TRXB_KLULA
ID TRXB_KLULA Reviewed; 349 AA.
AC Q6HA24; Q6CMB1;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Thioredoxin reductase, mitochondrial;
DE EC=1.8.1.9;
DE Flags: Precursor;
GN Name=TRR1; OrderedLocusNames=KLLA0E21692g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15157744; DOI=10.1016/j.bbaexp.2004.03.004;
RA Tarrio N., Diaz Prado S., Cerdan M.E., Gonzales Siso M.I.;
RT "Isolation and characterization of two nuclear genes encoding glutathione
RT and thioredoxin reductases from the yeast Kluyveromyces lactis.";
RL Biochim. Biophys. Acta 1678:170-175(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P29509};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P29509};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29509}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ504413; CAD43212.1; -; Genomic_DNA.
DR EMBL; CR382125; CAH00015.1; -; Genomic_DNA.
DR RefSeq; XP_454928.1; XM_454928.1.
DR AlphaFoldDB; Q6HA24; -.
DR SMR; Q6HA24; -.
DR STRING; 28985.XP_454928.1; -.
DR PRIDE; Q6HA24; -.
DR EnsemblFungi; CAH00015; CAH00015; KLLA0_E21605g.
DR GeneID; 2894621; -.
DR KEGG; kla:KLLA0_E21605g; -.
DR eggNOG; KOG0404; Eukaryota.
DR HOGENOM; CLU_031864_5_1_1; -.
DR InParanoid; Q6HA24; -.
DR OMA; VDNFPGY; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblFungi.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..349
FT /note="Thioredoxin reductase, mitochondrial"
FT /id="PRO_0000030302"
FT BINDING 41..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 70..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 75
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT BINDING 325..327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29509"
FT DISULFID 172..175
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P29509"
SQ SEQUENCE 349 AA; 38103 MW; DF1177B6AC372AEC CRC64;
MLLVRNSTLG RLSSLRGFFR NINESNIFYR MVHHKVTIIG SGPAAHTAAI YLARAEIKPT
LYEGFMANGI AAGGQLTTTT EIENFPGFPD GLTGSELMDR MKAQSIKFGT DVITETVSKV
DLSSRPFKFW TEFNEDQEPE TTDAIILSTG ASAKRLHLPG EETYWQQGIS ACAVCDGAVP
IFRNKPLAVI GGGDSACEEA QFLTKYGSKV YMLVRKDHLR ASQIMQRRAE QNEKIEILYN
HVTLEAKGDG KYLNALKVKN VKTNEEYDLP VNGLFYAIGH TPATNIVAGQ VDLDEAGYVK
TVPGSTLTNV PGVFAAGDVQ DARYRQAITS AGSGCMAALD AEKYITELE
