ID A0A087X9L9_POEFO Unreviewed; 600 AA.
AC A0A087X9L9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000002472.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000002472.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
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 ECO:0000256|RuleBase:RU003691}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYCK01008651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007560944.1; XM_007560882.2.
DR AlphaFoldDB; A0A087X9L9; -.
DR STRING; 48698.ENSPFOP00000002472; -.
DR Ensembl; ENSPFOT00000002476.2; ENSPFOP00000002472.2; ENSPFOG00000002288.2.
DR GeneID; 103144083; -.
DR KEGG; pfor:103144083; -.
DR CTD; 114112; -.
DR eggNOG; KOG1752; Eukaryota.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000159178; -.
DR OMA; VGGCDNT; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF7; THIOREDOXIN REDUCTASE 3; 1.
DR Pfam; PF00462; Glutaredoxin; 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.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
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:UP000028760};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 26..88
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT DOMAIN 116..453
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 473..584
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 600 AA; 65999 MW; 5B640FD1D0531814 CRC64;
MPPIEKDTGK NELKTKIQKL IDSNQVVVFS KSYCPYCIQV KDLFKELKIE FNAMELDLIE
NGSNYQEMLL EMTGQRTVPQ VFVNKTHVGG CDKTMQAHKD GSLQQLLSGV KEAYDYDLIV
IGGGSGGLAC SKEAAMLGKK VMVLDYVVPT PTGTTWGLGG TCVNVGCIPK KLMHQTALLS
TAIQDARKFG WEFDESVKHN WDTMKTAVNN YIGSLNWGYR VALRDKNVDY VNAYAEFIEP
HKIKATNKRG KETFYTAARF VLATGERPRY LGVPGDKEYC ITSDDLFSLS YCPGKTLVIG
ASYVALECGG FLAGLGLDVT VMVRSILLRG FDQDMANRAG AHMETHGVKF IRKFVPTKIE
QLEEGSPGRL KVTAKSTETD ETMEDEYNTV LIAVGRNACT DKIGLDKAGV KVNPKNGKIP
VNDEEQTNVP HIYAIGDILE GKWELTPVAI QAGKLLARRL YGGSNVKCDY INVPTTVFTP
LEYGACGLSE ERATELYGPD NIEVYHSLFW PLEFTVPGRD NNQCYAKIIC NKLDSDRVIG
FHYLGPNAGE VTQGFGAAMK CGATKEQFDI TIGIHPTCAE VFTTLEVSKR SGGDITQSGC
//
