ID L5KP37_PTEAL Unreviewed; 636 AA.
AC L5KP37;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
GN ORFNames=PAL_GLEAN10003931 {ECO:0000313|EMBL:ELK13077.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13077.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(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; KB030631; ELK13077.1; -; Genomic_DNA.
DR RefSeq; XP_006911496.1; XM_006911434.2.
DR AlphaFoldDB; L5KP37; -.
DR STRING; 9402.L5KP37; -.
DR GeneID; 102894141; -.
DR KEGG; pale:102894141; -.
DR CTD; 114112; -.
DR eggNOG; KOG1752; Eukaryota.
DR eggNOG; KOG4716; Eukaryota.
DR InParanoid; L5KP37; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000010552; 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: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; IPR011899; Glutaredoxin_euk/vir.
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; TIGR02180; GRX_euk; 1.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF7; THIOREDOXIN REDUCTASE 3; 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 Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933}.
FT DOMAIN 63..124
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT DOMAIN 152..489
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 509..620
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 69678 MW; CA8FCC0B2F667B73 CRC64;
MSPGPVQVGA VSNRRPGSGR SAPMSSPPGR RARLWSSGTS RSAPEAREEL RRRLLGLIEG
NRVMIFSKSY CPHSTRVKEL FSSLGVECNI LELDQVDDGA SVQEVLSEIT NQRTVPNIFV
NKVHMGGCDR TFQAHQSGLL QKLLQEDSAY DYDLIVIGGG SGGLACAQEA AILGKKVMVL
DFVVPSPQGT SWGLGGTCVN VGCVPKKLMH QAALLGQALS DSRKFGWEYN QQVKHNWETM
TEAIQNHIGS LNWSYRLSLR EKAVAYVNSY GEFVEHHKIK ATNRKGQETC YTAAKFVIAT
GERPRYLGIQ GDKEYCITSD DLFSLPYCPG KTLVVGASYV ALECAGFLAG LGLDVTVMVR
SVLLRGFDQE MAERVGSYME QHGVKFLRKF IPVMVQQLEK GSPGKLKVVA KSTEGPETVE
GMYNTVLLAI GRDSSTRKIG LEKIGVKINE KNGKIPVNDM EQTNVPYVYA IGDILEGKLE
LTPVAIQAGK LLARRLFGGR LEKCDYINVP TTVFTPLEYG CCGLSEEKAI DEYKKENLEV
YHTLFWPLEW TVAGRDNNTC YAKIICNKLD NNLVIGFHIL GPNAGEITQG FAAAMKCGLT
KQLLDDTIGI HPTCGEILTT LEITKSSGLD ISQKGC
//
