Reviewed, UniProtKB/Swiss-Prot P0AFG9 (ODP1_ECO57)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component
    EC=1.2.4.1

Gene names

Name:	aceE
Ordered Locus Names:	Z0124, ECs0118

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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) By similarity.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Magnesium By similarity. Thiamine pyrophosphate By similarity.
Subunit structure	Homodimer By similarity.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Magnesium Metal-binding Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 887	886	Pyruvate dehydrogenase E1 component		PRO_0000162244
Sites
	Metal binding	231	1	Magnesium By similarity
	Metal binding	261	1	Magnesium By similarity
	Metal binding	263	1	Magnesium; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	716	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AFG9-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 7FB3811DE11BDD02	FASTA	887	99,668
	10 20 30 40 50 60 MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY 70 80 90 100 110 120 INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV 130 140 150 160 170 180 CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH 190 200 210 220 230 240 PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK 250 260 270 280 290 300 GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD 310 320 330 340 350 360 ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL 370 380 390 400 410 420 NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH 430 440 450 460 470 480 IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ 490 500 510 520 530 540 DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS 550 560 570 580 590 600 PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY 610 620 630 640 650 660 SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD 670 680 690 700 710 720 PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI 730 740 750 760 770 780 EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP 790 800 810 820 830 840 LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH 850 860 870 880 HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG54418.1. BA000007 Genomic DNA. Translation: BAB33541.1.
PIR	F85494. F90643.
RefSeq	NP_285810.1. NP_308145.1.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P0AFG9.
Genome annotation databases
GeneID	913657. 956809.
GenomeReviews	Gene locus Z0124 in contig AE005174_GR. Gene locus ECs0118 in contig BA000007_GR.
KEGG	ece:Z0124. ecs:ECs0118.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289271.
OMA	REISTTQ.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS0118-MONOMER.
Family and domain databases
InterPro	IPR004660. 2-oxoA_DH_E1. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005474. Transketolase_N. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
Pfam	PF00456. Transketolase_N. 2 hits. [Graphical view]
PIRSF	PIRSF000156. Pyruvate_dh_E1. 1 hit.
TIGRFAMs	TIGR00759. aceE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODP1_ECO57

Accession

Primary (citable) accession number: P0AFG9
Secondary accession number(s): P06958, P78049, Q53382

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 37 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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