DLDH_AZOVI
ID DLDH_AZOVI Reviewed; 477 AA.
AC P18925;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
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 pyruvate complex;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832161; DOI=10.1111/j.1432-1033.1988.tb13887.x;
RA Westphal A.H., de Kok A.;
RT "Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning,
RT organization and sequence analysis of the gene.";
RL Eur. J. Biochem. 172:299-305(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, AND DISULFIDE BOND.
RX PubMed=2404760; DOI=10.1111/j.1432-1033.1990.tb15300.x;
RA Westphal A.H., de Kok A.;
RT "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2.
RT Molecular cloning and sequence analysis of the gene encoding the
RT succinyltransferase component.";
RL Eur. J. Biochem. 187:235-239(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=1880807; DOI=10.1016/0022-2836(91)90367-f;
RA Mattevi A., Schierbeek A.J., Hol W.G.J.;
RT "Refined crystal structure of lipoamide dehydrogenase from Azotobacter
RT vinelandii at 2.2-A resolution. A comparison with the structure of
RT glutathione reductase.";
RL J. Mol. Biol. 220:975-994(1991).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (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:1880807}.
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; M37307; AAA22139.1; -; Genomic_DNA.
DR EMBL; X52432; CAA36679.1; -; Genomic_DNA.
DR PIR; S00360; DEAVHL.
DR RefSeq; WP_012701528.1; NZ_FPKM01000019.1.
DR PDB; 3LAD; X-ray; 2.20 A; A/B=2-477.
DR PDBsum; 3LAD; -.
DR AlphaFoldDB; P18925; -.
DR SMR; P18925; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR PRIDE; P18925; -.
DR OMA; DAKYGEW; -.
DR SABIO-RK; P18925; -.
DR EvolutionaryTrace; P18925; -.
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; Disulfide bond; FAD; Flavoprotein; Glycolysis;
KW NAD; Oxidoreductase; Redox-active center.
FT CHAIN 1..477
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068014"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT BINDING 34..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1880807"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1880807"
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:0000269|PubMed:1880807"
FT BINDING 327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1880807"
FT DISULFID 49..54
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:1880807,
FT ECO:0000269|PubMed:2404760"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 88..113
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 206..217
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 255..275
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 327..343
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 370..375
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3LAD"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:3LAD"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:3LAD"
FT HELIX 455..465
FT /evidence="ECO:0007829|PDB:3LAD"
SQ SEQUENCE 477 AA; 49567 MW; 4219A8EA4DAFCAD0 CRC64;
MSQKFDVIVI GAGPGGYVAA IKSAQLGLKT ALIEKYKGKE GKTALGGTCL NVGCIPSKAL
LDSSYKFHEA HESFKLHGIS TGEVAIDVPT MIARKDQIVR NLTGGVASLI KANGVTLFEG
HGKLLAGKKV EVTAADGSSQ VLDTENVILA SGSKPVEIPP APVDQDVIVD STGALDFQNV
PGKLGVIGAG VIGLELGSVW ARLGAEVTVL EAMDKFLPAV DEQVAKEAQK ILTKQGLKIL
LGARVTGTEV KNKQVTVKFV DAEGEKSQAF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF
IYVDDYCATS VPGVYAIGDV VRGAMLAHKA SEEGVVVAER IAGHKAQMNY DLIPAVIYTH
PEIAGVGKTE QALKAEGVAI NVGVFPFAAS GRAMAANDTA GFVKVIADAK TDRVLGVHVI
GPSAAELVQQ GAIAMEFGTS AEDLGMMVFA HPALSEALHE AALAVSGHAI HVANRKK
