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Protein

Dihydrolipoyl dehydrogenase

Gene

lpd

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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) (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)DescriptionActionsGraphical viewLength
Binding sitei54FADBy similarity1
Binding sitei117FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei205NADBy similarity1
Binding sitei238NAD; via amide nitrogenBy similarity1
Binding sitei313FADBy similarity1
Binding sitei321FAD; via amide nitrogenBy similarity1
Active sitei445Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 45FADBy similarity10
Nucleotide bindingi182 – 186NADBy similarity5
Nucleotide bindingi270 – 273NADBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

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 2-oxoglutarate dehydrogenase complex
Gene namesi
Name:lpd
Ordered Locus Names:VP2517
OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic identifieri223926 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000002493 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680531 – 475Dihydrolipoyl dehydrogenaseAdd BLAST475

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 50Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiO50286.

Interactioni

Protein-protein interaction databases

STRINGi223926.VP2517.

Structurei

3D structure databases

ProteinModelPortaliO50286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiCSDGMTK.

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.

O50286-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKEIKAQVV VLGSGPAGYS AAFRCADLGL ETVLVERYST LGGVCLNVGC
60 70 80 90 100
IPSKALLHVS KVIEEAKAMA DHGVVFGEPQ TDINKIRIWK EKVVNQLTGG
110 120 130 140 150
LSGMAKMRNV TVVNGYGKFT GPNSILVEGE GESTVVNFDN AIVAAGSRPI
160 170 180 190 200
KLPFIPHEDP RIWDSTDALE LKEVPEKLLI MGGGIIGLEM GTVYHSLGSK
210 220 230 240 250
VEVVEMFDQV IPAADKDIVK VYTKRIKDKF KLMLETKVTA VEAKEDGIYV
260 270 280 290 300
SMEGKKAPAE AERYDAVLVA IGRVPNGKLI DGEKAGLEID ERGFINVDKQ
310 320 330 340 350
MRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVISGKKH YFDPKVIPSI
360 370 380 390 400
AYTEPEVAWV GKTEKEAKAE GIKYEVATFP WAASGRAIAS DCSDGMTKLI
410 420 430 440 450
FDKETHRVIG GAIVGTNGGE LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE
460 470
SVGLAAEVFE GSITDLPNKK AVKKK
Length:475
Mass (Da):50,988
Last modified:April 4, 2003 - v2
Checksum:i67F6E3A8C28DFB44
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160P → S in AAC46405 (PubMed:9620967).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035967 Genomic DNA. Translation: AAC46405.1.
BA000031 Genomic DNA. Translation: BAC60780.1.
RefSeqiNP_798896.1. NC_004603.1.
WP_005479684.1. NC_004603.1.

Genome annotation databases

EnsemblBacteriaiBAC60780; BAC60780; BAC60780.
GeneIDi1190032.
KEGGivpa:VP2517.
PATRICi20143174. VBIVibPar50997_2414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035967 Genomic DNA. Translation: AAC46405.1.
BA000031 Genomic DNA. Translation: BAC60780.1.
RefSeqiNP_798896.1. NC_004603.1.
WP_005479684.1. NC_004603.1.

3D structure databases

ProteinModelPortaliO50286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi223926.VP2517.

Proteomic databases

PRIDEiO50286.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC60780; BAC60780; BAC60780.
GeneIDi1190032.
KEGGivpa:VP2517.
PATRICi20143174. VBIVibPar50997_2414.

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiCSDGMTK.

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...

Entry informationi

Entry nameiDLDH_VIBPA
AccessioniPrimary (citable) accession number: O50286
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 4, 2003
Last modified: November 2, 2016
This is version 121 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, 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.