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Reviewed, UniProtKB/Swiss-Prot O50311 (DLDH_CHLP8)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 and 2-oxoglutarate dehydrogenases complexes
Gene names
Name: lpd
Ordered Locus Names: Cpar_0724
OrganismChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327)) [Complete proteome] [HAMAP]
Taxonomic identifier517417 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

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Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

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

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 By similarity.

Subcellular location

Cytoplasm Potential.

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 termComplete proteome
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 – 469469Dihydrolipoyl dehydrogenase
PRO_0000068023

Regions

Nucleotide binding40 – 489FAD By similarity
Nucleotide binding186 – 1905NAD By similarity
Nucleotide binding275 – 2784NAD By similarity

Sites

Active site4501Proton acceptor By similarity
Binding site571FAD By similarity
Binding site1201FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2091NAD By similarity
Binding site3171FAD By similarity
Binding site3251FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond48 ↔ 53Redox-active By similarity

Experimental info

Sequence conflict421A → R in CAB06298. Ref.1
Sequence conflict4631A → S in CAB06298. Ref.1
Sequence conflict466 – 4672QS → PN in CAB06298. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
O50311-1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 97FDD6D88E8249F8

FASTA46948,755
        10         20         30         40         50         60 
MQQSESSSAQ FDVAVIGSGP GGYEAALHAA RHGMKVCLVE KASLGGVCVN WGCIPTKALL 

        70         80         90        100        110        120 
RSAEVYDLAK NPSEFGVNVS ELSFDLAQAV KRSRKVSLKS SKGVEFMLKK AKVEVWRGEA 

       130        140        150        160        170        180 
VLTGSKGVKV TAEDGSERSL EAANIIVATG AQPRVIPGLE PDGKKIITSR EALILKDVPE 

       190        200        210        220        230        240 
SMIVVGGGAI GVEMAWFYAK AGAKVTIVEL MPRLLPAEEA EVSEALKRSF EKVDITVQCG 

       250        260        270        280        290        300 
AKLGNVAISE FGVNADLLAE GKEPQKIEAS CMLVAVGVTG VIDGLGLDAA GIETERGFIR 

       310        320        330        340        350        360 
TDELCRTSAS GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKLPEPLSEP LIPRCVYAQP 

       370        380        390        400        410        420 
SVASVGLTEE AAIAAGYKVL VGRSQFAASG KANAYGQLEG FVKLVFNAET GKMLGGHLIG 

       430        440        450        460 
HDAVELIGEL GLACRYGVTA EGLVGTVHAH PTLSETVREA AFAALQSKG

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References

« Hide 'large scale' references
[1]"Clustering of genes with function in the biosynthesis of bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium vibrioforme."
Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.
Hereditas 125:93-96(1996)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Chlorobaculum parvum NCIB 8327."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

Z83933 Genomic DNA. Translation: CAB06298.1.
CP001099 Genomic DNA. Translation: ACF11143.1.
PIRT17191.
RefSeqYP_001998343.1.

3D structure databases

HSSPHSSP built from PDB template 1EBD based on UniProtKB P11959.
ModBaseSearch...

Genome annotation databases

GeneID6419649.
GenomeReviewsGene locus Cpar_0724 in contig CP001099_GR.
KEGGcpc:Cpar_0724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAO50311. GMLLAHK.

Enzyme and pathway databases

BRENDA1.8.1.4. 190276.

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]
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 nameDLDH_CHLP8
AccessionPrimary (citable) accession number: O50311
Secondary accession number(s): B3QMJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 14, 2008
Last modified: June 16, 2009
This is version 68 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

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