DLDH3_PSEAE
ID DLDH3_PSEAE Reviewed; 467 AA.
AC Q9HUY1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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; OrderedLocusNames=PA4829;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08214.1; -; Genomic_DNA.
DR PIR; A83042; A83042.
DR RefSeq; NP_253516.1; NC_002516.2.
DR RefSeq; WP_003095344.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUY1; -.
DR SMR; Q9HUY1; -.
DR STRING; 287.DR97_2179; -.
DR PaxDb; Q9HUY1; -.
DR PRIDE; Q9HUY1; -.
DR EnsemblBacteria; AAG08214; AAG08214; PA4829.
DR GeneID; 882254; -.
DR KEGG; pae:PA4829; -.
DR PATRIC; fig|208964.12.peg.5060; -.
DR PseudoCAP; PA4829; -.
DR HOGENOM; CLU_016755_0_1_6; -.
DR InParanoid; Q9HUY1; -.
DR OMA; DAKYGEW; -.
DR PhylomeDB; Q9HUY1; -.
DR BioCyc; PAER208964:G1FZ6-4943-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..467
FT /note="Dihydrolipoyl dehydrogenase 3"
FT /id="PRO_0000287806"
FT ACT_SITE 446
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 182..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 272..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 49659 MW; 0DC0AACBF6D86A8C CRC64;
MMESYDVIVI GAGPGGYNAA IRAGQLGLKV ACVEGRETLG GTCLNVGCMP SKALLHASEL
YAAASGGEFA RLGIRVSPEL DLAQMMKQKD ESVAALTRGV EFLFRKHKVQ WIKGWARLQG
EGRVGVALAD GGHAQLEARD IVIATGSEPA PLPGVPVDNQ RILDSTGALE LVEVPRHLVV
IGAGVIGLEL GSVWRRLGAQ VTVLEYLERI CPGLDGETAR TLQRALTRQG MRFRLGTRVV
AARSGEQGVE LDLQPAAGGA TESLQADYVL VAIGRRPYTE GLGLETVGLA SDRRGMLENQ
GQRSAAPGVW VIGDVTSGPM LAHKAEEEAI VCIERIAGHA AEMNAEVIPS VIYTQPEVAS
VGLGEEQLQA ARREYKVGRF PFSANSRAKI NHESEGFIKI LSDARSDQVL GVHMIGPGVS
EMIGEACVAM EFSASAEDLA LTCHPHPTRS EALRQAAMDV HGRAMQN
