DLDH1_PSEAE
ID DLDH1_PSEAE Reviewed; 464 AA.
AC Q9I1L9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of branched-chain alpha-keto acid dehydrogenase complex;
DE AltName: Full=LPD-Val;
GN Name=lpdV {ECO:0000312|EMBL:AAG05638.1}; OrderedLocusNames=PA2250;
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).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 7-24; 54-64; 72-87; 99-108; 164-178; 199-211; 253-272;
RP 305-336; 385-396 AND 415-456.
RC STRAIN=ATCC 33467 / type 1 smooth;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3) (By similarity). {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 Evidence={ECO:0000250|UniProtKB:P18925};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P18925};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P18925};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P18925}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250|UniProtKB:P18925}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000255}.
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DR EMBL; AE004091; AAG05638.1; -; Genomic_DNA.
DR PIR; F83365; F83365.
DR RefSeq; NP_250940.1; NC_002516.2.
DR RefSeq; WP_003113729.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1L9; -.
DR SMR; Q9I1L9; -.
DR STRING; 287.DR97_6300; -.
DR PaxDb; Q9I1L9; -.
DR PRIDE; Q9I1L9; -.
DR EnsemblBacteria; AAG05638; AAG05638; PA2250.
DR GeneID; 878470; -.
DR KEGG; pae:PA2250; -.
DR PATRIC; fig|208964.12.peg.2351; -.
DR PseudoCAP; PA2250; -.
DR HOGENOM; CLU_016755_0_1_6; -.
DR InParanoid; Q9I1L9; -.
DR OMA; IHAAEEF; -.
DR PhylomeDB; Q9I1L9; -.
DR BioCyc; PAER208964:G1FZ6-2289-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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Glycolysis; NAD; Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..464
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068036"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18925"
FT BINDING 36..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 184..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P18925"
SQ SEQUENCE 464 AA; 48589 MW; 52604A0708418434 CRC64;
MSQILKTSLL IVGGGPGGYV AAIRAGQLGI PTVLVEGAAL GGTCLNVGCI PSKALIHAAE
EYLKARHYAS RSALGIQVQA PSIDIARTVE WKDAIVDRLT SGVAALLKKH GVDVVQGWAR
ILDGKSVAVE LAGGGSQRIE CEHLLLAAGS QSVELPILPL GGKVISSTEA LAPGSLPKRL
VVVGGGYIGL ELGTAYRKLG VEVAVVEAQP RILPGYDEEL TKPVAQALRR LGVELYLGHS
LLGPSENGVR VRDGAGEERE IAADQVLVAV GRKPRSEGWN LESLGLDMNG RAVKVDDQCR
TSMRNVWAIG DLAGEPMLAH RAMAQGEMVA ELIAGKRRQF APVAIPAVCF TDPEVVVAGL
SPEQAKDAGL DCLVASFPFA ANGRAMTLEA NEGFVRVVAR RDNHLVVGWQ AVGKAVSELS
TAFAQSLEMG ARLEDIAGTI HAHPTLGEAV QEAALRALGH ALHI
