ID Q47K81_THEFY Unreviewed; 310 AA.
AC Q47K81;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN OrderedLocusNames=Tfu_3108 {ECO:0000313|EMBL:AAZ57141.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ57141.1};
RN [1] {ECO:0000313|EMBL:AAZ57141.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ57141.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000849,
CC ECO:0000256|RuleBase:RU003880};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003881};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|RuleBase:RU003880}.
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DR EMBL; CP000088; AAZ57141.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47K81; -.
DR STRING; 269800.Tfu_3108; -.
DR KEGG; tfu:Tfu_3108; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_11; -.
DR OrthoDB; 109585at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
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; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|RuleBase:RU003880};
KW Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW NADP {ECO:0000256|RuleBase:RU003881};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003880};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003880}.
FT DOMAIN 6..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 310 AA; 33603 MW; 064D61C2FA55FC4B CRC64;
MSDVRNVIII GSGPAGYTAA IYAARAELKP LVFEGAITAG GALMNTTEVE NFPGFPDGIM
GPELMDNMRK QAERFGAELV PEDVTEVDLT ANPKVVKAGD QTFYARAVIV ATGSGYRKLG
VPGEEEFSGR GTSWCATCDG FFFRDQDIAV VGGGDSAMEE AIFLTRFARS VTVIHRRDQL
RASKIMQERA FANEKISFLW NTEVVEILGD TRVHAVRLRN RVTGEESTLN ISGLFIAIGH
DPRVELFKGQ LELDEQGYLK VDSPTTHTNI PGVFACGDVV DHRYRQAITA AGSGCAAALD
AERYLTEEAG
//
