ID   A0A125RCK2_9EURY        Unreviewed;       484 AA.
AC   A0A125RCK2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:AMD17442.1};
GN   ORFNames=TL18_05055 {ECO:0000313|EMBL:AMD17442.1};
OS   Methanobrevibacter sp. YE315.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=1609968 {ECO:0000313|EMBL:AMD17442.1, ECO:0000313|Proteomes:UP000057992};
RN   [1] {ECO:0000313|EMBL:AMD17442.1, ECO:0000313|Proteomes:UP000057992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE315 {ECO:0000313|EMBL:AMD17442.1,
RC   ECO:0000313|Proteomes:UP000057992};
RA   Ouwerkerk D., Gilbert R.A., Klieve A.V., Martinez E.;
RT   "Genome sequence of Methanobrevibacter sp. YE315.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP010834; AMD17442.1; -; Genomic_DNA.
DR   RefSeq; WP_067042299.1; NZ_CP010834.1.
DR   AlphaFoldDB; A0A125RCK2; -.
DR   STRING; 1609968.TL18_05055; -.
DR   GeneID; 28487206; -.
DR   KEGG; meye:TL18_05055; -.
DR   PATRIC; fig|1609968.3.peg.1043; -.
DR   OrthoDB; 27922at2157; -.
DR   Proteomes; UP000057992; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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.
PE   4: Predicted;
FT   DOMAIN          3..349
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          370..470
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   484 AA;  53640 MW;  01C82F56B95205A7 CRC64;
     MDYDVIYIGS GNAAWQGGRF LRKAGLKILI VEESLYGGAC ANRGCNSKAL LDAPYEIKAL
     TENFEGVGKS GNFDVNWSDL MELKRQRIAG MSIFLDGKFD EYDLDVAHGK GVIIDEHTVQ
     VGQRKFTTDK IVICTGLKPV IPDIKGKEYL HDSTDFLDIS ELPKHTIIIG AGFVGMEFAS
     ILAEAGLEAD VIIRGNMALK YFHQPYVQKI IEILKEKNIR FHFNQSVKEI IKDDNVIIDN
     PESKVLNVTS AMNSDEFLRD PESKVDNKAY ENAFTVNCES GLSLTGDYVI AAMGRTANVE
     DIGLENVGLT YTNKGIKVNG HLQTEVPNIY ASGDVADTGI AKLVTVAIHH SKYLAKELLG
     EADEITYPVV PAVAYTIPRI ATVGVPAYIA EKSDEYEVHT IKYGRSYSLE LKNDRTAEAK
     VIVDRDLNIV GAEIYAAEAE NVANMFAFII NKKITLEELD YMIYAFPSSS SVCLYKLHNI
     HYKF
//