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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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)-lipoateNote: Binds 3 lipoyl cofactors covalently.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei547Sequence analysis1
Active sitei6031
Active sitei607Sequence analysis1

GO - Molecular functioni

  • dihydrolipoyllysine-residue acetyltransferase activity Source: EcoliWiki
  • lipoic acid binding Source: EcoliWiki

GO - Biological processi

  • acetyl-CoA biosynthetic process from pyruvate Source: EcoliWiki
  • glycolytic process Source: UniProtKB-KW
  • oxidation-reduction process Source: GOC
  • pyruvate metabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciEcoCyc:E2P-MONOMER.
ECOL316407:JW0111-MONOMER.
MetaCyc:E2P-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
Ordered Locus Names:b0115, JW0111
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10025. aceF.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • pyruvate dehydrogenase complex Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi603H → C: Abolishes catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001622782 – 630Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST629

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41N6-lipoyllysinePROSITE-ProRule annotation2 Publications1
Modified residuei144N6-lipoyllysinePROSITE-ProRule annotation2 Publications1
Modified residuei245N6-lipoyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei396N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP06959.
PaxDbiP06959.
PRIDEiP06959.

2D gel databases

SWISS-2DPAGEP06959.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Binary interactionsi

WithEntry#Exp.IntActNotes
dcmP0AED92EBI-542707,EBI-548525
intAP320532EBI-542707,EBI-552967
lpdAP0A9P03EBI-542707,EBI-542856
pinRP0ADI02EBI-542707,EBI-544672

Protein-protein interaction databases

BioGridi4261371. 5 interactors.
DIPiDIP-9040N.
IntActiP06959. 84 interactors.
MINTiMINT-1311573.
STRINGi511145.b0115.

Structurei

Secondary structure

1630
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi206 – 209Combined sources4
Beta strandi215 – 217Combined sources3
Beta strandi219 – 223Combined sources5
Beta strandi227 – 229Combined sources3
Beta strandi236 – 246Combined sources11
Beta strandi248 – 254Combined sources7
Beta strandi256 – 260Combined sources5
Beta strandi276 – 280Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QJONMR-A206-284[»]
2K7VNMR-A/B206-293[»]
ProteinModelPortaliP06959.
SMRiP06959.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06959.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 75Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST74
Domaini105 – 178Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST74
Domaini206 – 279Lipoyl-binding 3PROSITE-ProRule annotationAdd BLAST74

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni317 – 630Subunit binding, catalyticAdd BLAST314
Regioni373 – 389HydrophobicAdd BLAST17
Regioni542 – 567HydrophobicAdd BLAST26

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 3 lipoyl-binding domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiENOG4107QSN. Bacteria.
COG0508. LUCA.
HOGENOMiHOG000281562.
InParanoidiP06959.
KOiK00627.
OMAiGKEFEPR.
PhylomeDBiP06959.

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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ
60 70 80 90 100
AGIVKEIKVS VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP
110 120 130 140 150
AAAAAKDVNV PDIGSDEVEV TEILVKVGDK VEAEQSLITV EGDKASMEVP
160 170 180 190 200
APFAGTVKEI KVNVGDKVST GSLIMVFEVA GEAGAAAPAA KQEAAPAAAP
210 220 230 240 250
APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT VEGDKASMEV
260 270 280 290 300
PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
310 320 330 340 350
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT
360 370 380 390 400
GRKGRILRED VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI
410 420 430 440 450
EEVELGRIQK ISGANLSRNW VMIPHVTHFD KTDITELEAF RKQQNEEAAK
460 470 480 490 500
RKLDVKITPV VFIMKAVAAA LEQMPRFNSS LSEDGQRLTL KKYINIGVAV
510 520 530 540 550
DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA GEMQGGCFTI
560 570 580 590 600
SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
610 620 630
FDHRVIDGAD GARFITIINN TLSDIRRLVM
Length:630
Mass (Da):66,096
Last modified:January 23, 2007 - v3
Checksum:i802A513A1E88F5DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01498 Genomic DNA. Translation: CAA24741.1.
U00096 Genomic DNA. Translation: AAC73226.1.
AP009048 Genomic DNA. Translation: BAB96685.1.
PIRiA30278. XXECDP.
RefSeqiNP_414657.1. NC_000913.3.
WP_000963518.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73226; AAC73226; b0115.
BAB96685; BAB96685; BAB96685.
GeneIDi944794.
KEGGiecj:JW0111.
eco:b0115.
PATRICi32115331. VBIEscCol129921_0117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01498 Genomic DNA. Translation: CAA24741.1.
U00096 Genomic DNA. Translation: AAC73226.1.
AP009048 Genomic DNA. Translation: BAB96685.1.
PIRiA30278. XXECDP.
RefSeqiNP_414657.1. NC_000913.3.
WP_000963518.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QJONMR-A206-284[»]
2K7VNMR-A/B206-293[»]
ProteinModelPortaliP06959.
SMRiP06959.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261371. 5 interactors.
DIPiDIP-9040N.
IntActiP06959. 84 interactors.
MINTiMINT-1311573.
STRINGi511145.b0115.

2D gel databases

SWISS-2DPAGEP06959.

Proteomic databases

EPDiP06959.
PaxDbiP06959.
PRIDEiP06959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73226; AAC73226; b0115.
BAB96685; BAB96685; BAB96685.
GeneIDi944794.
KEGGiecj:JW0111.
eco:b0115.
PATRICi32115331. VBIEscCol129921_0117.

Organism-specific databases

EchoBASEiEB0024.
EcoGeneiEG10025. aceF.

Phylogenomic databases

eggNOGiENOG4107QSN. Bacteria.
COG0508. LUCA.
HOGENOMiHOG000281562.
InParanoidiP06959.
KOiK00627.
OMAiGKEFEPR.
PhylomeDBiP06959.

Enzyme and pathway databases

BioCyciEcoCyc:E2P-MONOMER.
ECOL316407:JW0111-MONOMER.
MetaCyc:E2P-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP06959.
PROiP06959.

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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODP2_ECOLI
AccessioniPrimary (citable) accession number: P06959
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.