ID D8F2I2_9DELT Unreviewed; 462 AA.
AC D8F2I2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN Name=lpdA {ECO:0000313|EMBL:EFK10031.1};
GN ORFNames=NPH_1842 {ECO:0000313|EMBL:EFK10031.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK10031.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK10031.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK10031.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00043836,
CC ECO:0000256|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC ECO:0000256|RuleBase:RU003692};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC ECO:0000256|RuleBase:RU003692};
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000256|RuleBase:RU003692}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003692}.
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:EFK10031.1}.
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DR EMBL; ADZZ01000249; EFK10031.1; -; Genomic_DNA.
DR AlphaFoldDB; D8F2I2; -.
DR OrthoDB; 9786429at2; -.
DR Proteomes; UP000003834; Unassembled WGS sequence.
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; IPR006258; Lipoamide_DH.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003692};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003692};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000003834}.
FT DOMAIN 6..323
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 343..451
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 441
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 178..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 308
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 462 AA; 49169 MW; 46FA43E9F699370B CRC64;
MKMESYDVIV IGGGPGGYSA AVRASQLGCR TALVEKENLG GTCLNWGCIP TKSLLQNAEV
VHLLSKGRTF GFSMENLSID YAVAHKRSRS VVKRQTRRIA ALMKNYNVSV YNGTAGIKSV
KEVHIEPSGD AIKGKNIIIA TGAKGRQLPG IDDAGGKVIN YRQALNLTKV PSSGIIVGAG
PIGVEFATIW NRYGCDVTVV ELLDRVLPLE DSEISLEAEK QLKRSGIRIK TNARVERVVA
NSGGIDVTLR MGEETETLSA ETLLASIGVT PDTQDLGLEA AGVETENGSI IVDSQMRTSV
PNIFAVGDVT GKLALAHVAT AQGMIAAESV IGRKSRALDY HHMPRCIYAY PEVASVGLTE
KQALEQGHKI VTVKCPFVAN GKAVAMDENQ GFAKIVAEAK TKKLLGVHLI GGHVTELIAG
PTGMITLENS AEDLGRTVHP HPTMSEAIME AVHKLCGHAI HI
//
