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Protein

Dihydrolipoyl dehydrogenase

Gene

lpd

Organism
Mycobacterium leprae (strain TN)
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. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes (By similarity).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 sitei50 – 501FADBy similarity
Binding sitei113 – 1131FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei204 – 2041NADBy similarity
Binding sitei312 – 3121FADBy similarity
Binding sitei320 – 3201FAD; via amide nitrogenBy similarity
Active sitei446 – 4461Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 419FADBy similarity
Nucleotide bindingi181 – 1855NADBy similarity
Nucleotide bindingi269 – 2724NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of alpha-ketoacid dehydrogenase complexes
Gene namesi
Name:lpd
Ordered Locus Names:ML2387
ORF Names:u1740l
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML2387.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Dihydrolipoyl dehydrogenasePRO_0000068033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 46Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer. Part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3), and of the BCKADH complex, consisting of multiple copies of BkdA/BkdB (E1), BkdC (E2) and Lpd (E3).By similarity

Protein-protein interaction databases

STRINGi272631.ML2387.

Structurei

3D structure databases

ProteinModelPortaliQ50068.
SMRiQ50068. Positions 1-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

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

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 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.

Q50068-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHYDVVVLG AGPGGYVAAI RAAQLGLSTA VVEPKYWGGI CLNVGCIPSK
60 70 80 90 100
VLLHNAELAH IFTKEAKTFG ISGDASFDYG IAYDRSRKVS EGRVAGVHFL
110 120 130 140 150
MKKNKITEIH GYGRFTDANT LSVELSEGVP ETPLKVTFNN VIIATGSKTR
160 170 180 190 200
LVPGTLLSTN VITYEEQILT RELPDSIVIV GAGAIGIEFG YVLKNYGVDV
210 220 230 240 250
TIVEFLPRAM PNEDAEVSKE IEKQFKKMGI KILTGTKVES ISDNGSHVLV
260 270 280 290 300
AVSKDGQFQE LKADKVLQAI GFAPNVDGYG LDKVGVALTA DKAVDIDDYM
310 320 330 340 350
QTNVSHIYAI GDVTGKLQLA HVAEAQGVVA AEAIAGAETL ALSDYRMMPR
360 370 380 390 400
ATFCQPNVAS FGLTEQQARD GGYDVVVAKF PFTANAKAHG MGDPSGFVKL
410 420 430 440 450
VADAKYGELL GGHMIGHNVS ELLPELTLAQ KWDLTATELV RNVHTHPTLS
460
EALQECFHGL IGHMINF
Length:467
Mass (Da):50,077
Last modified:November 1, 1996 - v1
Checksum:iCA46B807119FC15A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15183 Genomic DNA. Translation: AAA63016.1.
AL583925 Genomic DNA. Translation: CAC31903.1.
PIRiG87207.
RefSeqiNP_302544.1. NC_002677.1.
WP_010908864.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31903; CAC31903; CAC31903.
GeneIDi908174.
KEGGimle:ML2387.
PATRICi18059357. VBIMycLep78757_4593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15183 Genomic DNA. Translation: AAA63016.1.
AL583925 Genomic DNA. Translation: CAC31903.1.
PIRiG87207.
RefSeqiNP_302544.1. NC_002677.1.
WP_010908864.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ50068.
SMRiQ50068. Positions 1-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML2387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC31903; CAC31903; CAC31903.
GeneIDi908174.
KEGGimle:ML2387.
PATRICi18059357. VBIMycLep78757_4593.

Organism-specific databases

LepromaiML2387.

Phylogenomic databases

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

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 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. Smith D.R., Robison K.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiDLDH_MYCLE
AccessioniPrimary (citable) accession number: Q50068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 127 of the entry and version 1 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, Reference 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.