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Database: UniProt
Entry: A0A087R121_APTFO
LinkDB: A0A087R121_APTFO
Original site: A0A087R121_APTFO 
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
//
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