ID A0A087R121_APTFO Unreviewed; 421 AA.
AC A0A087R121;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=glutathione-disulfide reductase {ECO:0000256|ARBA:ARBA00012607};
DE EC=1.8.1.7 {ECO:0000256|ARBA:ARBA00012607};
DE Flags: Fragment;
GN ORFNames=AS27_07611 {ECO:0000313|EMBL:KFM07175.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM07175.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM07175.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM07175.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KL226039; KFM07175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R121; -.
DR STRING; 9233.A0A087R121; -.
DR Proteomes; UP000053286; 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:UP000053286}.
FT DOMAIN 1..289
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 310..420
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM07175.1"
FT NON_TER 421
FT /evidence="ECO:0000313|EMBL:KFM07175.1"
SQ SEQUENCE 421 AA; 46040 MW; 2074D3AE1552975F CRC64;
VNVGCVPKKV MWNAAVHAEF VHDHADYGFE TPGVKFNWRT IKEKRDAYVR RLNEIYENNV
KKAHIDIIRG YGKFTADPEP TVEVDGKKYT APHILIATGG RPAAPPDSEI PGASLGMTSD
GFFELEELPR HSVIVGAGYI AVEIAGILST LGSKSSLLIR QDKVLRTFDS MISSNCTQEL
ENTGVDIWKH TQVKTVTKSP RGLLDVTVSS SVPGRKPTEG VIRDVDCLLW AVGREPNTEE
LCLDQVGVQV DAKGHVVVDE YQNTTRRGVY AVGDVCGRAL LTPVAIAAGR KLAHRLFEGK
QDSRLDYRDI PTVVFSHPPI GTVGLTEDEA VATHGRENVK IYSTSFMPLY HAVTQRKVKC
VMKLVCAGKE EKVVGLHMQG LGCDEMLQGF AVAIKMGATK ADLDNTVAIH PTSAEELVTL
R
//