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Database: UniProt
Entry: L9KQG1_TUPCH
LinkDB: L9KQG1_TUPCH
Original site: L9KQG1_TUPCH 
ID   L9KQG1_TUPCH            Unreviewed;       632 AA.
AC   L9KQG1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Thioredoxin reductase 2, mitochondrial {ECO:0000313|EMBL:ELW64714.1};
GN   ORFNames=TREES_T100000637 {ECO:0000313|EMBL:ELW64714.1};
OS   Tupaia chinensis (Chinese tree shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW64714.1, ECO:0000313|Proteomes:UP000011518};
RN   [1] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang G., Fan Y., Yao Y., Huang Z.;
RT   "Genome of the Chinese tree shrew, a rising model animal genetically
RT   related to primates.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23385571; DOI=10.1038/ncomms2416;
RA   Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA   Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA   Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA   Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA   Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT   "Genome of the Chinese tree shrew.";
RL   Nat. Commun. 4:1426-1426(2013).
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   EMBL; KB320718; ELW64714.1; -; Genomic_DNA.
DR   AlphaFoldDB; L9KQG1; -.
DR   STRING; 246437.L9KQG1; -.
DR   eggNOG; KOG4716; Eukaryota.
DR   InParanoid; L9KQG1; -.
DR   Proteomes; UP000011518; 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; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF3; THIOREDOXIN-DISULFIDE REDUCTASE; 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; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000011518}.
FT   DOMAIN          54..222
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          359..493
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          507..616
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   632 AA;  68250 MW;  F6F9E9B4F1C311BA CRC64;
     MTSSNSQQLR VIQMLDSWME HLPPSGQGQQ NYDLLVIGGG SGGLACAKEG QQNYDLLVIG
     GGSGGLACAK EAAQLGRKVA VVDYVEPSPR GTRWGLGGTC VNVGCIPKKL MHQAALLGGW
     IRDAHHYGWE VAQPVLHDWK KMAEAVQNHV KSLNWGHRVQ LQDRKVKYLN VKASFVSEHT
     VRGVARDGKE TLLSADHIVI ATGGRPRYPT HVEGALEHGI TSDDVFWLKE SPGKTRWPGL
     GTLVTVEGTP KDPQFFALGL GVAFQPGRFK SVLLTAPEAQ RPQGSTLLRA DESPALPAAT
     CHHCHEAPHR PEQLCLWGVA LHPGTACLHS ARSAGERVAG GPPGGHGSHV SVSFSLTDVA
     LECAGFLTGI GLDTTVMMRS IPLRGFDQQM SSLVTESMAS HGTRFLRRCT PSRVRKLADG
     RLQVAWQDHA AGKEDTGTFD TVLWAIGRAP ETRSLNLEKA GVNTNPESQK ILVDAREATS
     VPHVYAIGDV AERLFGQSTD LMDYDNVPTT VFTPLEYGCV GLSEEEAVAR HGQEHVYHAY
     YKPLEFTVAE RDASQCYIKM VCLREPPQLV LGLHFLGPNA GEVTQGFAVG IKCGASYAQV
     MQTVGIHPTC SEEVVKLRIS KRSGLDPTVT GC
//
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