ID A0A431V5I4_9GAMM Unreviewed; 487 AA.
AC A0A431V5I4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:RTR03889.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:RTR03889.1};
GN ORFNames=EKG36_10065 {ECO:0000313|EMBL:RTR03889.1};
OS Halomonas nitroreducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=447425 {ECO:0000313|EMBL:RTR03889.1, ECO:0000313|Proteomes:UP000267400};
RN [1] {ECO:0000313|EMBL:RTR03889.1, ECO:0000313|Proteomes:UP000267400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11S {ECO:0000313|EMBL:RTR03889.1,
RC ECO:0000313|Proteomes:UP000267400};
RA Yu L.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RTR03889.1}.
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DR EMBL; RXNS01000008; RTR03889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A431V5I4; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000267400; 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 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; 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:RTR03889.1}.
FT DOMAIN 22..339
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 363..462
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 455
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 192..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 324
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 57..62
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 487 AA; 53418 MW; D45419E041EB9E02 CRC64;
MNAHSQRGRR SESAMKTMNV EYAIIGAGTS GLGAYSRISR QTDSLVMIQD GPYGTTCARV
GCMPSKLLIT AADHAHHLQT SDFFGVPASG RVEGRKVLER LRRERDDRFV ARNLGYVDKI
PAHHKLEGRA RFIGPGRLMV GEGIEVNAKK FILACGSRPA ISEVFEPVMA RVLTSDTVFE
LEDLPRSIAV IGMGVIALEL GQALHRLGVA TTIYGRSGKI NALTHPAMQR QALDVLATEL
DIHASGQVRS TWEDAEGAWI EYEQSNGERV TKVFDRVLVA TGRVSNVDRL GMEHADVESS
DTGAIRFDPQ TMRCSHHPIF IAGDATDHLP VWHEAYDEGR IAADNALNYP DAAPAARRPP
LMVFFTDPQI AIVGQSFQRL QGREIVIGEL PFASPRHVVW NKVQGHIQVY LDARSGAILG
AELLGYQAEH LAHLLALAIT HGMTAEQVLE MPIYHPSAEE LLRDVLIDAQ KKRRSHAAKE
MSLASSA
//
