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Reviewed, UniProtKB/Swiss-Prot O50286 (DLDH_VIBPA)

Last modified November 3, 2009. Version 76. 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 2-oxoglutarate dehydrogenase complex
Gene names
Name: lpd
Ordered Locus Names: VP2517
OrganismVibrio parahaemolyticus [Complete proteome] [HAMAP]
Taxonomic identifier670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

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Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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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

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Sequences

Sequence LengthMass (Da)Tools
O50286-1 [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

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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: 9620967] [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: 12620739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633 / Serotype O3:K6.

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Cross-references

Sequence databases

AF035967 Genomic DNA. Translation: AAC46405.1.
BA000031 Genomic DNA. Translation: BAC60780.1.
RefSeqNP_798896.1.

3D structure databases

HSSPHSSP built from PDB template 1OJT based on UniProtKB Q51225.
ModBaseSearch...

Genome annotation databases

GeneID1190032.
GenomeReviewsGene locus VP2517 in contig BA000031_GR.
KEGGvpa:VP2517.
NMPDRfig|223926.1.peg.2517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO50286.
OMAPFIPEDP.

Enzyme and pathway databases

BioCycVPAR223926:VP2517-MON.
BRENDA1.8.1.4. 3063.

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]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF20. Lipoamide_DH. 1 hit.
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_VIBPA
AccessionPrimary (citable) accession number: O50286
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 4, 2003
Last modified: November 3, 2009
This is version 76 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