ID   L9XUV1_9EURY            Unreviewed;       477 AA.
AC   L9XUV1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:ELY65201.1};
DE            EC=1.8.1.4 {ECO:0000313|EMBL:ELY65201.1};
GN   ORFNames=C489_15512 {ECO:0000313|EMBL:ELY65201.1};
OS   Natrinema versiforme JCM 10478.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY65201.1, ECO:0000313|Proteomes:UP000011632};
RN   [1] {ECO:0000313|EMBL:ELY65201.1, ECO:0000313|Proteomes:UP000011632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY65201.1,
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   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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:ELY65201.1}.
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DR   EMBL; AOID01000047; ELY65201.1; -; Genomic_DNA.
DR   RefSeq; WP_006432189.1; NZ_AOID01000047.1.
DR   AlphaFoldDB; L9XUV1; -.
DR   STRING; 1227496.C489_15512; -.
DR   PATRIC; fig|1227496.3.peg.3129; -.
DR   OrthoDB; 27922at2157; -.
DR   Proteomes; UP000011632; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
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   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   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}.
FT   DOMAIN          4..319
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          351..455
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   477 AA;  49920 MW;  72037F473347A530 CRC64;
     MDAYDIVVLG GGSGSQIATA AAEQGLEAAV VEPGPLGGAC ITRGCVPSKA LIHRADIMEE
     VRGAENFGVP AALNDAEYGE ITASVHDTVY EKAENQESSL QDSENVTLYR GEGRFVDDRT
     IAIDTGDGEG EDDRIRGDTV VIAVGGRPMV PPIDGLEETE FLTSDDALFL AEQPDELAIV
     GGGYIGAELG YFFGALGTDV SIVGRSDRFV PREDDDVSAA VTESLESYCD VYTGYEAAEV
     EAGDEEGVVV TAEPSDGDGG ETVELTADEL LLATGRRPNT DTLDLEATGV ETDDKGSIET
     DETLATTADG VWAVGDVLGE QPYKHAADYE AKVVTANVLD DAGRTVDYEA MPHAIFTDPR
     VASVGRTEGD LEAEGRDYDA VTVPYGTAPM GMILEADDGF VKAIAGPDGE ILGCHIVGPQ
     AATLLHEVVV AMDGGGTVDD VAEPVHVHPA LNEVVYAAFD DLSDAAYSTA PDWRDVS
//