ID A0A151ER65_9EURY Unreviewed; 472 AA.
AC A0A151ER65;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:KYK31114.1};
GN ORFNames=AYK23_04150 {ECO:0000313|EMBL:KYK31114.1};
OS Candidatus Proteinoplasmatales archaeon SG8-5.
OC Archaea; Euryarchaeota; Candidatus Proteinoplasmatales.
OX NCBI_TaxID=1803822 {ECO:0000313|EMBL:KYK31114.1, ECO:0000313|Proteomes:UP000075319};
RN [1] {ECO:0000313|Proteomes:UP000075319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL Submitted (FEB-2016) 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:KYK31114.1}.
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DR EMBL; LSSH01000008; KYK31114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151ER65; -.
DR Proteomes; UP000075319; 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..314
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 343..454
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 472 AA; 51611 MW; A010B8DD05E3E8C2 CRC64;
MKEYDVIAIG SGSSMNIISA MLRKPGVKAA VIEKDDPGGI CLTRGCIPTK ILVYPAELVR
MVDDLGKFGI DAPLKKVDFA KVMQRMRDHI RPDIEGIRKG LSQAENIDYY PVAAEFTAPY
TLKVGNETIT SKLIFLCIGS EVRIPPVKGL DSVGYHTSDT VLGMTQLPAS LAIIGGGYIA
AEYGHFFSAM GSKVTIVGRN PQFLPQEEPE VSELALKEMG KHMTILTDHE VLEVRKGMTG
KKKVVAKNRA SGITASVTAD EILVATGRGP NTDILHPEKA GIEVDEKGWI KVNEYLETNQ
PGIWAFGDAT GKHLFKHVAN YESLVVYQNA ILGNSERAEY HAVPHAVFTH PEIAGVGMRE
KEAVAAYGEE RVGIGFQRFE DTAKGQAMGV KDYFVKVIID TETGRILGAH IIGPQASVLI
QEIINLMYTP SGNWAPARAA MHIHPGLSEV VERAFQGLMS PEHYHHMRSH HH
//
