Alternative name(s):
    L-TrxR

Gene names

Name:

TRXB

Organism

Spironucleus barkhanus

Taxonomic identifier

103874 [NCBI]

Taxonomic lineage

Eukaryota › Diplomonadida › Hexamitidae › Hexamitinae › Spironucleus

Protein attributes

Sequence length	305 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm 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
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW removal of superoxide radicals Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD 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 – 305	›305	Thioredoxin reductase		PRO_0000166760
Regions
	Nucleotide binding	28 – 35	8	FAD By similarity
	Nucleotide binding	272 – 281	10	FAD By similarity
Amino acid modifications
	Disulfide bond	129 ↔ 132		Redox-active By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q8T6Z1-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 7C4DCE73A0626A20	FASTA	305	32,907
	10 20 30 40 50 60 LVIVGGGPGG LAAAIYAGRA GLTPVIFLGI ETSSQLMTTT EVENYPGFKT IQGPDLVQNQ 70 80 90 100 110 120 VDQAEHCGAQ LFYEDVTKID ATARPFKITH GYENEIMTCD ALIFATGSTA QRLDVIGEKQ 130 140 150 160 170 180 FWQKGVSACA VCDSMMAKNK DTVVVGGGDV ACEEASYLSN IASKVYLILR RDAFRASAAM 190 200 210 220 230 240 VQRVKSNPKI EIIYNSAVQE IKGETRVNQI LVKNLKSGDI TPLKVEALFW CIGHTPQTRL 250 260 270 280 290 300 LKGQVKMSEN GYILVENQTQ YTNVPGIFAA GDCCDWIYRQ AIVAAGSGCK AALDAERWLA SNGGH

References

[1]	"The diversity and evolution of thioredoxin reductase: new perspectives." Hirt R.P., Mueller S., Embley T.M., Coombs G.H. Trends Parasitol. 18:302-308(2002) [PubMed: 12379950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF394238 mRNA. Translation: AAM00424.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.9. 291207.
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.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01292. TRX_reduct. 1 hit.
PROSITE	PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXB_SPIBA

Accession

Primary (citable) accession number: Q8T6Z1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)