Reviewed, UniProtKB/Swiss-Prot Q6BIS1 (TRXB_DEBHA)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase
    EC=1.8.1.9

Gene names

Name:	TRR1
Ordered Locus Names:	DEHA2G08096g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer 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
Technical term	Complete proteome
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 – 321	321	Thioredoxin reductase		PRO_0000166763
Regions
	Nucleotide binding	33 – 45	13	FAD By similarity
	Nucleotide binding	288 – 297	10	FAD By similarity
Amino acid modifications
	Disulfide bond	142 ↔ 145		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BIS1-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: C7F763EF8ACA4B87	FASTA	321	34,975
	10 20 30 40 50 60 MVHHNVTIIG SGPAAHTAAI YLSRAEIKPT LYEGMLANGT AAGGQLTTTT DVENFPGFPK 70 80 90 100 110 120 GINGTELMDQ MREQSVRFGT DIITETISKC DLSSRPFKLW TEWNEDSEPI TTDAVVIATG 130 140 150 160 170 180 ASAKRMHLPG EDTYWQQGIS ACAVCDGAVP IFRNKPLAVV GGGDSACEEA LFLTKYGSKV 190 200 210 220 230 240 YLLVRRDQLR ASNIMQKRVQ NNDKLEILWN SEAKEAKGDG KLLQNISVYN NKTKETKDLP 250 260 270 280 290 300 VNGLFYAIGH IPATQIFAKQ LETDDQNYIL TKPGTAETSI PGVFAAGDVQ DKRYRQAITS 310 320 AGTGCMAALD CEKFLSEEEA K

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382139 Genomic DNA. Translation: CAG90363.2. Different initiation.
RefSeq	XP_461900.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2904781.
KEGG	dha:DEHA0G08745g.
Phylogenomic databases
HOGENOM	Q6BIS1.
OMA	Q6BIS1. HLPGEDT.
Enzyme and pathway databases
BRENDA	1.8.1.9. 74267.
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_DEBHA

Accession

Primary (citable) accession number: Q6BIS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	August 16, 2004
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)