DLDH_PSEFL
ID DLDH_PSEFL Reviewed; 478 AA.
AC P14218;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
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;
GN Name=lpd;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-23.
RX PubMed=2515251; DOI=10.1099/00221287-135-7-1787;
RA Benen J.A.E., van Berkel W.J.H., van Dongen W.M.A.M., Mueller F.,
RA de Kok A.;
RT "Molecular cloning and sequence determination of the lpd gene encoding
RT lipoamide dehydrogenase from Pseudomonas fluorescens.";
RL J. Gen. Microbiol. 135:1787-1797(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT, AND
RP DISULFIDE BOND.
RX PubMed=8487301; DOI=10.1006/jmbi.1993.1236;
RA Mattevi A., Obmolova G., Kalk K.H., van Berkel W.J.H., Hol W.G.J.;
RT "Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas
RT fluorescens at 2.8-A resolution. Analysis of redox and thermostability
RT properties.";
RL J. Mol. Biol. 230:1200-1215(1993).
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 -!- 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;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8487301}.
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}.
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DR EMBL; M28356; AAA99234.1; -; Genomic_DNA.
DR PDB; 1LPF; X-ray; 2.80 A; A/B=2-478.
DR PDBsum; 1LPF; -.
DR AlphaFoldDB; P14218; -.
DR SMR; P14218; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR EvolutionaryTrace; P14218; -.
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 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2515251"
FT CHAIN 2..478
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068037"
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:0000269|PubMed:8487301"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8487301"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8487301"
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:0000269|PubMed:8487301"
FT BINDING 327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8487301"
FT DISULFID 49..54
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:8487301"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 88..113
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1LPF"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1LPF"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 370..375
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 402..411
FT /evidence="ECO:0007829|PDB:1LPF"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:1LPF"
FT HELIX 455..465
FT /evidence="ECO:0007829|PDB:1LPF"
SQ SEQUENCE 478 AA; 50151 MW; B23EB31268C69EC7 CRC64;
MSQKFDVVVI GAGPGGYVAA IRAAQLGLKT ACIEKYIGKE GKVALGGTCL NVGCIPSKAL
LDSSYKYHEA KEAFKVHGIE AKGVTIDVPA MVARKANIVK NLTGGIATLF KANGVTSFEG
HGKLLANKQV EVTGLDGKTQ VLEAENVIIA SGSRPVEIPP APLSDDIIVD STGALEFQAV
PKKLGVIGAG VIGLELGSVW ARLGAEVTVL EALDKFLPAA DEQIAKEALK VLTKQGLNIR
LGARVTASEV KKKQVTVTFT DANGEQKETF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF
IYVDDHCKTS VPGVFAIGDV VRGAMLAHKA SEEGVMVAER IAGHKAQMNY DLIPSVIYTH
PEIAWVGKTE QTLKAEGVEV NVGTFPFAAS GRAMAANDTT GLVKVIADAK TDRVLGVHVI
GPSAAELVQQ GAIGMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGHAI HIANRKKR
