ID Q23DC5_TETTS Unreviewed; 491 AA.
AC Q23DC5;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 3.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
GN ORFNames=TTHERM_00047660 {ECO:0000313|EMBL:EAR94708.3};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR94708.3, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; GG662712; EAR94708.3; -; Genomic_DNA.
DR RefSeq; XP_001014761.3; XM_001014761.4.
DR STRING; 312017.Q23DC5; -.
DR EnsemblProtists; EAR94708; EAR94708; TTHERM_00047660.
DR GeneID; 7839738; -.
DR KEGG; tet:TTHERM_00047660; -.
DR eggNOG; KOG4716; Eukaryota.
DR HOGENOM; CLU_016755_2_4_1; -.
DR InParanoid; Q23DC5; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Selenium {ECO:0000313|EMBL:EAR94708.3};
KW Selenocysteine {ECO:0000313|EMBL:EAR94708.3}.
FT DOMAIN 7..342
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 362..474
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 192..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT NON_STD 490
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:EAR94708.3"
FT DISULFID 53..58
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 491 AA; 54090 MW; 72B660D8FC19C201 CRC64;
MDVEFKYDFF VIGGGSGGLA AAKEAASFGA RVAVADFVKP SPVGTKWGLG GTCVNVGCIP
KKLMHFAASY GESHEAQKNM GWTEIKEKNK HEWQPMVERV QAHIKKLNWG YKVELAEKEV
KYYNSLASIV GKNTIELTNR KGEKEQVTAK YILIAVGGRP TFLDIPNTEK LVITSDDIFS
MQNPPGKTLV VGASYIALEC AGFLAGFGYD VTVMVRSILL RGFDQEIAEK IGEYMARHGT
KFIRGTVPHH IEATPDGRRR VVWKSPVEGQ GDVEEIFDTV MLAIGRTSDT KNIGVETMGI
KTKPNGKIIA NDDDTTNVEN IFAIGDCVDK RPELTPTAIK AGRLLARRLF NGDTKLMDYN
SIPTTVFTPI EYGTIGLSEE DAKTKYGEDN IKVYYSIFTP LDWSYSDHKH DDKGHAKLIV
NKADDERVVG FHYLGPHAGE VTQGFAIAFK FKATKANFDD VVGIHPTYAE EFTTLKNVKG
EGEAQESGCU G
//
