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
//