DLDH3_PSEPU
ID DLDH3_PSEPU Reviewed; 466 AA.
AC P31046;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Dihydrolipoyl dehydrogenase 3;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase 3;
DE Short=LPD-3;
GN Name=lpd3;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G2;
RX PubMed=1722146; DOI=10.1111/j.1432-1033.1991.tb16367.x;
RA Palmer J.A., Madhusudhan K.T., Hatter K., Sokatch J.R.;
RT "Cloning, sequence and transcriptional analysis of the structural gene for
RT LPD-3, the third lipoamide dehydrogenase of Pseudomonas putida.";
RL Eur. J. Biochem. 202:231-240(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=2914869; DOI=10.1128/jb.171.2.665-668.1989;
RA Burns G., Sykes P.J., Hatter K., Sokatch J.R.;
RT "Isolation of a third lipoamide dehydrogenase from Pseudomonas putida.";
RL J. Bacteriol. 171:665-668(1989).
CC -!- FUNCTION: LPD-3 may substitute for lipoamide dehydrogenase of the 2-
CC oxoglutarate dehydrogenase and pyruvate multienzyme complexes when the
CC latter is inactive or missing.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X55704; CAA39235.1; -; Genomic_DNA.
DR PIR; S19685; S19685.
DR AlphaFoldDB; P31046; -.
DR SMR; P31046; -.
DR STRING; 1240350.AMZE01000020_gene1470; -.
DR PRIDE; P31046; -.
DR eggNOG; COG1249; Bacteria.
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 GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT CHAIN 1..466
FT /note="Dihydrolipoyl dehydrogenase 3"
FT /id="PRO_0000068040"
FT ACT_SITE 445
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 33..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 181..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 466 AA; 49257 MW; E805AC5E879881F3 CRC64;
MKSYDVVIIG GGPGGYNAAI RAGQLGLTVA CVEGRSTLGG TCLNVGCMPS KALLHASELY
EAASGDEFAH LGIEVKPTLN LAQMMKQKDE SVTGLTKGIE YLFRKNKVDW IKGWGRLDGV
GKVVVKAEDG SETALQAKDI VIATGSEPTP LPGVTIDNQR IIDSTGALSL PQVPKHLVVI
GAGVIGLELG SVWRRLGSQV TVIEYLDRIC PGTDTETAKT LQKALAKQGM VFKLGSKVTQ
ATASADGVSL VLEPAAGGTA ESLQADYVLV AIGRRPYTKG LNLESVGLET DKRGMLAQRT
PPTSVPGVWV IGDVTSGPML AHKAEDEAVA CIERIAGKPH EVNYNLIPGV IYTRPELATV
GKTEEQLKAE GRAYKVGKFP FTANSRAKIN HETEGFAKVI ADAETDEVLG VHLVGPSVSE
MIGEFCVAME FSASAEDIAL TCHPHPTRSE ALRQAAMNVD GMAMQI
