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aceE:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

AceE

Synonyms

pyruvate dehydrogenase, decarboxylase component E1, thiamin-binding[1], B0114[2][1], AceE[2][1]

Product description

subunit of E1p component of pyruvate dehydrogenase complex[2][3];

Component of ; E1P-CPLX[2]; pyruvate dehydrogenase multienzyme complex[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0006096

glycolysis

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0324

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0004739

pyruvate dehydrogenase (acetyl-transferring) activity

GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.2.4.1

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0000287

magnesium ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0003824

catalytic activity

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009014
InterPro:IPR015941

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0008152

metabolic process

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009014
InterPro:IPR015941

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0016491

oxidoreductase activity

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR004660
SP_KW:KW-0560

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P05100

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0A8L7

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0A8N7

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0A9U1

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0AB83

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0AB89

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0AEV9

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0AG40

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P26602

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P46889

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P76049

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P76170

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P77439

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:16606699[6]

IPI: Inferred from Physical Interaction

UniProtKB:P0A6F5

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005624

membrane fraction

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required fields missing

GO:0016052

carbohydrate catabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006086

acetyl-CoA biosynthetic process from pyruvate

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0009436

glyoxylate catabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0009061

anaerobic respiration

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0004738

pyruvate dehydrogenase activity

F

required field missing

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Interactions

Partner TypePartnerNotesReferences

Protein

Subunits of E1P-CPLX

could be indirect

Protein

Subunits of pyruvate dehydrogenase multienzyme complex

could be indirect

Small Molecule

TTTPP

selectively inhibits pyruvate or 2-oxoglutarate dehydrogenase (El).


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Notes

Localization

CompartmentDescriptionEvidenceNotes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc 

MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY
INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV
CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH
PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK
GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL
NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH
IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ
DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS
PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD
PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI
EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP
LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH
HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
Mol. Wt

99.67 kDa (calc) [2]

pI

5.76[2]

Extinction coefficient

123080 - 123830 (calc based on 42 Y, 11 W, and 6 C residues)

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Domains/Motifs/Modification Sites

TypeResiduesDescriptionNotes
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Structure

Structures
  • Representative Escherichia coli structure:
    2QTA|A
    1-886 of 887 residues (E-value: 0.) (Percent Identity: 99.89)
  • Representative homolog:
    1TKA|A (Saccharomyces cerevisiae)
    62-219 of 887 residues (E-value: 1.6e-06) (Percent Identity: 29.41)
  • View all other structures.
Models

View models at:

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Notes

Gene Product Resources

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Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:E1P-MONOMER

PDB (EcoliWiki Page)

PDB:1RP7

SwissModel (EcoliWiki Page)

SwissModel:P0AFG8

UniProt (EcoliWiki Page)

UniProt:P0AFG8

RefSeq (EcoliWiki Page)

RefSeq:NP_414656


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Notes

Links

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NameURLComments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
  6. ↑ Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
  7. ↑ Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed EcoliWiki page


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