ID M3ZAJ4_NOMLE Unreviewed; 493 AA.
AC M3ZAJ4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Glutathione-disulfide reductase {ECO:0000313|Ensembl:ENSNLEP00000023731.2};
GN Name=GSR {ECO:0000313|Ensembl:ENSNLEP00000023731.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000023731.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000023731.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000023731.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
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; ADFV01050903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3ZAJ4; -.
DR Ensembl; ENSNLET00000032079.2; ENSNLEP00000023731.2; ENSNLEG00000011936.3.
DR GeneTree; ENSGT00940000156986; -.
DR HOGENOM; CLU_016755_2_2_1; -.
DR Proteomes; UP000001073; Chromosome 8.
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; 4.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
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 PIRSF; PIRSF000350; Mercury_reductase_MerA; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
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:UP000001073}.
FT DOMAIN 65..361
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 382..492
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 482
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 238..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 102..107
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 493 AA; 53045 MW; 5EA38D63B8B3A11A CRC64;
MALLPRALSA GAGQSWRRAA RAYRGFPLLL PEPAALTRTL SRAMACRQEP QPQGPPPAAD
AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS
EFMHDHADYG FTSCEGKFDW RVIKEKRDAY VSRLNTIYQN NLTKSHIEII RGHAAFTSDP
KPTIEVSGKK YTAPHILIAT GGVPSTPHES EIPGASLGIT SDGFFQLEEL PSRSVIVGAG
YIAVEIAGIL SALGSKTSLL IRHDKVTEVK KTLSGLEVSM VTAVPGRLPV MTVIPDVDCL
LWAIGRDPNS KGLSLDKLGI QTDDKGHIIV DEFQNTNVKG IYAVGDVCGK ALLTPVAIAA
GRKLAHRLFE YKEDSKLDYN NIPTVVFSHP PIGTVGLTED EAIHKYGKEN VKTYSTSFTP
MYHAVTKRKT KCVMKMVCAN KEEKVVGIHM QGLGCDEMLQ GFAVAVKMGA TKADFDNTVA
IHPTSSEELV TLR
//
