ID Q29FR6_DROPS Unreviewed; 490 AA.
AC Q29FR6; A0A6I8UF13;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Thioredoxin reductase 1, mitochondrial isoform X2 {ECO:0000313|RefSeq:XP_001354460.2};
GN Name=LOC4814288 {ECO:0000313|RefSeq:XP_001354460.2};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_001354460.2};
RN [1] {ECO:0000313|RefSeq:XP_001354460.2}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001354460.2};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_001354460.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_001354460.2; XM_001354424.4.
DR AlphaFoldDB; Q29FR6; -.
DR SMR; Q29FR6; -.
DR EnsemblMetazoa; FBtr0273687; FBpp0272125; FBgn0075294.
DR GeneID; 4814288; -.
DR KEGG; dpo:4814288; -.
DR eggNOG; KOG4716; Eukaryota.
DR HOGENOM; CLU_016755_2_4_1; -.
DR OMA; VHIIHHN; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0075294; Expressed in female reproductive system and 3 other cell types or tissues.
DR ExpressionAtlas; Q29FR6; baseline.
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 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:SF6; THIOREDOXIN REDUCTASE 2; 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:UP000001819}.
FT DOMAIN 10..341
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 361..472
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 463
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 193..200
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 325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 56..61
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 490 AA; 52947 MW; 8DC71A3E7912B5EC CRC64;
MAPVEGTYDY DLVVIGGGSA GLACAKEAVQ NGARVACLDY VKPTPIGTKW GVGGTCVNVG
CIPKKLMHQA SLLGEAVHEA AAYGWNVDDK IKPDWSKLVS SVQNHIKSVN WVTRVDLRDK
KVEYINGLGS FVDRHTMVAK LKSGDRTITA QTFVIAVGGR PRYPDIPGAV EYGITSDDLF
SLDHEPGKTL VVGAGYIGLE CAGFLKGLGY EPTVMVRSIV LRGFDQQMAE LVASSMDERG
IPFLRKTVPL SVTKQDNGKL LVKYKNTETG EEGEDTYDTV LWAVGRKGLV EDLNLSNAGV
TTFKDKIQVD TKEATNVANI FAVGDIIYGK PELTPVAVLA GRLLARRLYG GSNQRMDYSD
VATTVFTPLE YACVGLSEED AVKQHGADGV EVFHGYYKPT EFFIPQKSVR YCYLKAVAER
TGDQRVYGLH YLGPVAGEVI QGFAAALKSG LTINTLINTV GIHPTTAEEF TRLSITKRSG
LDPTPASCCS
//
