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Reviewed, UniProtKB/Swiss-Prot P11959 (DLDH1_BACST)

Last modified June 16, 2009. Version 93. 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
Gene names
Name: pdhD
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homodimer. Identified in a complex with pdhC. Ref.4

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 – 470470Dihydrolipoyl dehydrogenase
PRO_0000068015

Regions

Nucleotide binding39 – 479FAD
Nucleotide binding183 – 1875NAD By similarity
Nucleotide binding271 – 2744NAD By similarity

Sites

Active site4461Proton acceptor By similarity
Binding site561FAD
Binding site1191FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2061NAD By similarity
Binding site3141FAD
Binding site3221FAD; via amide nitrogen

Amino acid modifications

Disulfide bond47 ↔ 52Redox-active By similarity

Secondary structure

1 ................................................................................. 470
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P11959-1 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: C9C05F21A3EE4CB7

FASTA47049,356
        10         20         30         40         50         60 
MVVGDFAIET ETLVVGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV GCIPSKALIS 

        70         80         90        100        110        120 
ASHRYEQAKH SEEMGIKAEN VTIDFAKVQE WKASVVKKLT GGVEGLLKGN KVEIVKGEAY 

       130        140        150        160        170        180 
FVDANTVRVV NGDSAQTYTF KNAIIATGSR PIELPNFKFS NRILDSTGAL NLGEVPKSLV 

       190        200        210        220        230        240 
VIGGGYIGIE LGTAYANFGT KVTILEGAGE ILSGFEKQMA AIIKKRLKKK GVEVVTNALA 

       250        260        270        280        290        300 
KGAEEREDGV TVTYEANGET KTIDADYVLV TVGRRPNTDE LGLEQIGIKM TNRGLIEVDQ 

       310        320        330        340        350        360 
QCRTSVPNIF AIGDIVPGPA LAHKASYEGK VAAEAIAGHP SAVDYVAIPA VVFSDPECAS 

       370        380        390        400        410        420 
VGYFEQQAKD EGIDVIAAKF PFAANGRALA LNDTDGFLKL VVRKEDGVII GAQIIGPNAS 

       430        440        450        460        470 
DMIAELGLAI EAGMTAEDIA LTIHAHPTLG EIAMEAAEVA LGTPIHIITK

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References

[1]"Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
Hawkins C.F., Borges A., Perham R.N.
Eur. J. Biochem. 191:337-346(1990) [PubMed: 2200674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]"Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
Borges A., Hawkins C.F., Packman L.C., Perham R.N.
Eur. J. Biochem. 194:95-102(1990) [PubMed: 2253629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[3]"An amino acid sequence in the active site of lipoamide dehydrogenase from Bacillus stearothermophilus."
Packman L.C., Perham R.N.
FEBS Lett. 139:155-158(1982) [PubMed: 6896188] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-56.
[4]"Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase."
Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J.
Structure 4:277-286(1996) [PubMed: 8805537] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT.

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Cross-references

Sequence databases

X53560 Genomic DNA. Translation: CAA37631.1.
PIRS13839.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EBDX-ray2.60A/B7-461[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6155N.

Enzyme and pathway databases

BRENDA1.8.1.4. 266715.

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_BACST
AccessionPrimary (citable) accession number: P11959
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 93 of the entry and version 2 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