ID   GSHR_CAEEL              Reviewed;         503 AA.
AC   P30635;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-NOV-2008, entry version 79.
DE   RecName: Full=Probable glutathione reductase 2;
DE            Short=GRase;
DE            Short=GR;
DE            EC=1.8.1.7;
GN   Name=trxr-2; ORFNames=ZK637.10;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=92168156; 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.,
RA   Ainscough R., 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   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the
CC       cytosol.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z11115; CAA77459.1; -; Genomic_DNA.
DR   PIR; D88542; D88542.
DR   PIR; S15798; S15798.
DR   RefSeq; NP_498971.1; -.
DR   UniGene; Cel.9538; -.
DR   HSSP; Q94655; 1ONF.
DR   Ensembl; ZK637.10; Caenorhabditis elegans.
DR   GeneID; 176259; -.
DR   KEGG; cel:ZK637.10; -.
DR   NMPDR; fig|6239.3.peg.11001; -.
DR   WormBase; WBGene00014028; trxr-2.
DR   WormPep; ZK637.10; CE15373.
DR   NextBio; 891814; -.
DR   ArrayExpress; P30635; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016654; F:oxidoreductase activity, acting on NADH or ...; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR006338; Reduct_Se.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   PANTHER; PTHR22912:SF23; Reduct_Se; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01438; TGR; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    503       Probable glutathione reductase 2.
FT                                /FTId=PRO_0000067958.
FT   NP_BIND      58     67       FAD (By similarity).
FT   ACT_SITE    476    476       Proton acceptor (By similarity).
FT   DISULFID     67     72       Redox-active (By similarity).
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
//