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Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of 2-oxoglutarate dehydrogenase complex)

 DLDH_PSEFL              Reviewed;         478 AA.
P14218;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 130.
RecName: Full=Dihydrolipoyl dehydrogenase;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=E3 component of 2-oxoglutarate dehydrogenase complex;
Name=lpd;
Pseudomonas fluorescens.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=294;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-23.
PubMed=2515251; DOI=10.1099/00221287-135-7-1787;
Benen J.A.E., van Berkel W.J.H., van Dongen W.M.A.M., Mueller F.,
de Kok A.;
"Molecular cloning and sequence determination of the lpd gene encoding
lipoamide dehydrogenase from Pseudomonas fluorescens.";
J. Gen. Microbiol. 135:1787-1797(1989).
[2]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT,
AND DISULFIDE BOND.
PubMed=8487301; DOI=10.1006/jmbi.1993.1236;
Mattevi A., Obmolova G., Kalk K.H., van Berkel W.J.H., Hol W.G.J.;
"Three-dimensional structure of lipoamide dehydrogenase from
Pseudomonas fluorescens at 2.8-A resolution. Analysis of redox and
thermostability properties.";
J. Mol. Biol. 230:1200-1215(1993).
-!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex
catalyzes the overall conversion of alpha-keto acids to acyl-CoA
and CO(2). It contains multiple copies of 3 enzymatic components:
branched-chain alpha-keto acid decarboxylase (E1), lipoamide
acyltransferase (E2) and lipoamide dehydrogenase (E3).
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8487301}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
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EMBL; M28356; AAA99234.1; -; Genomic_DNA.
PDB; 1LPF; X-ray; 2.80 A; A/B=2-478.
PDBsum; 1LPF; -.
ProteinModelPortal; P14218; -.
SMR; P14218; -.
DrugBank; DB03147; Flavin adenine dinucleotide.
PRIDE; P14218; -.
EvolutionaryTrace; P14218; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase;
Redox-active center.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2515251}.
CHAIN 2 478 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000068037.
NP_BIND 34 49 FAD. {ECO:0000269|PubMed:8487301}.
NP_BIND 188 192 NAD. {ECO:0000250}.
NP_BIND 276 279 NAD. {ECO:0000250}.
ACT_SITE 451 451 Proton acceptor. {ECO:0000250}.
BINDING 58 58 FAD. {ECO:0000269|PubMed:8487301}.
BINDING 122 122 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:8487301}.
BINDING 211 211 NAD. {ECO:0000250}.
BINDING 245 245 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 319 319 FAD. {ECO:0000269|PubMed:8487301}.
BINDING 327 327 FAD; via amide nitrogen.
{ECO:0000269|PubMed:8487301}.
DISULFID 49 54 Redox-active.
{ECO:0000269|PubMed:8487301}.
STRAND 4 10 {ECO:0000244|PDB:1LPF}.
HELIX 14 25 {ECO:0000244|PDB:1LPF}.
STRAND 30 34 {ECO:0000244|PDB:1LPF}.
STRAND 39 43 {ECO:0000244|PDB:1LPF}.
HELIX 47 52 {ECO:0000244|PDB:1LPF}.
HELIX 54 72 {ECO:0000244|PDB:1LPF}.
HELIX 75 77 {ECO:0000244|PDB:1LPF}.
STRAND 79 86 {ECO:0000244|PDB:1LPF}.
HELIX 88 113 {ECO:0000244|PDB:1LPF}.
STRAND 115 124 {ECO:0000244|PDB:1LPF}.
HELIX 126 128 {ECO:0000244|PDB:1LPF}.
STRAND 129 134 {ECO:0000244|PDB:1LPF}.
STRAND 139 149 {ECO:0000244|PDB:1LPF}.
STRAND 153 155 {ECO:0000244|PDB:1LPF}.
TURN 165 167 {ECO:0000244|PDB:1LPF}.
HELIX 171 174 {ECO:0000244|PDB:1LPF}.
STRAND 182 187 {ECO:0000244|PDB:1LPF}.
HELIX 191 202 {ECO:0000244|PDB:1LPF}.
STRAND 206 210 {ECO:0000244|PDB:1LPF}.
STRAND 212 217 {ECO:0000244|PDB:1LPF}.
HELIX 222 235 {ECO:0000244|PDB:1LPF}.
STRAND 238 240 {ECO:0000244|PDB:1LPF}.
STRAND 244 247 {ECO:0000244|PDB:1LPF}.
STRAND 254 260 {ECO:0000244|PDB:1LPF}.
STRAND 265 271 {ECO:0000244|PDB:1LPF}.
STRAND 273 275 {ECO:0000244|PDB:1LPF}.
STRAND 279 281 {ECO:0000244|PDB:1LPF}.
TURN 284 286 {ECO:0000244|PDB:1LPF}.
STRAND 308 311 {ECO:0000244|PDB:1LPF}.
STRAND 314 316 {ECO:0000244|PDB:1LPF}.
HELIX 318 320 {ECO:0000244|PDB:1LPF}.
STRAND 321 323 {ECO:0000244|PDB:1LPF}.
HELIX 327 341 {ECO:0000244|PDB:1LPF}.
HELIX 350 352 {ECO:0000244|PDB:1LPF}.
STRAND 355 357 {ECO:0000244|PDB:1LPF}.
STRAND 359 367 {ECO:0000244|PDB:1LPF}.
HELIX 370 375 {ECO:0000244|PDB:1LPF}.
STRAND 380 386 {ECO:0000244|PDB:1LPF}.
HELIX 387 389 {ECO:0000244|PDB:1LPF}.
HELIX 391 396 {ECO:0000244|PDB:1LPF}.
STRAND 402 411 {ECO:0000244|PDB:1LPF}.
STRAND 413 421 {ECO:0000244|PDB:1LPF}.
HELIX 424 436 {ECO:0000244|PDB:1LPF}.
HELIX 441 445 {ECO:0000244|PDB:1LPF}.
HELIX 455 465 {ECO:0000244|PDB:1LPF}.
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


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