ID G7N5B1_MACMU Unreviewed; 621 AA.
AC G7N5B1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000256|ARBA:ARBA00044068};
DE EC=1.11.1.2 {ECO:0000256|ARBA:ARBA00044049};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
DE AltName: Full=Peroxidase TXNRD1 {ECO:0000256|ARBA:ARBA00044275};
DE AltName: Full=Thioredoxin reductase TR1 {ECO:0000256|ARBA:ARBA00044212};
DE Flags: Fragment;
GN ORFNames=EGK_04130 {ECO:0000313|EMBL:EHH21130.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH21130.1};
RN [1] {ECO:0000313|EMBL:EHH21130.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH21130.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + NADPH = 2 H2O + NADP(+); Xref=Rhea:RHEA:15173,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.11.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043653};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174;
CC Evidence={ECO:0000256|ARBA:ARBA00043653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00029303};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000256|ARBA:ARBA00029303};
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; CM001263; EHH21130.1; -; Genomic_DNA.
DR AlphaFoldDB; G7N5B1; -.
DR Proteomes; UP000013456; Chromosome 11.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
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; IPR002109; Glutaredoxin.
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 InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
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 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 Selenocysteine {ECO:0000256|ARBA:ARBA00022933}.
FT DOMAIN 38..98
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT DOMAIN 133..474
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 494..605
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH21130.1"
FT NON_TER 621
FT /evidence="ECO:0000313|EMBL:EHH21130.1"
SQ SEQUENCE 621 AA; 68187 MW; 33047ED50F9FF388 CRC64;
AKDHHPGKTL PENPAGFTST ATADLRALLQ AYIDGHSVVI FSRSTCTRCA EVKKLFKSLC
VPYFVLELDQ TEYGRALEGT LSELAAETDL PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK
MNGPEDLPES YDYDLIIIGG GSGGLAAAKA RLFEAAQYGK KVMVLDFVTP TPLGTRWGLG
GTCVNVGCIP KKLMHQAALL GQALQDSRNY GWKVEETVKH DWDRMIEAVQ NHIGSLNWGY
RVALREKKVV YENAYGQFIG PHRIKATNNK GKEKIYSAER FLIATGERPR YLGIPGDKEY
CISSDDLFSL PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMASKI
GEHMEEHGIK FIRQFVPIKI EQIEAGTPGR LRVVAQSTNS EEIIEGEYNT VLLAIGRDAC
TRKIGLETVG VKINEKTGKI PVTDEEQTNV PYIYAIGDIL EDKVELTPVA IQAGRLLAQR
LYAGSTVKCD YENVPTTVFT PLEYGACGLS EEKAVEKFGE ENIEVYHSYF WPLEWTIPSR
DNNKCYAKII CNTKDNERVV GFHVLGPNAG EVTQGFAAAL KCGLTKKQLD STIGIHPVCA
EVFTTLSVTK RSGASILQAG C
//
