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P0AFG9

- ODP1_ECO57

UniProt

P0AFG9 - ODP1_ECO57

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Protein
Pyruvate dehydrogenase E1 component
Gene
aceE, Z0124, ECs0118
Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity.

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Magnesium By similarity.
Thiamine pyrophosphate By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi231 – 2311Magnesium By similarity
Metal bindingi261 – 2611Magnesium By similarity
Metal bindingi263 – 2631Magnesium; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding, Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciECOL386585:GJFA-115-MONOMER.
ECOO157:ACEE-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component (EC:1.2.4.1)
Short name:
PDH E1 component
Gene namesi
Name:aceE
Ordered Locus Names:Z0124, ECs0118
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 887886Pyruvate dehydrogenase E1 component
PRO_0000162244Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei716 – 7161N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP0AFG9.

Interactioni

Subunit structurei

Homodimer By similarity. Part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Protein-protein interaction databases

IntActiP0AFG9. 3 interactions.
STRINGi155864.Z0124.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 683
Helixi76 – 9924
Helixi109 – 12416
Beta strandi131 – 1333
Beta strandi137 – 1393
Helixi142 – 1443
Helixi145 – 15410
Helixi160 – 1634
Turni181 – 1833
Turni185 – 1873
Helixi197 – 21418
Beta strandi225 – 2306
Helixi233 – 2353
Helixi237 – 2404
Helixi243 – 2486
Beta strandi254 – 2607
Beta strandi265 – 2695
Beta strandi271 – 2733
Helixi275 – 28511
Beta strandi289 – 2935
Helixi297 – 2993
Helixi300 – 3056
Helixi310 – 3178
Helixi320 – 3267
Helixi331 – 3377
Helixi339 – 3413
Helixi343 – 3464
Turni347 – 3493
Beta strandi350 – 3523
Helixi354 – 3574
Helixi363 – 3653
Helixi367 – 37913
Beta strandi385 – 3906
Turni393 – 3964
Helixi416 – 4249
Helixi431 – 4344
Helixi447 – 45711
Turni458 – 4603
Helixi479 – 4824
Helixi483 – 4864
Helixi495 – 50612
Turni510 – 5156
Beta strandi516 – 5227
Helixi525 – 5273
Helixi530 – 5367
Beta strandi565 – 5673
Helixi572 – 58312
Helixi585 – 5884
Beta strandi594 – 6007
Helixi601 – 6033
Helixi605 – 61713
Beta strandi623 – 6286
Turni631 – 6333
Turni635 – 6373
Turni639 – 6413
Helixi646 – 6505
Beta strandi656 – 6594
Helixi664 – 67916
Beta strandi687 – 6915
Helixi707 – 7126
Beta strandi714 – 7207
Beta strandi726 – 7316
Helixi733 – 7353
Helixi736 – 75015
Beta strandi753 – 7608
Helixi762 – 77817
Helixi788 – 7925
Beta strandi798 – 8014
Helixi807 – 8104
Helixi811 – 8155
Beta strandi817 – 8193
Beta strandi821 – 8244
Helixi835 – 8417
Helixi846 – 85914
Helixi865 – 87410
Turni884 – 8863

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LPLX-ray2.10A/B2-887[»]
3LQ2X-ray1.96A/B2-887[»]
3LQ4X-ray1.98A/B2-887[»]
ProteinModelPortaliP0AFG9.
SMRiP0AFG9. Positions 57-887.

Miscellaneous databases

EvolutionaryTraceiP0AFG9.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2609.
HOGENOMiHOG000115215.
KOiK00163.
OMAiKGIYKLD.
OrthoDBiEOG6BW4TW.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR004660. 2-oxoA_DH_E1.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005474. Transketolase_N.
[Graphical view]
PfamiPF00456. Transketolase_N. 2 hits.
[Graphical view]
PIRSFiPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00759. aceE. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0AFG9-1 [UniParc]FASTAAdd to Basket

« Hide

MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN    50
VAAGTGISNY INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK 100
DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF QGHISPGVYA 150
RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI 200
GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK 250
LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD 300
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA 350
DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA 400
AEGKNIAHQV KKMNMDGVRH IRDRFNVPVS DADIEKLPYI TFPEGSEEHT 450
YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS KEISTTIAFV 500
RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD 550
REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY 600
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS 650
LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP 700
AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY 750
GVGSDVYSVT SFTELARDGQ DCERWNMLHP LETPRVPYIA QVMNDAPAVA 800
STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH HFEVDASYVV 850
VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA 887
Length:887
Mass (Da):99,668
Last modified:January 23, 2007 - v2
Checksum:i7FB3811DE11BDD02
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG54418.1.
BA000007 Genomic DNA. Translation: BAB33541.1.
PIRiF85494.
F90643.
RefSeqiNP_285810.1. NC_002655.2.
NP_308145.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG54418; AAG54418; Z0124.
BAB33541; BAB33541; BAB33541.
GeneIDi913657.
956809.
KEGGiece:Z0124.
ecs:ECs0118.
PATRICi18349174. VBIEscCol44059_0117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG54418.1 .
BA000007 Genomic DNA. Translation: BAB33541.1 .
PIRi F85494.
F90643.
RefSeqi NP_285810.1. NC_002655.2.
NP_308145.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LPL X-ray 2.10 A/B 2-887 [» ]
3LQ2 X-ray 1.96 A/B 2-887 [» ]
3LQ4 X-ray 1.98 A/B 2-887 [» ]
ProteinModelPortali P0AFG9.
SMRi P0AFG9. Positions 57-887.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0AFG9. 3 interactions.
STRINGi 155864.Z0124.

Proteomic databases

PRIDEi P0AFG9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG54418 ; AAG54418 ; Z0124 .
BAB33541 ; BAB33541 ; BAB33541 .
GeneIDi 913657.
956809.
KEGGi ece:Z0124.
ecs:ECs0118.
PATRICi 18349174. VBIEscCol44059_0117.

Phylogenomic databases

eggNOGi COG2609.
HOGENOMi HOG000115215.
KOi K00163.
OMAi KGIYKLD.
OrthoDBi EOG6BW4TW.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-115-MONOMER.
ECOO157:ACEE-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AFG9.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR004660. 2-oxoA_DH_E1.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005474. Transketolase_N.
[Graphical view ]
Pfami PF00456. Transketolase_N. 2 hits.
[Graphical view ]
PIRSFi PIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMi SSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsi TIGR00759. aceE. 1 hit.
ProtoNeti Search...

Publicationsi

  1. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiODP1_ECO57
AccessioniPrimary (citable) accession number: P0AFG9
Secondary accession number(s): P06958, P78049, Q53382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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