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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 2 lipoyl cofactors covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei520 – 5201Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:aceF
Synonyms:aceB
Ordered Locus Names:PA5016
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5016.

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-lipoyllysinePROSITE-ProRule annotationBy similarity
Modified residuei159 – 1591N6-lipoyllysinePROSITE-ProRule annotationBy similarity

2D gel databases

World-2DPAGE0008:Q59638.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

STRINGi208964.PA5016.

Structurei

3D structure databases

SMRiQ59638. Positions 2-81, 119-198, 247-292, 305-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7574Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 19375Lipoyl-binding 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 2 lipoyl-binding domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
InParanoidiQ59638.
KOiK00627.
OMAiTEIMVAV.
PhylomeDBiQ59638.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELIRVPDI GNGEGEVIEL LVKPGDKVEA DQSLLTLESD KASMEIPSPK
60 70 80 90 100
AGVVKSIKAK VGDTLKEGDE ILELEVEGGE QPAEAKAEAA PAQPEAPKAE
110 120 130 140 150
APAPAPSESK PAAPAAASVQ DIKVPDIGSA GKANVIEVMV KAGDTVEADQ
160 170 180 190 200
SLITLESDKA SMEIPSPASG VVESVSIKVG DEVGTGDLIL KLKVEGAAPA
210 220 230 240 250
AEEQPAAAPA QAAAPAAEQK PAAAAPAPAK ADTPAPVGAP SRDGAKVHAG
260 270 280 290 300
PAVRMLAREF GVELSEVKAS GPKGRILKED VQVFVKEQLQ RAKSGGAGAT
310 320 330 340 350
GGAGIPPIPE VDFSKFGEVE EVAMTRLMQV GAANLHRSWL NVPHVTQFDQ
360 370 380 390 400
SDITDMEAFR VAQKAAAEKA GVKLTVLPIL LKACAHLLKE LPDFNSSLAP
410 420 430 440 450
SGKALIRKKY VHIGFAVDTP DGLLVPVIRD VDRKSLLQLA AEAADLADKA
460 470 480 490 500
RNKKLSADAM QGACFTISSL GHIGGTGFTP IVNAPEVAIL GVSKATMQPV
510 520 530 540
WDGKAFQPRL MLPLSLSYDH RVINGAAAAR FTKRLGELLA DIRTLLL
Length:547
Mass (Da):56,709
Last modified:December 7, 2000 - v2
Checksum:i24E15CCC9A590CB4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251A → V in AAC45354 (PubMed:9171401).Curated
Sequence conflicti295 – 3017GGAGATG → AVPAPR in AAC45354 (PubMed:9171401).Curated
Sequence conflicti328 – 3292MQ → IE in AAC45354 (PubMed:9171401).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47920 Genomic DNA. Translation: AAC45354.1.
AE004091 Genomic DNA. Translation: AAG08401.1.
PIRiH83018.
RefSeqiNP_253703.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG08401; AAG08401; PA5016.
GeneIDi881297.
KEGGipae:PA5016.
PATRICi19844857. VBIPseAer58763_5257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47920 Genomic DNA. Translation: AAC45354.1.
AE004091 Genomic DNA. Translation: AAG08401.1.
PIRiH83018.
RefSeqiNP_253703.1. NC_002516.2.

3D structure databases

SMRiQ59638. Positions 2-81, 119-198, 247-292, 305-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5016.

2D gel databases

World-2DPAGE0008:Q59638.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08401; AAG08401; PA5016.
GeneIDi881297.
KEGGipae:PA5016.
PATRICi19844857. VBIPseAer58763_5257.

Organism-specific databases

PseudoCAPiPA5016.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
InParanoidiQ59638.
KOiK00627.
OMAiTEIMVAV.
PhylomeDBiQ59638.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: PAO.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiODP2_PSEAE
AccessioniPrimary (citable) accession number: Q59638
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: December 7, 2000
Last modified: March 31, 2015
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.