ID   A0A0M0BY65_9ARCH        Unreviewed;       476 AA.
AC   A0A0M0BY65;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:KON33532.1};
GN   ORFNames=AC477_01455 {ECO:0000313|EMBL:KON33532.1};
OS   miscellaneous Crenarchaeota group-1 archaeon SG8-32-1.
OC   Archaea; Candidatus Bathyarchaeota; MCG-1.
OX   NCBI_TaxID=1685124 {ECO:0000313|EMBL:KON33532.1, ECO:0000313|Proteomes:UP000037237};
RN   [1] {ECO:0000313|EMBL:KON33532.1, ECO:0000313|Proteomes:UP000037237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8-32-1 {ECO:0000313|EMBL:KON33532.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KON33532.1}.
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DR   EMBL; LFWU01000028; KON33532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BY65; -.
DR   PATRIC; fig|1685124.3.peg.220; -.
DR   Proteomes; UP000037237; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|ARBA:ARBA00023027};
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..323
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          344..455
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   476 AA;  53262 MW;  1D36B5C68C30622A CRC64;
     MKEYDLICIG TGSALSIVEA MIQHNPKSKV AVIDKDEPGG ICLTRGCIPS KLLLYPADVV
     RTVEKANVFG IDSKIKNIDF KKIMERMRNT INKDMNDIRQ GLSQSKHVDY YHETAVFVAP
     YTIKVGKEII NAKMIVLGIG SKPSVPPIKG IEKTTYLTSD TILKISELPP SVIIIGGGYV
     AAEFSHFLSS MGSKVTVIGR NPQFIPEEEP EISTLAKREL GKHVTIYTNH EVKEVRINKN
     GKKKLIVINR ETRQKIELTA DEIMVATGRS SLSDVLHTEK GKIKTDRNGW IVVNEYLETS
     QPNIWALGDA NGKYPFKHVA NYEAAIVYYN ALLKQKIKTD YHAIPHAVFT YPEIAAVGLG
     EKDAIEKYGV DKVLIGFYRF EDTAKGEAMN AYDFFVKVIV EQSTMKILGA HIIGPSASVL
     IHEIIPLMYT LEQSANPITN SMHIHPALSE VVDRAFRSLM PPEHYHHLIE HHYKLL
//