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Database: UniProt
Entry: Q59099_CUPNE
LinkDB: Q59099_CUPNE
Original site: Q59099_CUPNE 
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
//
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