ID A0A093C0Z5_TAUER Unreviewed; 210 AA.
AC A0A093C0Z5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|ARBA:ARBA00012310, ECO:0000256|RuleBase:RU000499};
GN ORFNames=N340_11701 {ECO:0000313|EMBL:KFV06759.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV06759.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV06759.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV06759.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000217};
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; KL452535; KFV06759.1; -; Genomic_DNA.
DR RefSeq; XP_009990413.1; XM_009992111.1.
DR AlphaFoldDB; A0A093C0Z5; -.
DR GeneID; 104383847; -.
DR KEGG; teo:104383847; -.
DR CTD; 2882; -.
DR OrthoDB; 67394at2759; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR013376; Glut_perox_Gpx7.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02540; gpx7; 1.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF5; GLUTATHIONE PEROXIDASE 7; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..200
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 210 AA; 23455 MW; 28298ECACD32F1F4 CRC64;
MLDPEGSVEH QPSSSFPKVL LIALAMLLAI AALLLLAFSA TQQKEPDFYT FKVVNIRGKL
VSLEKYRGSV SLVVNVASEC GYTDSHYKAL QQLQRDLGPY HFNVLAFPCN QFGQQEPDTN
KEIESFARKT YGASFPMFSK IAVSGAGAIP AFKYLIDSTG EEPTWNFWKY LVDPNGKVVK
AWDSTVSVEE IRPSVTELVR KIILKKKDEL
//
