Reviewed, UniProtKB/Swiss-Prot Q6HA24 (TRXB_KLULA)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase, mitochondrial
    EC=1.8.1.9

Gene names

Name:	TRR1
Ordered Locus Names:	KLLA0E21692g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Mitochondrion Potential.
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	Mitochondrion
Domain	Redox-active center Transit peptide
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	mitochondrion 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
	Transit peptide	1 – 30	30	Mitochondrion Potential
	Chain	31 – 349	319	Thioredoxin reductase, mitochondrial		PRO_0000030302
Regions
	Nucleotide binding	63 – 75	13	FAD By similarity
	Nucleotide binding	318 – 327	10	FAD By similarity
Amino acid modifications
	Disulfide bond	172 ↔ 175		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HA24-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: DF1177B6AC372AEC	FASTA	349	38,103
	10 20 30 40 50 60 MLLVRNSTLG RLSSLRGFFR NINESNIFYR MVHHKVTIIG SGPAAHTAAI YLARAEIKPT 70 80 90 100 110 120 LYEGFMANGI AAGGQLTTTT EIENFPGFPD GLTGSELMDR MKAQSIKFGT DVITETVSKV 130 140 150 160 170 180 DLSSRPFKFW TEFNEDQEPE TTDAIILSTG ASAKRLHLPG EETYWQQGIS ACAVCDGAVP 190 200 210 220 230 240 IFRNKPLAVI GGGDSACEEA QFLTKYGSKV YMLVRKDHLR ASQIMQRRAE QNEKIEILYN 250 260 270 280 290 300 HVTLEAKGDG KYLNALKVKN VKTNEEYDLP VNGLFYAIGH TPATNIVAGQ VDLDEAGYVK 310 320 330 340 TVPGSTLTNV PGVFAAGDVQ DARYRQAITS AGSGCMAALD AEKYITELE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two nuclear genes encoding glutathione and thioredoxin reductases from the yeast Kluyveromyces lactis." Tarrio N., Diaz Prado S., Cerdan M.E., Gonzales Siso M.I. Biochim. Biophys. Acta 1678:170-175(2004) [PubMed: 15157744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ504413 Genomic DNA. Translation: CAD43212.1. CR382125 Genomic DNA. Translation: CAH00015.1.
RefSeq	XP_454928.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2894621.
KEGG	kla:KLLA0E21692g.
Phylogenomic databases
HOGENOM	Q6HA24.
OMA	Q6HA24. HLPGEDT.
Enzyme and pathway databases
BRENDA	1.8.1.9. 74088.
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_KLULA

Accession

Primary (citable) accession number: Q6HA24
Secondary accession number(s): Q6CMB1

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)