ID Q59099_CUPNE Unreviewed; 594 AA.
AC Q59099;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 139.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00016961, ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN Name=pdhL {ECO:0000313|EMBL:AAA21600.1};
GN Synonyms=lpdA {ECO:0000313|EMBL:QQB76783.1};
GN ORFNames=I6H87_00110 {ECO:0000313|EMBL:QQB76783.1};
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590 {ECO:0000313|EMBL:AAA21600.1};
RN [1] {ECO:0000313|EMBL:AAA21600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H16 {ECO:0000313|EMBL:AAA21600.1};
RX PubMed=8021225;
RA Hein S., Steinbuechel A.;
RT "Biochemical and molecular characterization of the Alcaligenes eutrophus
RT pyruvate dehydrogenase complex and identification of a new type of
RT dihydrolipoamide dehydrogenase.";
RL J. Bacteriol. 176:4394-4408(1994).
RN [2] {ECO:0000313|EMBL:QQB76783.1, ECO:0000313|Proteomes:UP000595791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_1030 {ECO:0000313|EMBL:QQB76783.1,
RC ECO:0000313|Proteomes:UP000595791};
RA Kerrigan L., Long C., Tallon L., Sadzewicz L., Zhao X., Boylan J., Ott S.,
RA Bowen H., Vavikolanu K., Mehta A., Aluvathingal J., Nadendla S., Yan Y.,
RA Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001492,
CC ECO:0000256|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
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}.
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DR EMBL; U09865; AAA21600.1; -; Genomic_DNA.
DR EMBL; CP066018; QQB76783.1; -; Genomic_DNA.
DR PIR; D55514; D55514.
DR RefSeq; WP_011615030.1; NZ_LVWN01000011.1.
DR AlphaFoldDB; Q59099; -.
DR GeneID; 57643476; -.
DR Proteomes; UP000595791; Chromosome 1.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
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 InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 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}; Lipoyl {ECO:0000256|ARBA:ARBA00022823};
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}.
FT DOMAIN 3..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 567
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 303..310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 394
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 435
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 441..444
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 159..164
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 594 AA; 62110 MW; D0E9EC3432B21A44 CRC64;
MSVIEVKVPD IGDFDAVEVI EVLVKAGDTV EVEQSLIVLE SDKASMDVPS SAAGKVVEVK
VKVGDKVGQG AVICTIEAQQ AAAAPAPAQA PAPAQAPAPA AAAPAPAPAA ASHSGGADIQ
CEMLVLGAGP GGYSAAFRAA DLGMNTVLVE RYSTLGGVCL NVGCIPSKAL LHNAAVIDEA
KALAAHGILF GEAKIDLDGL RHYKNQVVGK LTGGLAGMAK ARKVQVVRGI GNFLDPHHME
VELTEGEGKR STGKKTVIRF EKAIIAAGSQ AVKLPFIPED PRIVDSTGAL ELPEVPNKML
VIGGGIIGLE MATVYSTLGA DIDVVEMLDG LMNGADRDLV KVWEKKNKDR FGKVMLKTKT
VGVEAKPDGI YVKFEGEAAP AEPQRYDLVL VSVGRSPNGK RISAEKAGVA VSERGFINVD
KQMRTNVPHI FAIGDIVGQP MLAHKAVHEA HVAAEAAHGE KAYFDAKQIP SVAFTDPEVA
WAGLTEDECK EKGIKYSKGV FPWAASGRAI ANGRDEGFTK LIFDEETHRV IGGGIVGTHA
GDLISEVCLA IEMGADAVDI GKTIHPHPTL GESIGMAAEI YEGTCTDVPP PRKR
//