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Reviewed, UniProtKB/Swiss-Prot P09063 (DLDH1_PSEPU)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    LPD-Val
    E3 component of branched-chain alpha-keto acid dehydrogenase complex
Gene names
Name: lpdV
OrganismPseudomonas putida
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. 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

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer. Ref.3

Subcellular location

Cytoplasm.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

dihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Dihydrolipoyl dehydrogenase
PRO_0000068038

Regions

Nucleotide binding36 – 449FAD
Nucleotide binding179 – 1835NAD
Nucleotide binding264 – 2674NAD

Sites

Active site4381Proton acceptor By similarity
Binding site531FAD
Binding site1191FAD; via amide nitrogen and carbonyl oxygen
Binding site1421FAD; via carbonyl oxygen
Binding site1821FAD
Binding site2021NAD
Binding site2361NAD; via amide nitrogen
Binding site3061FAD; via amide nitrogen
Binding site3121NAD; via carbonyl oxygen
Binding site3141FAD; via amide nitrogen

Amino acid modifications

Disulfide bond44 ↔ 49Redox-active Ref.3

Secondary structure

1 ................................................................................... 459
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P09063-1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 3D60A7DE167D0586

FASTA45948,159
        10         20         30         40         50         60 
MQQTIQTTLL IIGGGPGGYV AAIRAGQLGI PTVLVEGQAL GGTCLNIGCI PSKALIHVAE 

        70         80         90        100        110        120 
QFHQASRFTE PSPLGISVAS PRLDIGQSVA WKDGIVDRLT TGVAALLKKH GVKVVHGWAK 

       130        140        150        160        170        180 
VLDGKQVEVD GQRIQCEHLL LATGSSSVEL PMLPLGGPVI SSTEALAPKA LPQHLVVVGG 

       190        200        210        220        230        240 
GYIGLELGIA YRKLGAQVSV VEARERILPT YDSELTAPVA ESLKKLGIAL HLGHSVEGYE 

       250        260        270        280        290        300 
NGCLLANDGK GGQLRLEADR VLVAVGRRPR TKGFNLECLD LKMNGAAIAI DERCQTSMHN 

       310        320        330        340        350        360 
VWAIGDVAGE PMLAHRAMAQ GEMVAEIIAG KARRFEPAAI AAVCFTDPEV VVVGKTPEQA 

       370        380        390        400        410        420 
SQQGLDCIVA QFPFAANGRA MSLESKSGFV RVVARRDNHL ILGWQAVGVA VSELSTAFAQ 

       430        440        450 
SLEMGACLED VAGTIHAHPT LGEAVQEAAL RALGHALHI

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References

[1]"Comparison of the amino acid sequences of the transacylase components of branched chain oxoacid dehydrogenase of Pseudomonas putida, and the pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli."
Burns G., Brown T., Hatter K., Sokatch J.R.
Eur. J. Biochem. 176:165-169(1988) [PubMed: 3046941] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G2.
[2]"Sequence analysis of the lpdV gene for lipoamide dehydrogenase of branched-chain-oxoacid dehydrogenase of Pseudomonas putida."
Burns G., Brown T., Hatter K., Sokatch J.R.
Eur. J. Biochem. 179:61-69(1989) [PubMed: 2917566] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: G2.
[3]"The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45-A resolution."
Mattevi A., Obmolova G., Sokatsch J.R., Betzel C., Hol W.G.J.
Proteins 13:336-351(1992) [PubMed: 1325638] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH NAD AND FAD, SUBUNIT, DISULFIDE BOND.

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Cross-references

Sequence databases

M57613 Genomic DNA. Translation: AAA65618.1.
PIRDEPSLP. S02139.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LVLX-ray2.45A2-459[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.4. 403.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF20. Lipoamide_DH. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDLDH1_PSEPU
AccessionPrimary (citable) accession number: P09063
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 16, 2009
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents