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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei520Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-5132-MONOMER

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:aceB1 Publication
Ordered Locus Names:PA5016
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5016

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

Disruption inactivates the pyruvate dehydrogenase complex and causes an increase in pyruvate concentration and acidity of the culture medium.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622831 – 547Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41N6-lipoyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei159N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

PaxDbiQ59638
PRIDEiQ59638

2D gel databases

World-2DPAGEi0008:Q59638

Expressioni

Inductioni

Induced by glucose.1 Publication

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

STRINGi208964.PA5016

Structurei

3D structure databases

ProteinModelPortaliQ59638
SMRiQ59638
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 75Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST74
Domaini119 – 193Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST75
Domaini248 – 285Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiENOG4107QSN Bacteria
COG0508 LUCA
HOGENOMiHOG000281562
InParanoidiQ59638
KOiK00627
OMAiTMEFESF
PhylomeDBiQ59638

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR006256 AcTrfase_Pyrv_DH_cplx
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PANTHERiPTHR43178:SF2 PTHR43178:SF2, 3 hits
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 2 hits
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 2 hits
TIGRFAMsiTIGR01348 PDHac_trf_long, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 2 hits
PS00189 LIPOYL, 2 hits
PS51826 PSBD, 1 hit

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 8, 2000 - v2
Checksum:i24E15CCC9A590CB4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti225A → V in AAC45354 (PubMed:9171401).Curated1
Sequence conflicti295 – 301GGAGATG → AVPAPR in AAC45354 (PubMed:9171401).Curated7
Sequence conflicti328 – 329MQ → IE in AAC45354 (PubMed:9171401).Curated2

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
WP_003115359.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG08401; AAG08401; PA5016
GeneIDi881297
KEGGipae:PA5016
PATRICifig|208964.12.peg.5257

Similar proteinsi

Entry informationi

Entry nameiODP2_PSEAE
AccessioniPrimary (citable) accession number: Q59638
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: March 28, 2018
This is version 128 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health