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Q59638 (ODP2_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. 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
Synonyms:aceB
Ordered Locus Names:PA5016
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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).

Catalytic activity

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

Cofactor

Binds 2 lipoyl cofactors covalently By similarity.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 2 lipoyl-binding domains.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentpyruvate dehydrogenase complex

Inferred from electronic annotation. Source: InterPro

   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 – 547547Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162283

Regions

Domain1 – 7474Lipoyl-binding 1
Domain120 – 19273Lipoyl-binding 2

Sites

Active site5201 Potential

Amino acid modifications

Modified residue411N6-lipoyllysine By similarity
Modified residue1591N6-lipoyllysine By similarity

Experimental info

Sequence conflict2251A → V in AAC45354. Ref.1
Sequence conflict295 – 3017GGAGATG → AVPAPR in AAC45354. Ref.1
Sequence conflict328 – 3292MQ → IE in AAC45354. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59638 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: 24E15CCC9A590CB4

FASTA54756,709
        10         20         30         40         50         60 
MSELIRVPDI GNGEGEVIEL LVKPGDKVEA DQSLLTLESD KASMEIPSPK AGVVKSIKAK 

        70         80         90        100        110        120 
VGDTLKEGDE ILELEVEGGE QPAEAKAEAA PAQPEAPKAE APAPAPSESK PAAPAAASVQ 

       130        140        150        160        170        180 
DIKVPDIGSA GKANVIEVMV KAGDTVEADQ SLITLESDKA SMEIPSPASG VVESVSIKVG 

       190        200        210        220        230        240 
DEVGTGDLIL KLKVEGAAPA AEEQPAAAPA QAAAPAAEQK PAAAAPAPAK ADTPAPVGAP 

       250        260        270        280        290        300 
SRDGAKVHAG PAVRMLAREF GVELSEVKAS GPKGRILKED VQVFVKEQLQ RAKSGGAGAT 

       310        320        330        340        350        360 
GGAGIPPIPE VDFSKFGEVE EVAMTRLMQV GAANLHRSWL NVPHVTQFDQ SDITDMEAFR 

       370        380        390        400        410        420 
VAQKAAAEKA GVKLTVLPIL LKACAHLLKE LPDFNSSLAP SGKALIRKKY VHIGFAVDTP 

       430        440        450        460        470        480 
DGLLVPVIRD VDRKSLLQLA AEAADLADKA RNKKLSADAM QGACFTISSL GHIGGTGFTP 

       490        500        510        520        530        540 
IVNAPEVAIL GVSKATMQPV WDGKAFQPRL MLPLSLSYDH RVINGAAAAR FTKRLGELLA 


DIRTLLL 

« Hide

References

« Hide 'large scale' references
[1]"Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa."
Rae J.L., Cutfield J.F., Lamont I.L.
J. Bacteriol. 179:3561-3571(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PAO.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U47920 Genomic DNA. Translation: AAC45354.1.
AE004091 Genomic DNA. Translation: AAG08401.1.
PIRH83018.
RefSeqNP_253703.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ59638.
SMRQ59638. Positions 2-81, 119-198, 305-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA5016.

2D gel databases

World-2DPAGE0008:Q59638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG08401; AAG08401; PA5016.
GeneID881297.
KEGGpae:PA5016.
PATRIC19844857. VBIPseAer58763_5257.

Organism-specific databases

PseudoCAPPA5016.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281562.
KOK00627.
OMATEIMVAV.
PhylomeDBQ59638.

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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_PSEAE
AccessionPrimary (citable) accession number: Q59638
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: July 9, 2014
This is version 105 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