DLDH1_PSEPU
ID DLDH1_PSEPU Reviewed; 459 AA.
AC P09063;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of branched-chain alpha-keto acid dehydrogenase complex;
DE AltName: Full=LPD-Val;
GN Name=lpdV;
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=3046941; DOI=10.1111/j.1432-1033.1988.tb14264.x;
RA Burns G., Brown T., Hatter K., Sokatch J.R.;
RT "Comparison of the amino acid sequences of the transacylase components of
RT branched chain oxoacid dehydrogenase of Pseudomonas putida, and the
RT pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli.";
RL Eur. J. Biochem. 176:165-169(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=G2;
RX PubMed=2917566; DOI=10.1111/j.1432-1033.1989.tb14521.x;
RA Burns G., Brown T., Hatter K., Sokatch J.R.;
RT "Sequence analysis of the lpdV gene for lipoamide dehydrogenase of
RT branched-chain-oxoacid dehydrogenase of Pseudomonas putida.";
RL Eur. J. Biochem. 179:61-69(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH NAD AND FAD,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=1325638; DOI=10.1002/prot.340130406;
RA Mattevi A., Obmolova G., Sokatsch J.R., Betzel C., Hol W.G.J.;
RT "The refined crystal structure of Pseudomonas putida lipoamide
RT dehydrogenase complexed with NAD+ at 2.45-A resolution.";
RL Proteins 13:336-351(1992).
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; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1325638}.
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; M57613; AAA65618.1; -; Genomic_DNA.
DR PIR; S02139; DEPSLP.
DR RefSeq; WP_027609417.1; NZ_AP022324.1.
DR PDB; 1LVL; X-ray; 2.45 A; A=2-459.
DR PDBsum; 1LVL; -.
DR AlphaFoldDB; P09063; -.
DR SMR; P09063; -.
DR STRING; 1240350.AMZE01000027_gene4715; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR GeneID; 66677014; -.
DR eggNOG; COG1249; Bacteria.
DR EvolutionaryTrace; P09063; -.
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 CHAIN 1..459
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068038"
FT ACT_SITE 438
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 36..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 179..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 264..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:1325638"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:1325638"
FT DISULFID 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:1325638"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 85..109
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 346..354
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:1LVL"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:1LVL"
FT STRAND 400..408
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:1LVL"
FT HELIX 443..452
FT /evidence="ECO:0007829|PDB:1LVL"
SQ SEQUENCE 459 AA; 48159 MW; 3D60A7DE167D0586 CRC64;
MQQTIQTTLL IIGGGPGGYV AAIRAGQLGI PTVLVEGQAL GGTCLNIGCI PSKALIHVAE
QFHQASRFTE PSPLGISVAS PRLDIGQSVA WKDGIVDRLT TGVAALLKKH GVKVVHGWAK
VLDGKQVEVD GQRIQCEHLL LATGSSSVEL PMLPLGGPVI SSTEALAPKA LPQHLVVVGG
GYIGLELGIA YRKLGAQVSV VEARERILPT YDSELTAPVA ESLKKLGIAL HLGHSVEGYE
NGCLLANDGK GGQLRLEADR VLVAVGRRPR TKGFNLECLD LKMNGAAIAI DERCQTSMHN
VWAIGDVAGE PMLAHRAMAQ GEMVAEIIAG KARRFEPAAI AAVCFTDPEV VVVGKTPEQA
SQQGLDCIVA QFPFAANGRA MSLESKSGFV RVVARRDNHL ILGWQAVGVA VSELSTAFAQ
SLEMGACLED VAGTIHAHPT LGEAVQEAAL RALGHALHI
