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Protein

Dihydrolipoyl dehydrogenase

Gene

lpd

Organism
Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571FADBy similarity
Binding sitei120 – 1201FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei209 – 2091NADBy similarity
Binding sitei317 – 3171FADBy similarity
Binding sitei325 – 3251FAD; via amide nitrogenBy similarity
Active sitei450 – 4501Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489FADBy similarity
Nucleotide bindingi186 – 1905NADBy similarity
Nucleotide bindingi275 – 2784NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciCPAR517417:GH95-750-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
Gene namesi
Name:lpd
Ordered Locus Names:Cpar_0724
OrganismiChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
Taxonomic identifieri517417 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000008811 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Dihydrolipoyl dehydrogenasePRO_0000068023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 53Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi517417.Cpar_0724.

Structurei

3D structure databases

ProteinModelPortaliO50311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiCHMIGAG.
OrthoDBiEOG6QCD6D.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O50311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQSESSSAQ FDVAVIGSGP GGYEAALHAA RHGMKVCLVE KASLGGVCVN
60 70 80 90 100
WGCIPTKALL RSAEVYDLAK NPSEFGVNVS ELSFDLAQAV KRSRKVSLKS
110 120 130 140 150
SKGVEFMLKK AKVEVWRGEA VLTGSKGVKV TAEDGSERSL EAANIIVATG
160 170 180 190 200
AQPRVIPGLE PDGKKIITSR EALILKDVPE SMIVVGGGAI GVEMAWFYAK
210 220 230 240 250
AGAKVTIVEL MPRLLPAEEA EVSEALKRSF EKVDITVQCG AKLGNVAISE
260 270 280 290 300
FGVNADLLAE GKEPQKIEAS CMLVAVGVTG VIDGLGLDAA GIETERGFIR
310 320 330 340 350
TDELCRTSAS GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKLPEPLSEP
360 370 380 390 400
LIPRCVYAQP SVASVGLTEE AAIAAGYKVL VGRSQFAASG KANAYGQLEG
410 420 430 440 450
FVKLVFNAET GKMLGGHLIG HDAVELIGEL GLACRYGVTA EGLVGTVHAH
460
PTLSETVREA AFAALQSKG
Length:469
Mass (Da):48,755
Last modified:October 14, 2008 - v2
Checksum:i97FDD6D88E8249F8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421A → R in CAB06298 (Ref. 1) Curated
Sequence conflicti463 – 4631A → S in CAB06298 (Ref. 1) Curated
Sequence conflicti466 – 4672QS → PN in CAB06298 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z83933 Genomic DNA. Translation: CAB06298.1.
CP001099 Genomic DNA. Translation: ACF11143.1.
PIRiT17191.
RefSeqiWP_012501976.1. NC_011027.1.

Genome annotation databases

EnsemblBacteriaiACF11143; ACF11143; Cpar_0724.
KEGGicpc:Cpar_0724.
PATRICi21364702. VBIChlPar72705_0724.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z83933 Genomic DNA. Translation: CAB06298.1.
CP001099 Genomic DNA. Translation: ACF11143.1.
PIRiT17191.
RefSeqiWP_012501976.1. NC_011027.1.

3D structure databases

ProteinModelPortaliO50311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi517417.Cpar_0724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF11143; ACF11143; Cpar_0724.
KEGGicpc:Cpar_0724.
PATRICi21364702. VBIChlPar72705_0724.

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiCHMIGAG.
OrthoDBiEOG6QCD6D.

Enzyme and pathway databases

BioCyciCPAR517417:GH95-750-MONOMER.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCIB 8327.

Entry informationi

Entry nameiDLDH_CHLP8
AccessioniPrimary (citable) accession number: O50311
Secondary accession number(s): B3QMJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 14, 2008
Last modified: November 11, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.