ID A0A091E649_FUKDA Unreviewed; 410 AA.
AC A0A091E649;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=glutathione-disulfide reductase {ECO:0000256|ARBA:ARBA00012607};
DE EC=1.8.1.7 {ECO:0000256|ARBA:ARBA00012607};
GN ORFNames=H920_00426 {ECO:0000313|EMBL:KFO38188.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO38188.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO38188.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO38188.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN120606; KFO38188.1; -; Genomic_DNA.
DR RefSeq; XP_010620408.1; XM_010622106.2.
DR AlphaFoldDB; A0A091E649; -.
DR STRING; 885580.ENSFDAP00000005506; -.
DR Ensembl; ENSFDAT00000018916; ENSFDAP00000005506; ENSFDAG00000014494.
DR GeneID; 104860819; -.
DR CTD; 2936; -.
DR eggNOG; KOG0405; Eukaryota.
DR OMA; MSKHYDY; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR006322; Glutathione_Rdtase_euk/bac.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR NCBIfam; TIGR01421; gluta_reduc_1; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF5; GLUTATHIONE REDUCTASE, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 32..278
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 299..409
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 410 AA; 45071 MW; 70DCAED6BFA9E27C CRC64;
MWNTAVHSEF IHDHADYGFQ SCESKFNWRV IKEKRDAYVS RLNTVYQNNL TRSNIEIIHG
YATFTSDPQP TVEVNGKKYT APHILIATGG VPSLPLESQI PGASLGITSD GFFQLEELPR
RSVIVGAGYI AVEIAGIFSA LGCKTMLMIR HDKVLRNFDS LISSNCTEEL ENAGVEVLKY
SQVKEVKKTS TGLELSVVTA IPGRKPTLTS ILDVDCLLWA IGRHPNSKGL NLDRLGIQTD
EKGHIIVDKF QNTSVKGIYA VGDVCGKALL TPVAIAAGRK LAHRLFECKE DSKLDYDNIP
TVVFSHPPIG TVGLTEDEAI HKFGKDNVKI YSTAFTPMYH AVTTRKTKCV MKMICANREE
KVVGIHMQGI GCDEMLQGFA VAVKMGATKA DFDNTVAIHP TSSEELVTLR
//
