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O50286 (DLDH_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 2-oxoglutarate dehydrogenase complex
Gene names
Name:lpd
Ordered Locus Names:VP2517
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

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

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Dihydrolipoyl dehydrogenase
PRO_0000068053

Regions

Nucleotide binding36 – 4510FAD By similarity
Nucleotide binding182 – 1865NAD By similarity
Nucleotide binding270 – 2734NAD By similarity

Sites

Active site4451Proton acceptor By similarity
Binding site541FAD By similarity
Binding site1171FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2051NAD By similarity
Binding site2381NAD; via amide nitrogen By similarity
Binding site3131FAD By similarity
Binding site3211FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond45 ↔ 50Redox-active By similarity

Experimental info

Sequence conflict1601P → S in AAC46405. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O50286 [UniParc].

Last modified April 4, 2003. Version 2.
Checksum: 67F6E3A8C28DFB44

FASTA47550,988
        10         20         30         40         50         60 
MSKEIKAQVV VLGSGPAGYS AAFRCADLGL ETVLVERYST LGGVCLNVGC IPSKALLHVS 

        70         80         90        100        110        120 
KVIEEAKAMA DHGVVFGEPQ TDINKIRIWK EKVVNQLTGG LSGMAKMRNV TVVNGYGKFT 

       130        140        150        160        170        180 
GPNSILVEGE GESTVVNFDN AIVAAGSRPI KLPFIPHEDP RIWDSTDALE LKEVPEKLLI 

       190        200        210        220        230        240 
MGGGIIGLEM GTVYHSLGSK VEVVEMFDQV IPAADKDIVK VYTKRIKDKF KLMLETKVTA 

       250        260        270        280        290        300 
VEAKEDGIYV SMEGKKAPAE AERYDAVLVA IGRVPNGKLI DGEKAGLEID ERGFINVDKQ 

       310        320        330        340        350        360 
MRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVISGKKH YFDPKVIPSI AYTEPEVAWV 

       370        380        390        400        410        420 
GKTEKEAKAE GIKYEVATFP WAASGRAIAS DCSDGMTKLI FDKETHRVIG GAIVGTNGGE 

       430        440        450        460        470 
LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNKK AVKKK

« Hide

References

« Hide 'large scale' references
[1]"OpaR, a homolog of Vibrio harveyi LuxR, controls opacity of Vibrio parahaemolyticus."
McCarter L.L.
J. Bacteriol. 180:3166-3173(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BB22.
[2]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF035967 Genomic DNA. Translation: AAC46405.1.
BA000031 Genomic DNA. Translation: BAC60780.1.
RefSeqNP_798896.1. NC_004603.1.

3D structure databases

ProteinModelPortalO50286.
SMRO50286. Positions 19-470.
ModBaseSearch...

Protein-protein interaction databases

STRING223926.VP2517.

Proteomic databases

PRIDEO50286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60780; BAC60780; BAC60780.
GeneID1190032.
KEGGvpa:VP2517.
PATRIC20143174. VBIVibPar50997_2414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
KOK00382.
OMAGMAAEIY.
ProtClustDBPRK06467.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PANTHERPTHR22912:SF20. PTHR22912:SF20. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH_VIBPA
AccessionPrimary (citable) accession number: O50286
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 4, 2003
Last modified: May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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