ID   TRXR2_CAEEL             Reviewed;         503 AA.
AC   P30635;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Probable glutathione reductase 2;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=trxr-2; ORFNames=ZK637.10;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1538779; DOI=10.1038/356037a0;
RA   Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA   Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA   Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA   Waterston R.;
RT   "The C. elegans genome sequencing project: a beginning.";
RL   Nature 356:37-41(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; Z11115; CAA77459.1; -; Genomic_DNA.
DR   PIR; D88542; D88542.
DR   PIR; S15798; S15798.
DR   RefSeq; NP_498971.1; NM_066570.4.
DR   AlphaFoldDB; P30635; -.
DR   SMR; P30635; -.
DR   BioGRID; 41460; 25.
DR   STRING; 6239.ZK637.10.1; -.
DR   ChEMBL; CHEMBL2366473; -.
DR   EPD; P30635; -.
DR   PaxDb; 6239-ZK637-10-2; -.
DR   PeptideAtlas; P30635; -.
DR   EnsemblMetazoa; ZK637.10.1; ZK637.10.1; WBGene00014028.
DR   GeneID; 176259; -.
DR   KEGG; cel:CELE_ZK637.10; -.
DR   UCSC; ZK637.10; c. elegans.
DR   AGR; WB:WBGene00014028; -.
DR   WormBase; ZK637.10; CE15373; WBGene00014028; trxr-2.
DR   eggNOG; KOG4716; Eukaryota.
DR   GeneTree; ENSGT00940000158832; -.
DR   HOGENOM; CLU_016755_2_4_1; -.
DR   InParanoid; P30635; -.
DR   OMA; CFDYVKP; -.
DR   OrthoDB; 5473641at2759; -.
DR   PhylomeDB; P30635; -.
DR   Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:P30635; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00014028; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
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:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IDA:WormBase.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; 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   InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR   NCBIfam; TIGR01438; TGR; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF6; THIOREDOXIN REDUCTASE 2; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..503
FT                   /note="Probable glutathione reductase 2"
FT                   /id="PRO_0000067958"
FT   ACT_SITE        476
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..67
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..72
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   503 AA;  55046 MW;  CE2385C9ACBD9AD2 CRC64;
     MLLSTFKRHL PIRRLFSSNK FDLIVIGAGS GGLSCSKRAA DLGANVALID AVEPTPHGHS
     WGIGGTCANV GCIPKKLMHQ AAIVGKELKH ADKYGWNGID QEKIKHDWNV LSKNVNDRVK
     ANNWIYRVQL NQKKINYFNA YAEFVDKDKI VITGTDKNKT KNFLSAPNVV ISTGLRPKYP
     NIPGAELGIT SDDLFTLASV PGKTLIVGGG YVALECAGFL SAFNQNVEVL VRSIPLKGFD
     RDCVHFVMEH LKTTGVKVKE HVEVERVEAV GSKKKVTFTG NGGVEEYDTV IWAAGRVPNL
     KSLNLDNAGV RTDKRSGKIL ADEFDRASCN GVYAVGDIVQ DRQELTPLAI QSGKLLADRL
     FSNSKQIVRF DGVATTVFTP LELSTVGLTE EEAIQKHGED SIEVFHSHFT PFEYVVPQNK
     DSGFCYVKAV CTRDESQKIL GLHFVGPNAA EVIQGYAVAF RVGISMSDLQ NTIAIHPCSS
     EEFVKLHITK RSGQDPRTQG CCG
//