Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P06959 (ODP2_ECOLI)

Last modified February 9, 2010. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
    EC=2.3.1.12
Alternative name(s):
    E2
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Gene names

Name:	aceF
Ordered Locus Names:	b0115, JW0111

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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 3 lipoyl cofactors covalently.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 3 lipoyl-binding domains.

Hide | Top

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl Repeat
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	acetyl-CoA biosynthetic process from pyruvate Inferred from mutant phenotype. Source: UniProtKB glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	pyruvate dehydrogenase complex Inferred from direct assay. Source: UniProtKB
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from direct assay. Source: UniProtKB lipoic acid binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
alkA	P04395	1	EBI-542707,EBI-544077
dcm	P0AED9	1	EBI-542707,EBI-548525
intA	P32053	1	EBI-542707,EBI-552967
pinR	P0ADI0	1	EBI-542707,EBI-544672
recG	P24230	1	EBI-542707,EBI-556882
rnt	P30014	1	EBI-542707,EBI-557418
tyrR	P07604	1	EBI-542707,EBI-559274
yraL	P67087	1	EBI-542707,EBI-561394

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 630

629

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

PRO_0000162278

Regions

Domain

2 – 74

Lipoyl-binding 1

Domain

106 – 177

Lipoyl-binding 2

Domain

207 – 278

Lipoyl-binding 3

Region

317 – 630

314

Subunit binding, catalytic

Region

373 – 389

Hydrophobic

Region

542 – 567

Hydrophobic

Sites

Active site

547

Potential

Active site

603

Active site

607

Potential

Amino acid modifications

Modified residue

N6-lipoyllysine

Modified residue

144

N6-lipoyllysine

Modified residue

245

N6-lipoyllysine

Modified residue

396

N6-acetyllysine Ref.8

Experimental info

Mutagenesis

603

H → C: Abolishes catalytic activity. Ref.6

Secondary structure

630

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P06959-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 802A513A1E88F5DA
Show »

FASTA

630

66,096

        10         20         30         40         50         60 
MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS 

        70         80         90        100        110        120 
VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV 

       130        140        150        160        170        180 
TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA 

       190        200        210        220        230        240 
GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT 

       250        260        270        280        290        300 
VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA 

       310        320        330        340        350        360 
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED 

       370        380        390        400        410        420 
VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW 

       430        440        450        460        470        480 
VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS 

       490        500        510        520        530        540 
LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA 

       550        560        570        580        590        600 
GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS 

       610        620        630 
FDHRVIDGAD GARFITIINN TLSDIRRLVM

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 6345153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 9298646] [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: 6821375] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-47.
[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: 2201286] [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: 2121129] [Abstract] Cited for: LIPOYLATED DOMAINS STUDIES.
[8]	"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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01498 Genomic DNA. Translation: CAA24741.1.
U00096 Genomic DNA. Translation: AAC73226.1.
AP009048 Genomic DNA. Translation: BAB96685.1.

PIR

XXECDP. A30278.

RefSeq

AP_000776.1.
NP_414657.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QJO	NMR	-	A	206-284	[»]
2K7V	NMR	-	A/B	219-293	[»]

SMR

P06959. Positions 1-81, 106-183, 326-370, 388-630.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9040N.

IntAct

P06959. 83 interactions.

STRING

P06959.

2-D gel databases

SWISS-2DPAGE

P06959.

ECO2DBASE

C062.7. 6TH EDITION.
C070.0. 6TH EDITION.

Proteomic databases

PRIDE

P06959.

Genome annotation databases

GeneID

944794.

GenomeReviews

Gene locus JW0111 in contig AP009048_GR.
Gene locus b0115 in contig U00096_GR.

KEGG

ecj:JW0111.
eco:b0115.

Organism-specific databases

EchoBASE

EB0024.

EcoGene

EG10025. aceF.

CMR

Search...

Phylogenomic databases

eggNOG

COG0508.

HOGENOM

HBG630916.

OMA

MEIPAPK.

Enzyme and pathway databases

BioCyc

EcoCyc:E2P-MONOMER.
ECOL168927:B0115-MONOMER.
MetaCyc:E2P-MONOMER.

Gene expression databases

Genevestigator

P06959.

Family and domain databases

InterPro

IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR004167. E3_bd.
IPR011053. Single_hybrid_motif.
[Graphical view]

Gene3D

G3DSA:4.10.320.10. E3_bd. 1 hit.

Pfam

PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01348. PDHac_trf_long. 1 hit.

PROSITE

PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

ProtoNet

Search...

Hide | Top

Entry information

Entry name

ODP2_ECOLI

Accession

Primary (citable) accession number: P06959

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 120 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents