ID X6MU02_RETFI Unreviewed; 287 AA.
AC X6MU02;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:ETO17443.1};
DE Flags: Fragment;
GN ORFNames=RFI_19876 {ECO:0000313|EMBL:ETO17443.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO17443.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO17443.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETO17443.1}.
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DR EMBL; ASPP01016607; ETO17443.1; -; Genomic_DNA.
DR AlphaFoldDB; X6MU02; -.
DR EnsemblProtists; ETO17443; ETO17443; RFI_19876.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000023152; 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: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; 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; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 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:UP000023152}.
FT DOMAIN 12..126
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 147..263
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETO17443.1"
SQ SEQUENCE 287 AA; 32165 MW; 8B006D62F995751D CRC64;
KKKKQRNGII RNLFDRLVQC GVHEALLHSG ADVITGADIA AIEKKEDLLL LKCQDKREFK
GYDCVIYAVG RGPLSTELGL EHTSVKQDKR GFIITNEWEE THQKGIYALG DVNNKVPLTP
VAIRAGRKWA DRVFGSIKDA KMEYDLVPSV IFSHPPIGTI GLTEEHVREQ VKNKKLPEPI
KIYETHFRDL KYGMYSNQSE KVMTHMKLVC VGKEEKIVGL HMIGDGCDES LQGFAVAIKM
GATKEDFDNI TAIHPTAAEE LVTIKVARGD EDNYSYNCGP DQKVDLK
//
