ID A0A0N4VB99_ENTVE Unreviewed; 124 AA.
AC A0A0N4VB99;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=EVEC_LOCUS7286 {ECO:0000313|EMBL:VDD92535.1};
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_0000780201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000780201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD92535.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001346};
CC -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC {ECO:0000256|ARBA:ARBA00025782}.
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DR EMBL; UXUI01008856; VDD92535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4VB99; -.
DR STRING; 51028.A0A0N4VB99; -.
DR WBParaSite; EVEC_0000780201-mRNA-1; EVEC_0000780201-mRNA-1; EVEC_0000780201.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR CDD; cd02964; TryX_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR PANTHER; PTHR13871:SF7; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000274131}.
FT DOMAIN 1..124
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 124 AA; 14399 MW; 84CDD9393E2E71CF CRC64;
MGKVVGVYFS AHWCPPCRMF TPVLKDFYEE ICDDGFEVVF ASFDHSEEEQ MNYIRSEHGD
WYYVPFGHPS IREAANKLDA NGIPALIIFK KNGEIVTKNG RSDVSVWSFI YCFAYWYSSE
LRSL
//
