Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P14218 (DLDH_PSEFL)

Last modified June 16, 2009. Version 90. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of 2-oxoglutarate dehydrogenase complex
Gene names
Name: lpd
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Hide | Top

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

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.

Subunit structure

Homodimer. Ref.2

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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 478477Dihydrolipoyl dehydrogenase
PRO_0000068037

Regions

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

Sites

Active site4511Proton acceptor By similarity
Binding site581FAD
Binding site1221FAD; via amide nitrogen and carbonyl oxygen
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

Secondary structure

1 ........................................................................................ 478
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P14218-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B23EB31268C69EC7

FASTA47850,151
        10         20         30         40         50         60 
MSQKFDVVVI GAGPGGYVAA IRAAQLGLKT ACIEKYIGKE GKVALGGTCL NVGCIPSKAL 

        70         80         90        100        110        120 
LDSSYKYHEA KEAFKVHGIE AKGVTIDVPA MVARKANIVK NLTGGIATLF KANGVTSFEG 

       130        140        150        160        170        180 
HGKLLANKQV EVTGLDGKTQ VLEAENVIIA SGSRPVEIPP APLSDDIIVD STGALEFQAV 

       190        200        210        220        230        240 
PKKLGVIGAG VIGLELGSVW ARLGAEVTVL EALDKFLPAA DEQIAKEALK VLTKQGLNIR 

       250        260        270        280        290        300 
LGARVTASEV KKKQVTVTFT DANGEQKETF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF 

       310        320        330        340        350        360 
IYVDDHCKTS VPGVFAIGDV VRGAMLAHKA SEEGVMVAER IAGHKAQMNY DLIPSVIYTH 

       370        380        390        400        410        420 
PEIAWVGKTE QTLKAEGVEV NVGTFPFAAS GRAMAANDTT GLVKVIADAK TDRVLGVHVI 

       430        440        450        460        470 
GPSAAELVQQ GAIGMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGHAI HIANRKKR

« Hide

Hide | Top

References

[1]"Molecular cloning and sequence determination of the lpd gene encoding lipoamide dehydrogenase from Pseudomonas fluorescens."
Benen J.A.E., van Berkel W.J.H., van Dongen W.M.A.M., Mueller F., de Kok A.
J. Gen. Microbiol. 135:1787-1797(1989) [PubMed: 2515251] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-23.
[2]"Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8-A resolution. Analysis of redox and thermostability properties."
Mattevi A., Obmolova G., Kalk K.H., van Berkel W.J.H., Hol W.G.J.
J. Mol. Biol. 230:1200-1215(1993) [PubMed: 8487301] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT, DISULFIDE BOND.

Hide | Top

Cross-references

Sequence databases

M28356 Genomic DNA. Translation: AAA99234.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LPFX-ray2.80A/B2-478[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.4. 329.

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...

Hide | Top

Entry information

Entry nameDLDH_PSEFL
AccessionPrimary (citable) accession number: P14218
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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