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Database: UniProt
Entry: S7VWJ1_9FLAO
LinkDB: S7VWJ1_9FLAO
Original site: S7VWJ1_9FLAO 
ID   S7VWJ1_9FLAO            Unreviewed;       172 AA.
AC   S7VWJ1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Dihydrolipoamide dehydrogenase of branched-chain alpha-keto acid dehydrogenase {ECO:0000313|EMBL:EPR73732.1};
DE            EC=1.8.1.4 {ECO:0000313|EMBL:EPR73732.1};
GN   ORFNames=ADIWIN_1369 {ECO:0000313|EMBL:EPR73732.1};
OS   Winogradskyella psychrotolerans RS-3.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR73732.1, ECO:0000313|Proteomes:UP000014962};
RN   [1] {ECO:0000313|EMBL:EPR73732.1, ECO:0000313|Proteomes:UP000014962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-3 {ECO:0000313|EMBL:EPR73732.1,
RC   ECO:0000313|Proteomes:UP000014962};
RX   PubMed=23950132;
RA   Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT   "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT   from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT   Ocean.";
RL   Genome Announc. 1:e00630-e00613(2013).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:EPR73732.1}.
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DR   EMBL; ATMR01000089; EPR73732.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7VWJ1; -.
DR   STRING; 641526.ADIWIN_1369; -.
DR   PATRIC; fig|641526.4.peg.1358; -.
DR   eggNOG; COG1249; Bacteria.
DR   Proteomes; UP000014962; Unassembled WGS sequence.
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; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
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:EPR73732.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014962}.
FT   DOMAIN          53..161
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   172 AA;  18099 MW;  EFDAF1827BA4DA6B CRC64;
     MVNDFYQTNI PGYYAIGDVT PGQALAHVAS AEGILCVEKI AGQHVEALDY GNIPGCTYCS
     PEIASVGLTE AQAKEQGLDV KIGKFPFSAS GKASASGAKD GFVKVIFDAK YGEWLGCHMI
     GAGVTDMIAE AVLGRKLETT GHEVLKTVHP HPTMSEAVME AVAAAYDEVI HL
//
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