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P0A9G6 (ACEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate lyase

Short name=ICL
Short name=Isocitrase
Short name=Isocitratase
EC=4.1.3.1
Gene names
Name:aceA
Synonyms:icl
Ordered Locus Names:b4015, JW3975
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway By similarity.

Catalytic activity

Isocitrate = succinate + glyoxylate.

Cofactor

Divalent cations.

Enzyme regulation

Is activated by phosphorylation (on histidine) and is inhibited by PEP, 3-phosphoglycerate and succinate.

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred by curator PubMed 366070. Source: EcoliWiki

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_functioncation binding

Inferred from direct assay Ref.10. Source: EcoliWiki

isocitrate lyase activity

Inferred from direct assay Ref.10. Source: EcoliWiki

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Isocitrate lyase
PRO_0000068774

Sites

Active site1951 Probable

Experimental info

Mutagenesis1951C → A: Large decrease in activity. Ref.11
Mutagenesis1951C → S: Large decrease in activity. Ref.11
Sequence conflict101 – 11717LAASM…PANSV → WRPACIRISRSIRQTRC in CAA30416. Ref.3
Sequence conflict2151A → P in CAA30416. Ref.3
Sequence conflict2931P → R in AAA24009. Ref.8
Sequence conflict3381Q → E in CAA30416. Ref.3
Sequence conflict419 – 43416TSSVT…EESQF → DVFSHRADRLH Ref.4

Secondary structure

................................................................... 434
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9G6 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: F66449CCD1E168E9

FASTA43447,522
        10         20         30         40         50         60 
MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA AKMWRLLHGE 

        70         80         90        100        110        120 
SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN LAASMYPDQS LYPANSVPAV 

       130        140        150        160        170        180 
VERINNTFRR ADQIQWSAGI EPGDPRYVDY FLPIVADAEA GFGGVLNAFE LMKAMIEAGA 

       190        200        210        220        230        240 
AAVHFEDQLA SVKKCGHMGG KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL 

       250        260        270        280        290        300 
ITSDCDPYDS EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR 

       310        320        330        340        350        360 
FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI TLAGIHSMWF 

       370        380        390        400        410        420 
NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ QEVGTGYFDK VTTIIQGGTS 

       430 
SVTALTGSTE ESQF 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli."
Byrne C.R., Stokes H.W., Ward K.A.
Nucleic Acids Res. 16:9342-9342(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli."
Byrne C.R., Stokes H.W., Ward K.A.
Nucleic Acids Res. 16:10924-10924(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Nucleotide sequence of the aceA gene coding for isocitrate lyase in Escherichia coli."
Rieul C., Bleicher F., Duclos B., Cortay J.-C., Cozzone A.J.
Nucleic Acids Res. 16:5689-5689(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[4]"Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli."
Matsuoka M., McFadden B.A.
J. Bacteriol. 170:4528-4536(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase."
Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T., Laporte D.C.
J. Bacteriol. 170:2763-2769(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-434.
[9]"Evidence of histidine phosphorylation in isocitrate lyase from Escherichia coli."
Robertson E.F., Hoyt J.C., Reeves H.C.
J. Biol. Chem. 263:2477-2482(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[10]"Escherichia coli isocitrate lyase: properties and comparisons."
Hoyt J.C., Robertson E.F., Berlyn K.A., Reeves H.C.
Biochim. Biophys. Acta 966:30-35(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[11]"Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308."
Robertson A.G., Nimmo H.G.
Biochem. J. 305:239-244(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-195.
Strain: ML308.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12431 Genomic DNA. Translation: CAA30974.1.
X07543 Genomic DNA. Translation: CAA30416.1.
M22621 Genomic DNA. Translation: AAC13650.1.
U00006 Genomic DNA. Translation: AAC43109.1.
U00096 Genomic DNA. Translation: AAC76985.1.
AP009048 Genomic DNA. Translation: BAE78017.1.
M20714 Genomic DNA. Translation: AAA24009.1.
PIRWZECIC. S05692.
RefSeqNP_418439.1. NC_000913.3.
YP_492158.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IGWX-ray2.10A/B/C/D1-434[»]
ProteinModelPortalP0A9G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35893N.
IntActP0A9G6. 3 interactions.
STRING511145.b4015.

2D gel databases

SWISS-2DPAGEP0A9G6.

Proteomic databases

PaxDbP0A9G6.
PRIDEP0A9G6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76985; AAC76985; b4015.
BAE78017; BAE78017; BAE78017.
GeneID12934475.
948517.
KEGGecj:Y75_p3902.
eco:b4015.
PATRIC32123557. VBIEscCol129921_4127.

Organism-specific databases

EchoBASEEB0021.
EcoGeneEG10022. aceA.

Phylogenomic databases

eggNOGCOG2224.
HOGENOMHOG000238475.
KOK01637.
OMADQIQWAN.
OrthoDBEOG689HMX.
PhylomeDBP0A9G6.

Enzyme and pathway databases

BioCycEcoCyc:ISOCIT-LYASE-MONOMER.
ECOL316407:JW3975-MONOMER.
MetaCyc:ISOCIT-LYASE-MONOMER.
UniPathwayUPA00703; UER00719.

Gene expression databases

GenevestigatorP0A9G6.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
InterProIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamPF00463. ICL. 2 hits.
[Graphical view]
PIRSFPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR01346. isocit_lyase. 2 hits.
PROSITEPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A9G6.
PROP0A9G6.

Entry information

Entry nameACEA_ECOLI
AccessionPrimary (citable) accession number: P0A9G6
Secondary accession number(s): P05313, Q2M6T9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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