ECMDB

Identification

Name:

Aconitate hydratase 2

Synonyms:

Aconitase
Citrate hydro-lyase

Gene Name:

acnB

Enzyme Class:

4.2.1.3

Biological Properties

General Function:

Involved in metabolic process

Specific Function:

Citrate = isocitrate

Cellular Location:

Not Available

SMPDB Pathways:

Propanoate metabolism PW000940
Secondary Metabolites: Glyoxylate cycle PW000967
TCA cycle PW000779
TCA cycle (ubiquinol-0) PW002023
TCA cycle (ubiquinol-10) PW001010
TCA cycle (ubiquinol-2) PW001002
TCA cycle (ubiquinol-3) PW001003
TCA cycle (ubiquinol-4) PW001004
TCA cycle (ubiquinol-5) PW001005
TCA cycle (ubiquinol-6) PW001006
TCA cycle (ubiquinol-7) PW001007
TCA cycle (ubiquinol-8) PW001008
TCA cycle (ubiquinol-9) PW001009
glycolate and glyoxylate degradation II PW002021

KEGG Pathways:

Citrate cycle (TCA cycle) ec00020
Glyoxylate and dicarboxylate metabolism ec00630
Metabolic pathways eco01100
Microbial metabolism in diverse environments ec01120
Propanoate metabolism ec00640
Reductive carboxylate cycle (CO2 fixation) ec00720

KEGG Reactions:

1.0

↔

1.0

1.0cis-Aconitic acid + 1.0Water ↔ 1.0Isocitric acid
ReactionCard

1.0

↔

1.0

1.0Citric acid ↔ 1.0cis-Aconitic acid + 1.0Water
ReactionCard

1.0

↔

1.0

1.0Cis-2-Methylaconitate + 1.0Water ↔ 1.0Methylisocitric acid
ReactionCard

1.0

↔

1.0

1.0Citric acid ↔ 1.0Isocitric acid
ReactionCard

1.0

↔

1.0

1.0Isocitric acid ↔ 1.0cis-Aconitic acid + 1.0Water
ReactionCard

1.0

↔

1.0

1.0Methylisocitric acid ↔ 1.0Cis-2-Methylaconitate + 1.0Water
ReactionCard

1.0

↔

1.0

1.0Citric acid + 1.0cis-Aconitic acid + 1.0Water ↔ 1.0Isocitric acid
ReactionCard

SMPDB Reactions:

1.0

→

1.0

1.0Citric acid → 1.0Water + 1.0cis-Aconitic acid
ReactionCard

1.0

→

1.0

1.0cis-Aconitic acid + 1.0Water → 1.0D-threo-Isocitric acid
ReactionCard

1.0

→

1.0

1.0Cis-2-Methylaconitate → 1.0Water + 1.0Methylisocitric acid
ReactionCard

1.0

↔

1.0

1.0Water + 1.0cis-Aconitic acid ↔ 1.0Citric acid
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.0cis-Aconitic acid + 1.0Water ↔ 1.0Isocitric acid
ReactionCard

1.0

↔

1.0

1.0Citric acid ↔ 1.0cis-Aconitic acid + 1.0Water
ReactionCard

1.0

↔

1.0

1.0Cis-2-Methylaconitate + 1.0Water ↔ 1.0Methylisocitric acid
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB06357	Cis-2-Methylaconitate	MetaboCard
ECMDB00072	cis-Aconitic acid	MetaboCard
ECMDB00094	Citric acid	MetaboCard
ECMDB24074	D-threo-Isocitric acid	MetaboCard
ECMDB04088	Isocitric acid	MetaboCard
ECMDB06471	Methylisocitric acid	MetaboCard
ECMDB00494	Water	MetaboCard

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 Orientation

Clockwise

Centisome Percentage:

2.84

Left Sequence End

131615

Right Sequence End

134212

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:

Aconitase (PF00330 )
Aconitase_2_N (PF06434 )
Aconitase_B_N (PF11791 )

Protein Residues:

865

Protein Molecular Weight:

93497

Protein Theoretical pI:

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:

Resource	Link
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

Aconitate hydratase 2 (P36683)