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P06959

- ODP2_ECOLI

UniProt

P06959 - ODP2_ECOLI

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei547 – 5471Sequence Analysis
Active sitei603 – 6031
Active sitei607 – 6071Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: EcoliWiki
  2. lipoic acid binding Source: EcoliWiki

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: EcoliWiki
  2. glycolytic process Source: UniProtKB-KW
  3. oxidation-reduction process Source: GOC
  4. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10025. aceF.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi603 – 6031H → C: Abolishes catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 630629Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-lipoyllysine2 PublicationsPROSITE-ProRule annotation
Modified residuei144 – 1441N6-lipoyllysine2 PublicationsPROSITE-ProRule annotation
Modified residuei245 – 2451N6-lipoyllysine1 PublicationPROSITE-ProRule annotation
Modified residuei396 – 3961N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP06959.
PRIDEiP06959.

2D gel databases

SWISS-2DPAGEP06959.

Expressioni

Gene expression databases

GenevestigatoriP06959.

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

DIPiDIP-9040N.
IntActiP06959. 84 interactions.
MINTiMINT-1311573.
STRINGi511145.b0115.

Structurei

Secondary structure

1
630
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi206 – 2094Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi236 – 24611Combined sources
Beta strandi248 – 2547Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi276 – 2805Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QJONMR-A206-284[»]
2K7VNMR-A/B206-293[»]
ProteinModelPortaliP06959.
SMRiP06959. Positions 1-81, 106-183, 206-284, 384-630.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06959.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7574Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini105 – 17874Lipoyl-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini206 – 27974Lipoyl-binding 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni317 – 630314Subunit binding, catalyticAdd
BLAST
Regioni373 – 38917HydrophobicAdd
BLAST
Regioni542 – 56726HydrophobicAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
InParanoidiP06959.
KOiK00627.
OMAiTEIMVAV.
OrthoDBiEOG610413.
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.
YP_488418.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73226; AAC73226; b0115.
BAB96685; BAB96685; BAB96685.
GeneIDi12932377.
944794.
KEGGiecj:Y75_p0112.
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 .
PIRi A30278. XXECDP.
RefSeqi NP_414657.1. NC_000913.3.
YP_488418.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QJO NMR - A 206-284 [» ]
2K7V NMR - A/B 206-293 [» ]
ProteinModelPortali P06959.
SMRi P06959. Positions 1-81, 106-183, 206-284, 384-630.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9040N.
IntActi P06959. 84 interactions.
MINTi MINT-1311573.
STRINGi 511145.b0115.

2D gel databases

SWISS-2DPAGE P06959.

Proteomic databases

PaxDbi P06959.
PRIDEi P06959.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73226 ; AAC73226 ; b0115 .
BAB96685 ; BAB96685 ; BAB96685 .
GeneIDi 12932377.
944794.
KEGGi ecj:Y75_p0112.
eco:b0115.
PATRICi 32115331. VBIEscCol129921_0117.

Organism-specific databases

EchoBASEi EB0024.
EcoGenei EG10025. aceF.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281562.
InParanoidi P06959.
KOi K00627.
OMAi TEIMVAV.
OrthoDBi EOG610413.
PhylomeDBi P06959.

Enzyme and pathway databases

BioCyci EcoCyc:E2P-MONOMER.
ECOL316407:JW0111-MONOMER.
MetaCyc:E2P-MONOMER.

Miscellaneous databases

EvolutionaryTracei P06959.
PROi P06959.

Gene expression databases

Genevestigatori P06959.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component."
    Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.
    Eur. J. Biochem. 133:481-489(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], LIPOYLATION AT LYS-41; LYS-144 AND LYS-245.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  5. "Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli."
    Hale G., Perham R.N.
    Biochem. J. 187:905-908(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-47, LIPOYLATION AT LYS-41.
  6. "Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue."
    Russel G.C., Guest J.R.
    Biochem. J. 269:443-450(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-603.
  7. "Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli."
    Ali S.T., Guest J.R.
    Biochem. J. 271:139-145(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPOYLATED DOMAINS STUDIES, LIPOYLATION AT LYS-144.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

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 26, 2014
This is version 159 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

External Data

Dasty 3