DLDH2_PSEPU
ID DLDH2_PSEPU Reviewed; 478 AA.
AC P31052;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of 2-oxoglutarate dehydrogenase complex;
DE AltName: Full=Glycine oxidation system L-factor;
DE AltName: Full=LPD-GLC;
GN Name=lpdG;
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=1902462; DOI=10.1128/jb.173.10.3109-3116.1991;
RA Palmer J.A., Hatter K., Sokatch J.R.;
RT "Cloning and sequence analysis of the LPD-glc structural gene of
RT Pseudomonas putida.";
RL J. Bacteriol. 173:3109-3116(1991).
RN [2]
RP SEQUENCE REVISION.
RA Sokatch J.R.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-26.
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: 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).
CC -!- FUNCTION: Also acts in the glycine cleavage system.
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; M80189; AAA96437.1; -; Genomic_DNA.
DR PIR; A39406; A39406.
DR RefSeq; WP_003254207.1; NZ_SCFX01000032.1.
DR AlphaFoldDB; P31052; -.
DR SMR; P31052; -.
DR STRING; 1240350.AMZE01000031_gene1965; -.
DR PRIDE; P31052; -.
DR GeneID; 66676323; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2914869"
FT CHAIN 2..478
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068039"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 188..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 276..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 49..54
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 49896 MW; 2B7979445DC60812 CRC64;
MTQKFDVVVI GAGPGGYVAA IKAAQLGLKT ACIEKYTDAE GKLALGGTCL NVGCIPSKAL
LDSSWKYKEA KESFNVHGIS TGEVKMDVAA MVGRKAGIVK NLTGGVATLF KANGVTSIQG
HGKLLAGKKV EVTKADGTTE VIEAENVILA SGSRPIDIPP APVDQNVIVD STGALEFQAV
PKRLGVIGAG VIGLELGSVW ARLGAEVTVL EALDTFLMAA DTAVSKEAQK TLTKQGLDIK
LGARVTGSKV NGNEVEVTYT NAEGEQKITF DKLIVAVGRR PVTTDLLAAD SGVTIDERGY
IFVDDYCATS VPGVYAIGDV VRGMMLAHKA SEEGIMVVER IKGHKAQMNY DLIPSVIYTH
PEIAWVGKTE QALKAEGVEV NVGTFPFAAS GRAMAANDTG GFVKVIADAK TDRVLGVHVI
GPSAAELVQQ GAIAMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGGAI HVANRKKR
