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Q89AQ9 (ODP2_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:bbp_190
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length410 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 AAO26922.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

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 – 410410Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162277

Regions

Domain1 – 6868Lipoyl-binding

Sites

Active site3831 Potential

Amino acid modifications

Modified residue351N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89AQ9 [UniParc].

Last modified June 16, 2003. Version 1.
Checksum: 69EF982E6C212730

FASTA41046,119
        10         20         30         40         50         60 
MPDIGTDLVE VIEILVKIGD QVKKDDSLIT VEGQKASIEI PASHTGTIKN IIVHIGEKIT 

        70         80         90        100        110        120 
TGSLIAILNG IDDNVKSKND SSSYSFKNSK NTSTNSNLGN VNNNINNRTI LVHATPTVRR 

       130        140        150        160        170        180 
LARKFDIKLE NITGTGRKGR ILKEDVISYK NISLFNDIKK SLKKTNVNYY KDNVTCDDFK 

       190        200        210        220        230        240 
SIELTRTQIR SSKNLLKSWL TIPHVTQFDE SDITELENFR QKYNSDLKDK SKKLTILIFV 

       250        260        270        280        290        300 
IKAVSKALEM FPKFNGRLIN KDNRIAIVLN EHINIGIVVD TDDGLLVPVI NRVNKKNISS 

       310        320        330        340        350        360 
ISNDLRIISE RARSRKLNFS DIKEYGSFTI SNLGGIGGTN FTPIIKYPEL AILGISRALI 

       370        380        390        400        410 
KPYWNSHAFI PKLMLPLSLS YDHRAIDGVA AVRFITFVKK MLTDIRFLMI 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26922.1. Different initiation.
RefSeqNP_777817.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AQ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp190.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26922; AAO26922; bbp_190.
GeneID1058122.
KEGGbab:bbp190.
PATRIC21245155. VBIBucAph80364_0184.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
KOK00627.
OMAFWHVSEG.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-190-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_BUCBP
AccessionPrimary (citable) accession number: Q89AQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: June 11, 2014
This is version 78 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