GenomeNet

Database: UniProt
Entry: A0A369SK52_9METZ
LinkDB: A0A369SK52_9METZ
Original site: A0A369SK52_9METZ 
ID   A0A369SK52_9METZ        Unreviewed;       592 AA.
AC   A0A369SK52;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000313|EMBL:RDD47277.1};
GN   ORFNames=TrispH2_000181 {ECO:0000313|EMBL:RDD47277.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD47277.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD47277.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD47277.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD47277.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
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}.
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:RDD47277.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NOWV01000004; RDD47277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369SK52; -.
DR   STRING; 287889.A0A369SK52; -.
DR   Proteomes; UP000253843; 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: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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR   NCBIfam; TIGR01438; TGR; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF3; THIOREDOXIN-DISULFIDE REDUCTASE; 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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000253843}.
FT   DOMAIN          110..446
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          466..576
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        567
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         165
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         294..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         390
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         430
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        156..161
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   592 AA;  64905 MW;  DF1191C71F7442B8 CRC64;
     MATELPSPIR TYVKENTIVV IGKTDCSKTQ TLVNFLRLRN ITDNVARVNV DTLDYNVDEL
     QAALQKSSGI ATLPILYCKG TLIGDFEASK ESILYGQISQ QLTMHSEYSY DLIVVGGGSG
     GLACSKEAAE QGLTVALLDF VKPTPLGCSW GLGGTCVNVG CIPKKLMHQA SLLGESIHDA
     SHYGWEINEN CSHSWEKMKD NVQNHIGSIN FGYRVQLRDR KVKYLNAYGT LVDPHTIKAV
     DRRGKETLLT AKNFVISSGC RPRYPDIPGA KEHCVTSDDL FSLEKCPGKT LVIGASYVAL
     ECAGFLAGLG LDVTVMVRSI LLRGFDQDMA ERVGKYMKDI GIKFIRPAVP LSVEAITMND
     GKKVLNVNYT MLDNGNKAQD KFDTVLLAIG RDPCTVNIGL DNAGVVVEKN GYIKTVNEQT
     NVPSIYGIGD ILYDKPELTP VAIHAGRLLA KRLSGVSTQQ CDYDSIPTTI FTPLEYSCCG
     LSEEVAIEKL GDDVEVYHAQ FMPLEWTIPH RDENSCYLKL ICNKRDQERV IGIHILGPNS
     GEVMQGFATA MKCGATKAHF DDTVGIHPTN AEWFTTLRIT RRSGQDVKVT GC
//
DBGET integrated database retrieval system