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P0AFG9

- ODP1_ECO57

UniProt

P0AFG9 - ODP1_ECO57

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Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi231 – 2311MagnesiumBy similarity
Metal bindingi261 – 2611MagnesiumBy similarity
Metal bindingi263 – 2631Magnesium; via carbonyl oxygenBy 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 – 11RemovedBy similarity
Chaini2 – 887886Pyruvate dehydrogenase E1 componentPRO_0000162244Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP0AFG9.

Interactioni

Subunit structurei

Homodimer. 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

1
887
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 683Combined sources
Helixi76 – 9924Combined sources
Helixi109 – 12416Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi137 – 1393Combined sources
Helixi142 – 1443Combined sources
Helixi145 – 15410Combined sources
Helixi160 – 1634Combined sources
Turni181 – 1833Combined sources
Turni185 – 1873Combined sources
Helixi197 – 21418Combined sources
Beta strandi225 – 2306Combined sources
Helixi233 – 2353Combined sources
Helixi237 – 2404Combined sources
Helixi243 – 2486Combined sources
Beta strandi254 – 2607Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi271 – 2733Combined sources
Helixi275 – 28511Combined sources
Beta strandi289 – 2935Combined sources
Helixi297 – 2993Combined sources
Helixi300 – 3056Combined sources
Helixi310 – 3178Combined sources
Helixi320 – 3267Combined sources
Helixi331 – 3377Combined sources
Helixi339 – 3413Combined sources
Helixi343 – 3464Combined sources
Turni347 – 3493Combined sources
Beta strandi350 – 3523Combined sources
Helixi354 – 3574Combined sources
Helixi363 – 3653Combined sources
Helixi367 – 37913Combined sources
Beta strandi385 – 3906Combined sources
Turni393 – 3964Combined sources
Helixi416 – 4249Combined sources
Helixi431 – 4344Combined sources
Helixi447 – 45711Combined sources
Turni458 – 4603Combined sources
Helixi479 – 4824Combined sources
Helixi483 – 4864Combined sources
Helixi495 – 50612Combined sources
Turni510 – 5156Combined sources
Beta strandi516 – 5227Combined sources
Helixi525 – 5273Combined sources
Helixi530 – 5367Combined sources
Beta strandi565 – 5673Combined sources
Helixi572 – 58312Combined sources
Helixi585 – 5884Combined sources
Beta strandi594 – 6007Combined sources
Helixi601 – 6033Combined sources
Helixi605 – 61713Combined sources
Beta strandi623 – 6286Combined sources
Turni631 – 6333Combined sources
Turni635 – 6373Combined sources
Turni639 – 6413Combined sources
Helixi646 – 6505Combined sources
Beta strandi656 – 6594Combined sources
Helixi664 – 67916Combined sources
Beta strandi687 – 6915Combined sources
Helixi707 – 7126Combined sources
Beta strandi714 – 7207Combined sources
Beta strandi726 – 7316Combined sources
Helixi733 – 7353Combined sources
Helixi736 – 75015Combined sources
Beta strandi753 – 7608Combined sources
Helixi762 – 77817Combined sources
Helixi788 – 7925Combined sources
Beta strandi798 – 8014Combined sources
Helixi807 – 8104Combined sources
Helixi811 – 8155Combined sources
Beta strandi817 – 8193Combined sources
Beta strandi821 – 8244Combined sources
Helixi835 – 8417Combined sources
Helixi846 – 85914Combined sources
Helixi865 – 87410Combined sources
Turni884 – 8863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN
60 70 80 90 100
VAAGTGISNY INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK
110 120 130 140 150
DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF QGHISPGVYA
160 170 180 190 200
RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI
210 220 230 240 250
GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK
260 270 280 290 300
LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
310 320 330 340 350
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA
360 370 380 390 400
DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA
410 420 430 440 450
AEGKNIAHQV KKMNMDGVRH IRDRFNVPVS DADIEKLPYI TFPEGSEEHT
460 470 480 490 500
YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS KEISTTIAFV
510 520 530 540 550
RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD
560 570 580 590 600
REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
610 620 630 640 650
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS
660 670 680 690 700
LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP
710 720 730 740 750
AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY
760 770 780 790 800
GVGSDVYSVT SFTELARDGQ DCERWNMLHP LETPRVPYIA QVMNDAPAVA
810 820 830 840 850
STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH HFEVDASYVV
860 870 880
VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
Length:887
Mass (Da):99,668
Last modified:January 23, 2007 - v2
Checksum:i7FB3811DE11BDD02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 68 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