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Q8K9T7 (DLDH_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase

EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
Gene names
Name:lpdA
Ordered Locus Names:BUsg_201
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond By similarity.

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

glycolytic process

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: UniProtKB-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 – 476476Dihydrolipoyl dehydrogenase
PRO_0000068020

Regions

Nucleotide binding36 – 4510FAD By similarity
Nucleotide binding182 – 1865NAD By similarity
Nucleotide binding271 – 2744NAD By similarity

Sites

Active site4461Proton 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 site3141FAD By similarity
Binding site3221FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond45 ↔ 50Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9T7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 2BCD5F1ECB08BA58

FASTA47652,187
        10         20         30         40         50         60 
MHQEIQSEVV IIGSGPAGYS AAFRCADLGL ETVLIEHQER LGGVCLNVGC IPSKSLLHIA 

        70         80         90        100        110        120 
KIIKDASELS ESGVFFNKPI IDIKKINNWK EKIIKKLTTG LSNMGEKRKV RIVQGKALFN 

       130        140        150        160        170        180 
TDHSVLVKNK KNDFTIFFKH AIIATGSKPI KIPSLPNEDN RIWNSTDALS LKSIPNRFLI 

       190        200        210        220        230        240 
IGGGIIGLEM ATIYSALGSK VDIVDRFNAF LPSVDKDITD IYIKSIKKRF KLLLNTHVKS 

       250        260        270        280        290        300 
VEKSKDNDLI VKIAEENSDE NVCCYDNILV AIGRSPNVDF LGLEKIGLKL NESGFIEINQ 

       310        320        330        340        350        360 
QLKTNISHIY AIGDVTGFPM LAHKAVQQAH IAAEVISGKK HYFEPKVIPS VAYTDPEIAW 

       370        380        390        400        410        420 
VGLSEKEAEN NDIDYEVSLF PWSASGRAHA SNCTLGMTKL IFNKNTNKII GGSIIGTNAS 

       430        440        450        460        470 
ELISEIGLAI EMGSDAEDIS LTIHPHPTLS ESISLASEVF QGTITDLLNL KKSLLN 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67765.1.
RefSeqNP_660554.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9T7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67765; AAM67765; BUsg_201.
GeneID1005398.
KEGGbas:BUsg201.
PATRIC21247189. VBIBucAph100086_0208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1249.
KOK00382.
OMAIWNSTDA.
OrthoDBEOG6QCD6D.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-211-MONOMER.

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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH_BUCAP
AccessionPrimary (citable) accession number: Q8K9T7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 92 of the entry and version 1 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names