ID A0A0M2HNG6_9MICO Unreviewed; 478 AA.
AC A0A0M2HNG6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:KJL48282.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:KJL48282.1};
GN Name=lpd_1 {ECO:0000313|EMBL:KJL48282.1};
GN ORFNames=RS84_01041 {ECO:0000313|EMBL:KJL48282.1};
OS Microbacterium hydrocarbonoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL48282.1, ECO:0000313|Proteomes:UP000033900};
RN [1] {ECO:0000313|EMBL:KJL48282.1, ECO:0000313|Proteomes:UP000033900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA35 {ECO:0000313|EMBL:KJL48282.1,
RC ECO:0000313|Proteomes:UP000033900};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL48282.1}.
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DR EMBL; JYJB01000007; KJL48282.1; -; Genomic_DNA.
DR RefSeq; WP_045256709.1; NZ_JYJB01000007.1.
DR AlphaFoldDB; A0A0M2HNG6; -.
DR STRING; 273678.RS84_01041; -.
DR PATRIC; fig|273678.4.peg.1037; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000033900; 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; 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 FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000313|EMBL:KJL48282.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033900}.
FT DOMAIN 10..324
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 361..466
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 149..151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 186..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 47..52
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 478 AA; 49681 MW; 9D873790547321E0 CRC64;
MDAAAKTDEY DLIVLGGGPV GENVADRAVQ GGLTAIIVES ELVGGECSYW ACMPSKALLR
SAQALRVAQH VKGAAEAVTG ALDVSAVFAR RDSFTSNWSD DGQVRWLESA HIDLARGHGR
LTGEREVTVT DADGGTRVLR ARHAVAVSTG SDAVIPPIDG LAGVAPWTSR EATSAQELPA
SLAVIGGGVV AVEMATAYAA LGSTVTVIAR SGLLGGMEPF AGERVAAGLE ELGVDVRLSV
GTESVRRDEE GVHIVLSDGS TVTASEVLVA TGRSPRSGDI GLETVGLEPG AWIRVDDTLQ
VPDVPWLYAV GDVNGRVLLT HQGKYQARAA GDLIAARALG EAVDDAPWGR HVATADHAAA
PQVTFSFPEV ASVGLTEKAA KDAGISVQVV DYDLGWVAGA SLYEDGFEGQ ARLVIDTERD
VIVGATFVGP EVAELVQTAT VAIVGEVPIS RLWHAVPAYP TVSEIWLRLL EGYGRDSA
//
