Reviewed, UniProtKB/Swiss-Prot Q6FR39 (TRXB_CANGA)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase
    EC=1.8.1.9

Gene names

Name:	TRR1
Ordered Locus Names:	CAGL0I01166g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	319 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 – 319	319	Thioredoxin reductase		PRO_0000166762
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)
	Q6FR39-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 9E9919E212B08345	FASTA	319	34,386
	10 20 30 40 50 60 MNHKKVVIIG SGPAAHTAAI YLARAEIKPT MYEGMLANGI AAGGQLTTTT EIENFPGFPD 70 80 90 100 110 120 GMTGSELMDR MRAQSTKFGT EIITETIAKV DLSSRPFKLW TEFNEDGEPI TTDAIVIATG 130 140 150 160 170 180 ASAKRLHIPG EETYWQQGIS ACAVCDGAVP IFRNKPLAVI GGGDSACEEA QFLTKYGSKV 190 200 210 220 230 240 YLIVRKDHLR ASTIMQRRAE QNDKIEILYN TVTLEAQGDG KLLNNLRIKN VKTNEETDLP 250 260 270 280 290 300 VNGLFYAIGH TPATKIVEGQ VETDETGYIK TIPGSSLTSV PGVFAAGDVQ DSKYRQAITS 310 AGSGCMAGLD AEKYLTELE

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 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380955 Genomic DNA. Translation: CAG60242.1.
RefSeq	XP_447305.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2889334.
KEGG	cgr:CAGL0I01166g.
Phylogenomic databases
HOGENOM	Q6FR39.
OMA	Q6FR39. YRNREVA.
Enzyme and pathway databases
BRENDA	1.8.1.9. 189220.
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_CANGA

Accession

Primary (citable) accession number: Q6FR39

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	July 19, 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)