GenomeNet

Database: UniProt
Entry: Q6FR39
LinkDB: Q6FR39
Original site: Q6FR39 
ID   TRXB_CANGA              Reviewed;         319 AA.
AC   Q6FR39;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   20-JAN-2016, entry version 77.
DE   RecName: Full=Thioredoxin reductase;
DE            EC=1.8.1.9;
GN   Name=TRR1; OrderedLocusNames=CAGL0I01166g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
CC       + NADPH.
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: Cytoplasm {ECO:0000250|UniProtKB:P29509}.
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}.
DR   EMBL; CR380955; CAG60242.1; -; Genomic_DNA.
DR   RefSeq; XP_447305.1; XM_447305.1.
DR   ProteinModelPortal; Q6FR39; -.
DR   SMR; Q6FR39; 2-318.
DR   STRING; 284593.XP_447305.1; -.
DR   PRIDE; Q6FR39; -.
DR   EnsemblFungi; CAG60242; CAG60242; CAGL0I01166g.
DR   GeneID; 2889334; -.
DR   KEGG; cgr:CAGL0I01166g; -.
DR   CGD; CAL0132754; TRR1.
DR   EuPathDB; FungiDB:CAGL0I01166g; -.
DR   eggNOG; KOG0404; Eukaryota.
DR   eggNOG; COG0492; LUCA.
DR   InParanoid; Q6FR39; -.
DR   KO; K00384; -.
DR   OMA; TDSGQVW; -.
DR   OrthoDB; EOG7DC2FH; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN         1    319       Thioredoxin reductase.
FT                                /FTId=PRO_0000166762.
FT   NP_BIND      11     14       FAD. {ECO:0000250|UniProtKB:P29509}.
FT   NP_BIND      40     41       FAD. {ECO:0000250|UniProtKB:P29509}.
FT   NP_BIND     295    297       FAD. {ECO:0000250|UniProtKB:P29509}.
FT   BINDING      45     45       FAD; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P29509}.
FT   BINDING      54     54       FAD. {ECO:0000250|UniProtKB:P29509}.
FT   BINDING     145    145       FAD. {ECO:0000250|UniProtKB:P29509}.
FT   BINDING     288    288       FAD. {ECO:0000250|UniProtKB:P29509}.
FT   DISULFID    142    145       Redox-active.
FT                                {ECO:0000250|UniProtKB:P29509}.
SQ   SEQUENCE   319 AA;  34386 MW;  9E9919E212B08345 CRC64;
     MNHKKVVIIG SGPAAHTAAI YLARAEIKPT MYEGMLANGI AAGGQLTTTT EIENFPGFPD
     GMTGSELMDR MRAQSTKFGT EIITETIAKV DLSSRPFKLW TEFNEDGEPI TTDAIVIATG
     ASAKRLHIPG EETYWQQGIS ACAVCDGAVP IFRNKPLAVI GGGDSACEEA QFLTKYGSKV
     YLIVRKDHLR ASTIMQRRAE QNDKIEILYN TVTLEAQGDG KLLNNLRIKN VKTNEETDLP
     VNGLFYAIGH TPATKIVEGQ VETDETGYIK TIPGSSLTSV PGVFAAGDVQ DSKYRQAITS
     AGSGCMAGLD AEKYLTELE
//
DBGET integrated database retrieval system