Identification
Name:Aconitate hydratase 2
Synonyms:
  • Aconitase
  • Citrate hydro-lyase
Gene Name:acnB
Enzyme Class:
Biological Properties
General Function:Involved in metabolic process
Specific Function:Citrate = isocitrate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
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SMPDB Reactions:
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EcoCyc Reactions:
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Complex Reactions:
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Metabolites:
ECMDB IDNameView
ECMDB06357Cis-2-MethylaconitateMetaboCard
ECMDB00072cis-Aconitic acidMetaboCard
ECMDB00094Citric acidMetaboCard
ECMDB24074D-threo-Isocitric acidMetaboCard
ECMDB04088Isocitric acidMetaboCard
ECMDB06471Methylisocitric acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
4 iron, 4 sulfur cluster binding
aconitate hydratase activity
binding
carbon-oxygen lyase activity
catalytic activity
hydro-lyase activity
iron-sulfur cluster binding
lyase activity
metal cluster binding
protein binding
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
tricarboxylic acid cycle
Gene Properties
Blattner:b0118
Gene OrientationClockwise
Centisome Percentage:2.84
Left Sequence End131615
Right Sequence End134212
Gene Sequence:
>2598 bp
GTGCTAGAAGAATACCGTAAGCACGTAGCTGAGCGTGCCGCTGAGGGGATTGCGCCCAAA
CCCCTGGATGCAAACCAAATGGCCGCACTTGTAGAGCTGCTGAAAAACCCGCCCGCGGGC
GAAGAAGAATTCCTGTTAGATCTGTTAACCAACCGTGTTCCCCCAGGCGTCGATGAAGCC
GCCTATGTCAAAGCAGGCTTCCTGGCTGCTATCGCGAAAGGCGAAGCCAAATCCCCTCTG
CTGACTCCGGAAAAAGCCATCGAACTGCTGGGCACCATGCAGGGTGGTTACAACATTCAT
CCGCTGATCGACGCGCTGGATGATGCCAAACTGGCACCTATTGCTGCCAAAGCACTTTCT
CACACGCTGCTGATGTTCGATAACTTCTATGACGTAGAAGAGAAAGCGAAAGCAGGCAAC
GAATATGCGAAGCAGGTTATGCAGTCCTGGGCGGATGCCGAATGGTTCCTGAATCGCCCG
GCGCTGGCTGAAAAACTGACCGTTACTGTCTTCAAAGTCACTGGCGAAACTAACACCGAT
GACCTTTCTCCGGCACCGGATGCGTGGTCACGCCCGGATATCCCACTGCACGCGCTGGCG
ATGCTGAAAAACGCCCGTGAAGGTATTGAGCCAGACCAGCCTGGTGTTGTTGGTCCGATC
AAGCAAATCGAAGCTCTGCAACAGAAAGGTTTCCCGCTGGCGTACGTCGGTGACGTTGTG
GGTACGGGTTCTTCGCGTAAATCCGCCACTAACTCCGTTCTGTGGTTTATGGGCGATGAT
ATTCCACATGTGCCGAACAAACGCGGCGGTGGTTTGTGCCTCGGCGGTAAAATTGCACCC
ATCTTCTTTAACACGATGGAAGACGCGGGTGCACTGCCAATCGAAGTCGACGTCTCTAAC
CTGAACATGGGCGACGTGATTGACGTTTACCCGTACAAAGGTGAAGTGCGTAACCACGAA
ACCGGCGAACTGCTGGCGACCTTCGAACTGAAAACCGACGTGCTGATTGATGAAGTGCGT
GCTGGTGGCCGTATTCCGCTGATTATCGGGCGTGGCCTGACCACCAAAGCGCGTGAAGCA
CTTGGTCTGCCGCACAGTGATGTGTTCCGTCAGGCGAAAGATGTCGCTGAGAGCGATCGC
GGCTTCTCGCTGGCGCAAAAAATGGTAGGCCGTGCCTGTGGCGTGAAAGGCATTCGTCCG
GGCGCGTACTGTGAACCGAAAATGACTTCTGTAGGTTCCCAGGACACCACCGGCCCGATG
ACCCGTGATGAACTGAAAGACCTGGCGTGCCTGGGCTTCTCGGCTGACCTGGTGATGCAG
TCTTTCTGCCACACCGCGGCGTATCCGAAGCCAGTTGACGTGAACACGCACCACACGCTG
CCGGACTTCATTATGAACCGTGGCGGTGTGTCGCTGCGTCCGGGTGACGGCGTCATTCAC
TCCTGGCTGAACCGTATGCTGCTGCCGGATACCGTCGGTACCGGTGGTGACTCCCATACC
CGTTTCCCGATCGGTATCTCTTTCCCGGCGGGTTCTGGTCTGGTGGCGTTTGCTGCCGCA
ACTGGCGTAATGCCGCTTGATATGCCGGAATCCGTTCTGGTGCGCTTCAAAGGCAAAATG
CAGCCGGGCATCACCCTGCGCGATCTGGTACACGCTATTCCGCTGTATGCGATCAAACAA
GGTCTGCTGACCGTTGAGAAGAAAGGCAAGAAAAACATCTTCTCTGGCCGCATCCTGGAA
ATTGAAGGTCTGCCGGATCTGAAAGTTGAGCAGGCCTTTGAGCTAACCGATGCGTCCGCC
GAGCGTTCTGCCGCTGGTTGTACCATCAAGCTGAACAAAGAACCGATCATCGAATACCTG
AACTCTAACATCGTCCTGCTGAAGTGGATGATCGCGGAAGGTTACGGCGATCGTCGTACC
CTGGAACGTCGTATTCAGGGCATGGAAAAATGGCTGGCGAATCCTGAGCTGCTGGAAGCC
GATGCAGATGCGGAATACGCGGCAGTGATCGACATCGATCTGGCGGATATTAAAGAGCCA
ATCCTGTGTGCTCCGAACGACCCGGATGACGCGCGTCCGCTGTCTGCGGTACAGGGTGAG
AAGATCGACGAAGTGTTTATCGGTTCCTGCATGACCAACATCGGTCACTTCCGTGCTGCG
GGTAAACTGCTGGATGCGCATAAAGGTCAGTTGCCGACCCGCCTGTGGGTGGCACCGCCA
ACCCGTATGGACGCCGCACAGTTGACCGAAGAAGGCTACTACAGCGTCTTCGGTAAGAGT
GGTGCGCGTATCGAGATCCCTGGCTGTTCCCTGTGTATGGGTAACCAGGCGCGTGTGGCG
GACGGTGCAACGGTGGTTTCCACCTCTACCCGTAACTTCCCGAACCGTCTGGGTACTGGC
GCGAATGTCTTCCTGGCTTCTGCGGAACTGGCGGCTGTTGCGGCGCTGATTGGCAAACTG
CCGACGCCGGAAGAGTACCAGACCTACGTGGCGCAGGTAGATAAAACAGCCGTTGATACT
TACCGTTATCTGAACTTCAACCAGCTTTCTCAGTACACCGAGAAAGCCGATGGGGTGATT
TTCCAGACTGCGGTTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:865
Protein Molecular Weight:93497
Protein Theoretical pI:5
PDB File:1L5J
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aconitate hydratase 2
MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEA
AYVKAGFLAAIAKGEAKSPLLTPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALS
HTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLNRPALAEKLTVTVFKVTGETNTD
DLSPAPDAWSRPDIPLHALAMLKNAREGIEPDQPGVVGPIKQIEALQQKGFPLAYVGDVV
GTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSN
LNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREA
LGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPM
TRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIH
SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKM
QPGITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASA
ERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERRIQGMEKWLANPELLEA
DADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFRAA
GKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVA
DGATVVSTSTRNFPNRLGTGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDT
YRYLNFNQLSQYTEKADGVIFQTAV
References
External Links:
ResourceLink
Uniprot ID:P36683
Uniprot Name:ACON2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674339
PDB ID:1L5J
Ecogene ID:EG12316
Ecocyc:EG12316
ColiBase:b0118
Kegg Gene:b0118
EchoBASE ID:EB2222
CCDB:ACON2_ECOLI
BacMap:16128111
General Reference:
  • 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
  • Bradbury, A. J., Gruer, M. J., Rudd, K. E., Guest, J. R. (1996). "The second aconitase (AcnB) of Escherichia coli." Microbiology 142 ( Pt 2):389-400. Pubmed: 8932712
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Gruer, M. J., Guest, J. R. (1994). "Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli." Microbiology 140 ( Pt 10):2531-2541. Pubmed: 8000525
  • 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
  • Jordan, P. A., Tang, Y., Bradbury, A. J., Thomson, A. J., Guest, J. R. (1999). "Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)." Biochem J 344 Pt 3:739-746. Pubmed: 10585860
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Williams, C. H., Stillman, T. J., Barynin, V. V., Sedelnikova, S. E., Tang, Y., Green, J., Guest, J. R., Artymiuk, P. J. (2002). "E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition." Nat Struct Biol 9:447-452. Pubmed: 11992126