ID A0A091EW42_CORBR Unreviewed; 453 AA.
AC A0A091EW42;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000256|ARBA:ARBA00044068};
DE EC=1.11.1.2 {ECO:0000256|ARBA:ARBA00044049};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
DE AltName: Full=Peroxidase TXNRD1 {ECO:0000256|ARBA:ARBA00044275};
DE AltName: Full=Thioredoxin reductase TR1 {ECO:0000256|ARBA:ARBA00044212};
DE Flags: Fragment;
GN ORFNames=N302_12628 {ECO:0000313|EMBL:KFO61206.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO61206.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO61206.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO61206.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + NADPH = 2 H2O + NADP(+); Xref=Rhea:RHEA:15173,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.11.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043653};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174;
CC Evidence={ECO:0000256|ARBA:ARBA00043653};
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:ARBA00029303};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000256|ARBA:ARBA00029303};
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; KK719069; KFO61206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EW42; -.
DR STRING; 85066.A0A091EW42; -.
DR Proteomes; UP000052976; 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:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0010035; P:response to inorganic substance; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProt.
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:UP000052976};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933}.
FT DOMAIN 2..319
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 339..447
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 441
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 104
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 169..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 31..36
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO61206.1"
FT NON_TER 453
FT /evidence="ECO:0000313|EMBL:KFO61206.1"
SQ SEQUENCE 453 AA; 50001 MW; 00084898993086B5 CRC64;
QEAAKYEKKV MVLDFVTPTP QGSSWGLGGT CVNVGCIPKK LMHQAALLGQ ALQDSRKFGW
QLTEEVKHNW MTMTESVQNY IGSLNWGYRV ALRDTKVTYE NAYGEFVGPH TIKATNKKGI
EKLYTAERFI IATGERPRYL GIPGDKEYCI SSDDLFSLPY CPGKTLVVGA SYVALECAGF
LAGLGLDVTV MVRSILLRGF DQDMANKIGE YMKEHGVNFI REFVPIKVEE GTPGILKVTA
KSTTGNQMIE GEYNTVLLAI GRDPCTRKIG LDKVGVNINE KTGKIPVNDE EQTNVPHIYA
VGDILQGKLE LTPVAIQAGR LLVRRLYAGE TTKCDYVNVP TTVFTPLEYG ACGYSEETAV
EKFGEENIEV YHSHFWPLEW TVPSRDNNKC YAKIICNIQD NERVIGFHVL GPNAGEVTQG
FAAAIKCGLT KEQLDSTIGI HPVCAEVCIQ GHL
//
