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Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of pyruvate complex)

 DLDH1_GEOSE             Reviewed;         470 AA.
P11959;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
28-FEB-2018, entry version 133.
RecName: Full=Dihydrolipoyl dehydrogenase;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=E3 component of pyruvate complex;
Name=pdhD;
Geobacillus stearothermophilus (Bacillus stearothermophilus).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
NCBI_TaxID=1422;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
PubMed=2200674; DOI=10.1111/j.1432-1033.1990.tb19128.x;
Hawkins C.F., Borges A., Perham R.N.;
"Cloning and sequence analysis of the genes encoding the alpha and
beta subunits of the E1 component of the pyruvate dehydrogenase
multienzyme complex of Bacillus stearothermophilus.";
Eur. J. Biochem. 191:337-346(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
PubMed=2253629; DOI=10.1111/j.1432-1033.1990.tb19432.x;
Borges A., Hawkins C.F., Packman L.C., Perham R.N.;
"Cloning and sequence analysis of the genes encoding the
dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase
components of the pyruvate dehydrogenase multienzyme complex of
Bacillus stearothermophilus.";
Eur. J. Biochem. 194:95-102(1990).
[3]
PROTEIN SEQUENCE OF 41-56.
PubMed=6896188; DOI=10.1016/0014-5793(82)80839-9;
Packman L.C., Perham R.N.;
"An amino acid sequence in the active site of lipoamide dehydrogenase
from Bacillus stearothermophilus.";
FEBS Lett. 139:155-158(1982).
[4]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD, AND
SUBUNIT.
PubMed=8805537; DOI=10.1016/S0969-2126(96)00032-9;
Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J.;
"Protein-protein interactions in the pyruvate dehydrogenase
multienzyme complex: dihydrolipoamide dehydrogenase complexed with the
binding domain of dihydrolipoamide acetyltransferase.";
Structure 4:277-286(1996).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-
ketoacid dehydrogenase complexes.
-!- 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. Identified in a complex with PdhC.
{ECO:0000269|PubMed:8805537}.
-!- INTERACTION:
P11961:pdhC; NbExp=3; IntAct=EBI-9021392, EBI-1040691;
-!- 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; X53560; CAA37631.1; -; Genomic_DNA.
PIR; S13839; S13839.
PDB; 1EBD; X-ray; 2.60 A; A/B=7-461.
PDBsum; 1EBD; -.
ProteinModelPortal; P11959; -.
SMR; P11959; -.
DIP; DIP-6155N; -.
IntAct; P11959; 1.
BRENDA; 1.8.1.4; 623.
EvolutionaryTrace; P11959; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron transfer 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.
CHAIN 1 470 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000068015.
NP_BIND 39 47 FAD. {ECO:0000269|PubMed:8805537}.
NP_BIND 183 187 NAD. {ECO:0000250}.
NP_BIND 271 274 NAD. {ECO:0000250}.
ACT_SITE 446 446 Proton acceptor. {ECO:0000250}.
BINDING 56 56 FAD. {ECO:0000269|PubMed:8805537}.
BINDING 119 119 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 206 206 NAD. {ECO:0000250}.
BINDING 314 314 FAD. {ECO:0000269|PubMed:8805537}.
BINDING 322 322 FAD; via amide nitrogen.
{ECO:0000269|PubMed:8805537}.
DISULFID 47 52 Redox-active. {ECO:0000250}.
STRAND 11 15 {ECO:0000244|PDB:1EBD}.
HELIX 19 30 {ECO:0000244|PDB:1EBD}.
STRAND 35 41 {ECO:0000244|PDB:1EBD}.
HELIX 45 49 {ECO:0000244|PDB:1EBD}.
HELIX 52 69 {ECO:0000244|PDB:1EBD}.
HELIX 72 74 {ECO:0000244|PDB:1EBD}.
HELIX 85 108 {ECO:0000244|PDB:1EBD}.
TURN 109 111 {ECO:0000244|PDB:1EBD}.
STRAND 113 123 {ECO:0000244|PDB:1EBD}.
STRAND 126 131 {ECO:0000244|PDB:1EBD}.
STRAND 134 139 {ECO:0000244|PDB:1EBD}.
STRAND 141 145 {ECO:0000244|PDB:1EBD}.
STRAND 149 151 {ECO:0000244|PDB:1EBD}.
STRAND 161 164 {ECO:0000244|PDB:1EBD}.
HELIX 166 170 {ECO:0000244|PDB:1EBD}.
STRAND 177 182 {ECO:0000244|PDB:1EBD}.
HELIX 186 197 {ECO:0000244|PDB:1EBD}.
STRAND 201 212 {ECO:0000244|PDB:1EBD}.
HELIX 217 229 {ECO:0000244|PDB:1EBD}.
STRAND 233 246 {ECO:0000244|PDB:1EBD}.
STRAND 249 256 {ECO:0000244|PDB:1EBD}.
STRAND 259 270 {ECO:0000244|PDB:1EBD}.
STRAND 274 277 {ECO:0000244|PDB:1EBD}.
STRAND 279 282 {ECO:0000244|PDB:1EBD}.
TURN 283 287 {ECO:0000244|PDB:1EBD}.
STRAND 309 311 {ECO:0000244|PDB:1EBD}.
HELIX 313 315 {ECO:0000244|PDB:1EBD}.
STRAND 316 318 {ECO:0000244|PDB:1EBD}.
HELIX 322 336 {ECO:0000244|PDB:1EBD}.
STRAND 350 352 {ECO:0000244|PDB:1EBD}.
STRAND 354 356 {ECO:0000244|PDB:1EBD}.
STRAND 358 362 {ECO:0000244|PDB:1EBD}.
HELIX 365 369 {ECO:0000244|PDB:1EBD}.
TURN 370 372 {ECO:0000244|PDB:1EBD}.
STRAND 375 381 {ECO:0000244|PDB:1EBD}.
HELIX 382 384 {ECO:0000244|PDB:1EBD}.
HELIX 386 391 {ECO:0000244|PDB:1EBD}.
STRAND 397 403 {ECO:0000244|PDB:1EBD}.
TURN 404 406 {ECO:0000244|PDB:1EBD}.
STRAND 408 416 {ECO:0000244|PDB:1EBD}.
HELIX 419 432 {ECO:0000244|PDB:1EBD}.
HELIX 436 441 {ECO:0000244|PDB:1EBD}.
HELIX 451 459 {ECO:0000244|PDB:1EBD}.
SEQUENCE 470 AA; 49356 MW; C9C05F21A3EE4CB7 CRC64;
MVVGDFAIET ETLVVGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV GCIPSKALIS
ASHRYEQAKH SEEMGIKAEN VTIDFAKVQE WKASVVKKLT GGVEGLLKGN KVEIVKGEAY
FVDANTVRVV NGDSAQTYTF KNAIIATGSR PIELPNFKFS NRILDSTGAL NLGEVPKSLV
VIGGGYIGIE LGTAYANFGT KVTILEGAGE ILSGFEKQMA AIIKKRLKKK GVEVVTNALA
KGAEEREDGV TVTYEANGET KTIDADYVLV TVGRRPNTDE LGLEQIGIKM TNRGLIEVDQ
QCRTSVPNIF AIGDIVPGPA LAHKASYEGK VAAEAIAGHP SAVDYVAIPA VVFSDPECAS
VGYFEQQAKD EGIDVIAAKF PFAANGRALA LNDTDGFLKL VVRKEDGVII GAQIIGPNAS
DMIAELGLAI EAGMTAEDIA LTIHAHPTLG EIAMEAAEVA LGTPIHIITK


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