Isocitrate lyase (P0A9G6)

Identification
Name:Isocitrate lyase
Synonyms:
  • ICL
  • Isocitrase
  • Isocitratase
Gene Name:aceA
Enzyme Class:
Biological Properties
General Function:Involved in isocitrate lyase activity
Specific 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
Cellular Location:Cytoplasm
SMPDB Pathways:
  • Secondary Metabolites: Glyoxylate cycle PW000967
  • glycolate and glyoxylate degradation II PW002021
KEGG Pathways:
  • Glyoxylate and dicarboxylate metabolism ec00630
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Isocitric acid ↔ 1.0Glyoxylic acid + 1.0Succinic acid
ReactionCard
SMPDB Reactions:
1.0Isocitric acid+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Isocitric acid + 1.0Isocitric acid ↔ 1.0Succinic acid + 1.0Glyoxylic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Isocitric acid ↔ 1.0Glyoxylic acid + 1.0Succinic acid
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Isocitric acid → 1.0Succinic acid + 1.0Glyoxylic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00119Glyoxylic acidMetaboCard
ECMDB04088Isocitric acidMetaboCard
ECMDB00254Succinic acidMetaboCard
GO Classification:
Function
carbon-carbon lyase activity
catalytic activity
isocitrate lyase activity
lyase activity
oxo-acid-lyase activity
Process
carboxylic acid metabolic process
cellular metabolic process
metabolic process
organic acid metabolic process
oxoacid metabolic process
Gene Properties
Blattner:b4015
Gene OrientationClockwise
Centisome Percentage:90.85
Left Sequence End4215132
Right Sequence End4216436
Gene Sequence:
>1305 bp
ATGAAATTTCCCGGTAAACGTAAATCCAAACATTACTTCCCCGTAAACGCACGCGATCCG
CTGCTTCAGCAATTCCAGCCAGAAAACGAAACCAGCGCTGCCTGGGTAGTGGGTATCGAT
CAAACGCTGGTCGATATTGAAGCGAAAGTGGATGATGAATTTATTGAGCGTTATGGATTA
AGCGCCGGGCATTCACTGGTGATTGAGGATGATGTAGCCGAAGCGCTTTATCAGGAACTA
AAACAGAAAAACCTGATTACCCATCAGTTTGCGGGTGGCACCATTGGTAACACCATGCAC
AACTACTCGGTGCTCGCGGACGACCGTTCGGTGCTGCTGGGCGTCATGTGCAGCAATATT
GAAATTGGCAGTTATGCCTATCGTTACCTGTGTAACACTTCCAGCCGTACCGATCTTAAC
TATCTACAAGGCGTGGATGGCCCGATTGGTCGTTGCTTTACGCTGATTGGCGAGTCCGGG
GAACGTACCTTTGCTATCAGTCCAGGCCACATGAACCAGCTGCGGGCTGAAAGCATTCCG
GAAGATGTGATTGCCGGAGCCTCGGCACTGGTTCTCACCTCATATCTGGTGCGTTGCAAG
CCGGGTGAACCCATGCCGGAAGCAACCATGAAAGCCATTGAGTACGCGAAGAAATATAAC
GTACCGGTGGTGCTGACGCTGGGCACCAAGTTTGTCATTGCCGAGAATCCGCAGTGGTGG
CAGCAATTCCTCAAAGATCACGTCTCTATCCTTGCGATGAACGAAGATGAAGCCGAAGCG
TTGACCGGAGAAAGCGATCCGTTGTTGGCATCTGACAAGGCGCTGGACTGGGTAGATCTG
GTGCTGTGCACCGCCGGGCCAATCGGCTTGTATATGGCGGGCTTTACCGAAGACGAAGCG
AAACGTAAAACCCAGCATCCGCTGCTGCCGGGCGCTATAGCGGAATTCAACCAGTATGAG
TTTAGCCGCGCCATGCGCCACAAGGATTGCCAGAATCCGCTGCGTGTATATTCGCACATT
GCGCCGTACATGGGCGGGCCGGAAAAAATCATGAACACTAATGGAGCGGGGGATGGCGCA
TTGGCAGCGTTGCTGCATGACATTACCGCCAACAGCTACCATCGTAGCAACGTACCAAAC
TCCAGCAAACATAAATTCACCTGGTTAACTTATTCATCGTTAGCGCAGGTGTGTAAATAT
GCTAACCGTGTGAGCTATCAGGTACTGAACCAGCATTCACCTCGTTTAACGCGCGGCTTG
CCGGAGCGTGAAGACAGCCTGGAAGAGTCTTACTGGGATCGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:434
Protein Molecular Weight:47521
Protein Theoretical pI:5
PDB File:1IGW
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Isocitrate lyase
MKTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAAKMWRLLHGE
SKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANLAASMYPDQSLYPANSVPAV
VERINNTFRRADQIQWSAGIEPGDPRYVDYFLPIVADAEAGFGGVLNAFELMKAMIEAGA
AAVHFEDQLASVKKCGHMGGKVLVPTQEAIQKLVAARLAADVTGVPTLLVARTDADAADL
ITSDCDPYDSEFITGERTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARR
FAQAIHAKYPGKLLAYNCSPSFNWQKNLDDKTIASFQQQLSDMGYKFQFITLAGIHSMWF
NMFDLANAYAQGEGMKHYVEKVQQPEFAAAKDGYTFVSHQQEVGTGYFDKVTTIIQGGTS
SVTALTGSTEESQF
References
External Links:
ResourceLink
Uniprot ID:P0A9G6
Uniprot Name:ACEA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674616
PDB ID:1IGW
Ecogene ID:EG10022
Ecocyc:EG10022
ColiBase:b4015
Kegg Gene:b4015
EchoBASE ID:EB0021
CCDB:ACEA_ECOLI
BacMap:16131841
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Byrne, C., Stokes, H. W., Ward, K. A. (1988). "Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli." Nucleic Acids Res 16:10924. Pubmed: 3060852
  • Byrne, C., Stokes, H. W., Ward, K. A. (1988). "Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli." Nucleic Acids Res 16:9342. Pubmed: 3050899
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hoyt, J. C., Robertson, E. F., Berlyn, K. A., Reeves, H. C. (1988). "Escherichia coli isocitrate lyase: properties and comparisons." Biochim Biophys Acta 966:30-35. Pubmed: 3291954
  • Klumpp, D. J., Plank, D. W., Bowdin, L. J., Stueland, C. S., Chung, T., LaPorte, D. C. (1988). "Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase." J Bacteriol 170:2763-2769. Pubmed: 2836370
  • Matsuoka, M., McFadden, B. A. (1988). "Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli." J Bacteriol 170:4528-4536. Pubmed: 3049537
  • Rieul, C., Bleicher, F., Duclos, B., Cortay, J. C., Cozzone, A. J. (1988). "Nucleotide sequence of the aceA gene coding for isocitrate lyase in Escherichia coli." Nucleic Acids Res 16:5689. Pubmed: 3290857
  • Robertson, A. G., Nimmo, H. G. (1995). "Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308." Biochem J 305 ( Pt 1):239-244. Pubmed: 7826335
  • Robertson, E. F., Hoyt, J. C., Reeves, H. C. (1988). "Evidence of histidine phosphorylation in isocitrate lyase from Escherichia coli." J Biol Chem 263:2477-2482. Pubmed: 3276689