ID R4W7M3_9EURY Unreviewed; 453 AA.
AC R4W7M3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:AGN01048.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:AGN01048.1};
GN ORFNames=L593_05495 {ECO:0000313|EMBL:AGN01048.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN01048.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN01048.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN01048.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
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}.
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DR EMBL; CP005962; AGN01048.1; -; Genomic_DNA.
DR RefSeq; WP_020445942.1; NC_021313.1.
DR AlphaFoldDB; R4W7M3; -.
DR STRING; 1333523.L593_05495; -.
DR GeneID; 16180612; -.
DR KEGG; sali:L593_05495; -.
DR PATRIC; fig|1333523.5.peg.1122; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_1_2_2; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000014072; Chromosome.
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 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:AGN01048.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014072}.
FT DOMAIN 4..313
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 340..445
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 453 AA; 48253 MW; 76AABECC4C0F025E CRC64;
MADFDVLVIG GGTGNNVAAA AADAGLETAL VEPGPLGGTC LNRGCNPSKM LIQAANAVHD
VRDAERFHVD ATFEGIDHAV VVDEMDELLG GIAADMETRY RERDHLTLFD ERTEFVDERT
VELGGEAVTA EKIVIAAGSR PVVPPIDGLA DVDYLTSQDA LYRRTTPESL VILGGGYIAV
ELGYFFDAMG TDVKIVEMMD SLVHREDADV AGAFTELAAD RHDVYTGHRV TAVEEADESY
AVHAETEAGE ATTVEGSEVL VALGRRPNSD TLALETAGIE VDDRGFVETN EYLETTAEGV
WAQGDVAGNA LFKHSGDYET RHTIANVVDE ERRTLDLSAM PHAIFTEPQI AGVGATADDL
DEEGSEYVTG RADYADSAMG RAKKLDHGFV KVLADPDGEI LGAHAIGYEA ATLLHEAVVA
MRTGATVEDV GGTIHAHPTL SKVVEAAFRD VPR
//
