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Database: UniProt
Entry: L9XWU3_9EURY
LinkDB: L9XWU3_9EURY
Original site: L9XWU3_9EURY 
ID   L9XWU3_9EURY            Unreviewed;       293 AA.
AC   L9XWU3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ELY66309.1};
GN   ORFNames=C489_13156 {ECO:0000313|EMBL:ELY66309.1};
OS   Natrinema versiforme JCM 10478.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY66309.1, ECO:0000313|Proteomes:UP000011632};
RN   [1] {ECO:0000313|EMBL:ELY66309.1, ECO:0000313|Proteomes:UP000011632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY66309.1,
RC   ECO:0000313|Proteomes:UP000011632};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELY66309.1}.
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DR   EMBL; AOID01000036; ELY66309.1; -; Genomic_DNA.
DR   AlphaFoldDB; L9XWU3; -.
DR   STRING; 1227496.C489_13156; -.
DR   PATRIC; fig|1227496.3.peg.2651; -.
DR   Proteomes; UP000011632; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          48..243
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   293 AA;  32433 MW;  A7457DAC250E3968 CRC64;
     MMQDVHNLLG VTEETSGNEF LSVGRDQLRE YGCDIHNDLL VSCDSTEDGS IRLCGNNADY
     RTEYVVLATG FNDVRPEPPL PRTGRGLHYC LHCDAYMFVN EPVYVMGYGE SAAHVAAIML
     NFTDDVDILT RNDSPEWSDE TATMLSNHPI DIIHEDITGV QNDKDGWLAA LEFEDGMVRE
     YKGGFAMYGA EYNNGLARNL GCDINDDGTV VVDDHGQTTV DRVYAVGDLT PGHNQLPIAL
     GEGAKAGISL HFALREFPRD LDVIEEQGPV RSDEVPGIPD ELLEQEVDFH TYD
//
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