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Q8K9T8 (ODP2_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 80. 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:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
Gene names
Name:aceF
Ordered Locus Names:BUsg_200
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence caution

The sequence AAM67764.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162276

Regions

Domain1 – 6868Lipoyl-binding

Sites

Active site3751 Potential

Amino acid modifications

Modified residue351N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9T8 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: 1F784349E26E5643

FASTA40245,421
        10         20         30         40         50         60 
MPDIGLEEVE VTEILVKIGE EIKLDQGLIT VEGDKASMEI PSPISGIVKD ITIKIGEKVK 

        70         80         90        100        110        120 
TSSIIMIFKV NNLNSIKNEK DLNYIKTEKK LNENFLEEKK DIKKIVLVHA TPVVRRLARH 

       130        140        150        160        170        180 
LNVDLKNITP SGPKNRILKE DIELYIRNNT SNKSSFNIEK NNTTNFHKDL FNEIPITNIQ 

       190        200        210        220        230        240 
QIIGKNLHQN WVNIPHVTQF DEVNITLLEE FRHKYNTEKK QKNNMCSKIT ILPFIIKSVA 

       250        260        270        280        290        300 
YGLLEFPIFN SSLSVNKKTI FLKKYVNVGI AVDVQNALFV PVLKNVDKKN IANLSSELIF 

       310        320        330        340        350        360 
LSKKAHENKL DASDMKDGCF TISNLGGIGG SWFSPIINSP EVAILGVSKA LIKPLWNGKE 

       370        380        390        400 
FIPSLMLPLS LSYDHRVING ADAARFLTFI GKMLSDIRFL IM 

« 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: AAM67764.1. Different initiation.
RefSeqNP_660553.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9T8.
SMRQ8K9T8. Positions 1-70, 171-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67764; AAM67764; BUsg_200.
GeneID1005397.
KEGGbas:BUsg200.
PATRIC21247187. VBIBucAph100086_0207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
KOK00627.
OMACIINRIG.
OrthoDBEOG610413.
ProtClustDBPRK11856.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-210-MONOMER.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_BUCAP
AccessionPrimary (citable) accession number: Q8K9T8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 8, 2002
Last modified: November 13, 2013
This is version 80 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

Buchnera aphidicola (subsp. Schizaphis graminum)

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