ID E8LYY5_9VIBR Unreviewed; 485 AA.
AC E8LYY5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:EGA64105.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:EGA64105.1};
GN ORFNames=VIBR0546_16703 {ECO:0000313|EMBL:EGA64105.1};
OS Vibrio brasiliensis LMG 20546.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA64105.1, ECO:0000313|Proteomes:UP000004371};
RN [1] {ECO:0000313|EMBL:EGA64105.1, ECO:0000313|Proteomes:UP000004371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA64105.1,
RC ECO:0000313|Proteomes:UP000004371};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
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:EGA64105.1}.
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DR EMBL; AEVS01000096; EGA64105.1; -; Genomic_DNA.
DR RefSeq; WP_006881054.1; NZ_AEVS01000096.1.
DR AlphaFoldDB; E8LYY5; -.
DR STRING; 945543.VIBR0546_16703; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000004371; 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; 2.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
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; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000313|EMBL:EGA64105.1}.
FT DOMAIN 7..328
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 351..460
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 450
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 142..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 179..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 485 AA; 52811 MW; CCF3B4F8E94918D8 CRC64;
MKQLNVDVAV IGGGTAGLGA YRAAKAHTDS VVMIEGGPYG TTCARVGCMP SKLLIAAAES
VHQIEKAPGF GVHPQGEIVI NGREVMDRVK RERDRFVGFV LEGVDEIPAE DKIAGYAKFI
DNNTLVVDDH TQINAKRIVI ATGSRPAYPA VWNELGDRLI INDDVFNWDD LPESVAVFGP
GVIGLELGQS LHRLGVKVKL FGLGGQVGPI TDPEVMAYAD KTFKQEFYLD ADVKIESMKR
IDGTDKVEIL FINHQGELES FIVDYVLAAT GRRPNVDKLG LENTSVELDE RGVPVAEHYT
LQTSVESIFI AGDASNQIPL LHEAADQARI AGDNAGRFPD IRAGLRRSPI SAVFSDPQIA
MVGETYKQLT TRLGNCGCFA TGEVSFENQG RSRVMLRNKG ILHVYGEQGT GRFLGAEMMG
PNAEHLAHLL AWAHQNKMTV SEMLDMPFYH PVIEEGVRTA LRDLNAKLHL GPEMIKHCLD
CGPGC
//
