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Reviewed, UniProtKB/Swiss-Prot P18925 (DLDH_AZOVI)

Last modified February 9, 2010. Version 92. 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
    E3 component of pyruvate complex
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter

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Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (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.

Subunit structure

Homodimer.

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
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 – 477477Dihydrolipoyl dehydrogenase
PRO_0000068014

Regions

Nucleotide binding34 – 4916FAD
Nucleotide binding188 – 1925NAD By similarity
Nucleotide binding276 – 2794NAD By similarity

Sites

Active site4511Proton acceptor
Binding site581FAD
Binding site1221FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2111NAD By similarity
Binding site2451NAD; via amide nitrogen By similarity
Binding site3191FAD
Binding site3271FAD; via amide nitrogen

Amino acid modifications

Disulfide bond49 ↔ 54Redox-active Ref.2 Ref.3

Secondary structure

1 ........................................................................... 477
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P18925-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 4219A8EA4DAFCAD0

FASTA47749,567
        10         20         30         40         50         60 
MSQKFDVIVI GAGPGGYVAA IKSAQLGLKT ALIEKYKGKE GKTALGGTCL NVGCIPSKAL 

        70         80         90        100        110        120 
LDSSYKFHEA HESFKLHGIS TGEVAIDVPT MIARKDQIVR NLTGGVASLI KANGVTLFEG 

       130        140        150        160        170        180 
HGKLLAGKKV EVTAADGSSQ VLDTENVILA SGSKPVEIPP APVDQDVIVD STGALDFQNV 

       190        200        210        220        230        240 
PGKLGVIGAG VIGLELGSVW ARLGAEVTVL EAMDKFLPAV DEQVAKEAQK ILTKQGLKIL 

       250        260        270        280        290        300 
LGARVTGTEV KNKQVTVKFV DAEGEKSQAF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF 

       310        320        330        340        350        360 
IYVDDYCATS VPGVYAIGDV VRGAMLAHKA SEEGVVVAER IAGHKAQMNY DLIPAVIYTH 

       370        380        390        400        410        420 
PEIAGVGKTE QALKAEGVAI NVGVFPFAAS GRAMAANDTA GFVKVIADAK TDRVLGVHVI 

       430        440        450        460        470 
GPSAAELVQQ GAIAMEFGTS AEDLGMMVFA HPALSEALHE AALAVSGHAI HVANRKK

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References

[1]"Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene."
Westphal A.H., de Kok A.
Eur. J. Biochem. 172:299-305(1988) [PubMed: 2832161] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component."
Westphal A.H., de Kok A.
Eur. J. Biochem. 187:235-239(1990) [PubMed: 2404760] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, DISULFIDE BOND.
[3]"Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2-A resolution. A comparison with the structure of glutathione reductase."
Mattevi A., Schierbeek A.J., Hol W.G.J.
J. Mol. Biol. 220:975-994(1991) [PubMed: 1880807] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FAD.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M37307 Genomic DNA. Translation: AAA22139.1.
X52432 Genomic DNA. Translation: CAA36679.1.
PIRDEAVHL. S00360.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LADX-ray2.20A/B2-477[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.4. 883.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. 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. 2 hits.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDLDH_AZOVI
AccessionPrimary (citable) accession number: P18925
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 9, 2010
This is version 92 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