ID A0A0N4VDV8_ENTVE Unreviewed; 571 AA.
AC A0A0N4VDV8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000881801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000881801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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 AlphaFoldDB; A0A0N4VDV8; -.
DR WBParaSite; EVEC_0000881801-mRNA-1; EVEC_0000881801-mRNA-1; EVEC_0000881801.
DR Proteomes; UP000038041; Unplaced.
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 Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; 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 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; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 87..410
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 430..541
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 571 AA; 63809 MW; 989B5AD2618CAADA CRC64;
LQIDSIFSEL GEELHKVEVN KAVANFVLYV VDRDTFPLVF IKGDCVGGLC ELRLLEENGV
LRNWLSKHTY DLIVCDFHWS FLGGFMAAKY GKKVACLDFV KPSTQGTTWG LGGTCVNVGC
IPKKLMHRAS ILGEHINDAK KFGWEIDGEP KLDWCKMRNA VQDHVASLNW NYRVQLRENS
VTYINAYGKF VDSHTLEAKN KKGKVEMLTA DRFLLATGLR PRFPNVPGCL ECCISSDDLF
SLPYNPGKTL CVGASYISLE SAGFLKGIGN DVTVMVRSII LRGFDRDMAE RIQKHMLEIG
VKFINAVPFK YEKIKEPSVD KPGLIRVYTI NTLEDGSKQE VSEDFNTVLM AIGRDAVTDD
VGLDEIGVER APNKKIIGRH EQSKSCPYVY AVGDVLDGCL ELTPVARTAG KVLMRRLYTG
NCEMTEYDKV PTTVFTPLEY GSCGLSEETA KQRYGAENVN VYHGMFLPLE FTIPQRVENR
HCYLKLICVK SQNDRVVGLH ILSPDAGEIT QGFAIALKLD ATKADFDRLI GIHPTVAEVC
SHLLLRKKRL HFTVLVLFGW SDESPGLFGI I
//
