ID A0A0B2V4T4_TOXCA Unreviewed; 652 AA.
AC A0A0B2V4T4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
GN Name=trxr-1 {ECO:0000313|EMBL:KHN78441.1};
GN ORFNames=Tcan_02846 {ECO:0000313|EMBL:KHN78441.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN78441.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN78441.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN78441.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN78441.1}.
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DR EMBL; JPKZ01002099; KHN78441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2V4T4; -.
DR STRING; 6265.A0A0B2V4T4; -.
DR OMA; HPTCGEI; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1.
DR Pfam; PF07992; Pyr_redox_2; 2.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT DOMAIN 105..273
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 281..504
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 524..636
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 652 AA; 72147 MW; E87E7D7798FDBB2E CRC64;
MAPTTSPGSS AAERVFKEAS EKRAVVVYTD RDAELQKITD MLTKRNETVE LLKISRVAAK
NVLNVVQRDN VPLIFIKGDC VGGLVDLLKL EESGALDEWL KQHKYDIVVV GGGSGGLAAA
KEAARLGKKV LCLDFVKPSV MGTAWGLGGT CVNVGCIPKK LMHQTALLGE YIEDAKKYGW
EIPKGDVKLK WEKMKNAVQD HIASLNWGYR VQLRERMVTY LNAYGVFTGS HEMTTTTKKK
KVEKITADRF IIATGLRPRY PDVPGAKECC ITSHEVTYLN AYGVFTGSHE MTTTTKKKKV
EKITADRFII ATGLRPRYPD VPGAKECCIS SDDLFSLSYN PGKTLCVGAS YVSLECAGFL
RGIGNEVTVM VRSILLRGFD QDMAERIRKH MMTRGIEFIN AVPSKYERIE EPTDDKPGLV
RVSWEKTLEN GEKKIETKDF NTVLMAIGRD PVTNGMGLET ISVERTKSGK IVGRREQSTC
PYVYALGDVL DGCPELTPVA IQAGRVLMRR LITGNSELVE YDQVPTTVFT PLEYGCCGLA
EEAAIQKYGK ENINVYHNVF IPLEYTVPER VENSHCYCKI ICLKTEQDLV VGYHILAPNA
GEIVQGFAIA LKLKGKKADF DRLIGIHPTV AENFTTLTLL KEEGQELKAT GC
//
