ECMDB

Identification

Name:

Aconitate hydratase 1

Synonyms:

Aconitase 1
Citrate hydro-lyase 1

Gene Name:

acnA

Enzyme Class:

4.2.1.3

Biological Properties

General Function:

Involved in metabolic process

Specific Function:

May have an iron-responsive regulatory function

Cellular Location:

Not Available

SMPDB Pathways:

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
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

1.0Citric acid ↔ 1.0Isocitric acid
ReactionCard

1.0

↔

1.0

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

1.0

↔

1.0

1.0Citric 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

1.0Water + 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

Complex Reactions:

1.0

→

1.0

1.0Citric acid → 1.0Isocitric acid
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00072	cis-Aconitic acid	MetaboCard
ECMDB00094	Citric acid	MetaboCard
ECMDB24074	D-threo-Isocitric acid	MetaboCard
ECMDB04088	Isocitric acid	MetaboCard
ECMDB00494	Water	MetaboCard

GO Classification:

Function
4 iron, 4 sulfur cluster binding
binding
iron-sulfur cluster binding
metal cluster binding
Process
metabolic process

Gene Properties

Blattner:

b1276

Gene Orientation

Clockwise

Centisome Percentage:

28.75

Left Sequence End

1333855

Right Sequence End

1336530

Gene Sequence:

>2676 bp
ATGTCGTCAACCCTACGAGAAGCCAGTAAGGACACGTTGCAGGCCAAAGATAAAACTTAC
CACTACTACAGCCTGCCGCTTGCTGCTAAATCACTGGGCGATATCACCCGTCTACCCAAG
TCACTCAAAGTTTTGCTCGAAAACCTGCTGCGCTGGCAGGATGGTAACTCGGTTACCGAA
GAGGATATCCACGCGCTGGCAGGATGGCTGAAAAATGCCCATGCTGACCGTGAAATTGCC
TACCGCCCGGCAAGGGTGCTGATGCAGGACTTTACCGGCGTACCTGCCGTTGTTGATCTG
GCGGCAATGCGCGAAGCGGTTAAACGCCTCGGCGGCGATACTGCAAAGGTTAACCCGCTC
TCACCGGTCGACCTGGTCATTGACCACTCGGTGACCGTCGATCGTTTTGGTGATGATGAG
GCATTTGAAGAAAACGTACGCCTGGAAATGGAGCGCAACCACGAACGTTATGTGTTCCTG
AAATGGGGAAAGCAAGCGTTCAGTCGGTTTAGCGTCGTGCCGCCAGGCACAGGCATTTGC
CATCAGGTTAACCTCGAATATCTCGGCAAAGCAGTGTGGAGTGAATTGCAGGACGGTGAA
TGGATTGCTTATCCGGATACACTCGTTGGTACTGACTCGCACACCACCATGATCAACGGC
CTTGGCGTGCTGGGGTGGGGCGTTGGTGGGATCGAAGCAGAAGCCGCAATGTTAGGCCAG
CCGGTTTCCATGCTTATCCCGGATGTAGTGGGCTTCAAACTTACCGGAAAATTACGTGAA
GGTATTACCGCCACAGACCTGGTTCTCACTGTTACCCAAATGCTGCGCAAACATGGCGTG
GTGGGGAAATTCGTCGAATTTTATGGTGATGGTCTGGATTCACTACCGTTGGCGGATCGC
GCCACCATTGCCAATATGTCGCCAGAATATGGTGCCACCTGTGGCTTCTTCCCAATCGAT
GCTGTAACCCTCGATTACATGCGTTTAAGCGGGCGCAGCGAAGATCAGGTCGAGTTGGTC
GAAAAATATGCCAAAGCGCAGGGCATGTGGCGTAACCCGGGCGATGAACCAATTTTTACC
AGTACGTTAGAACTGGATATGAATGACGTTGAAGCGAGCCTGGCAGGGCCTAAACGCCCA
CAGGATCGCGTTGCACTGCCCGATGTACCAAAAGCATTTGCCGCCAGTAACGAACTGGAA
GTGAATGCCACGCATAAAGATCGCCAGCCGGTCGATTATGTTATGAACGGACATCAGTAT
CAGTTACCTGATGGCGCTGTGGTCATTGCTGCGATAACCTCGTGCACCAACACCTCTAAC
CCAAGTGTGCTGATGGCCGCAGGCTTGCTGGCGAAAAAAGCCGTAACTCTGGGCCTCAAG
CGGCAACCATGGGTCAAAGCGTCGCTGGCACCGGGTTCGAAAGTCGTTTCTGATTATCTG
GCAAAAGCGAAACTGACACCGTATCTCGACGAACTGGGGTTTAACCTTGTGGGATACGGT
TGTACCACCTGTATTGGTAACTCTGGGCCGCTGCCCGATCCTATCGAAACGGCAATCAAA
AAAGGCGATTTAACCGTCGGTGCGGTGCTGTCCGGCAACCGTAACTTTGAAGGCCGTATC
CATCCGCTGGTTAAAACTAACTGGCTGGCCTCGCCGCCGCTGGTGGTTGCCTATGCGCTG
GCGGGAAATATGAATATCAACCTGGCTTCTGAGCCTATCGGCCATGATCGCAAAGGCGAT
CCGGTTTATCTGAAAGATATCTGGCCATCGGCACAAGAAATTGCCCGTGCGGTAGAACAA
GTCTCCACAGAAATGTTCCGCAAAGAGTACGCAGAAGTTTTTGAAGGCACAGCAGAGTGG
AAGGGAATTAACGTCACACGATCCGATACCTACGGTTGGCAGGAGGACTCAACCTATATT
CGCTTATCGCCTTTCTTTGATGAAATGCAGGCAACACCAGCACCAGTGGAAGATATTCAC
GGTGCGCGGATCCTCGCAATGCTGGGGGATTCAGTCACCACTGACCATATCTCTCCGGCG
GGCAGTATTAAGCCCGACAGCCCAGCGGGTCGATATCTACAAGGTCGGGGTGTTGAGCGA
AAAGACTTTAACTCCTACGGTTCGCGGCGTGGTAACCATGAAGTGATGATGCGCGGCACC
TTCGCCAATATTCGCATCCGTAATGAAATGGTGCCTGGCGTTGAAGGGGGGATGACGCGG
CATTTACCTGACAGCGACGTAGTCTCTATTTATGATGCTGCGATGCGCTATAAGCAGGAG
CAAACGCCGCTGGCGGTGATTGCCGGGAAAGAGTATGGATCAGGCTCCAGTCGTGACTGG
GCGGCAAAAGGTCCGCGTCTGCTTGGTATTCGTGTGGTGATTGCCGAATCGTTTGAACGA
ATTCACCGTTCGAATTTAATTGGCATGGGCATCCTGCCGCTGGAATTTCCGCAAGGCGTA
ACGCGTAAAACGTTAGGGCTAACCGGGGAAGAGAAGATTGATATTGGCGATCTGCAAAAC
CTACAACCCGGCGCGACGGTTCCGGTGACGCTTACGCGCGCGGATGGTAGCCAGGAAGTC
GTACCCTGCCGTTGTCGTATCGACACCGCGACGGAGTTGACCTACTACCAGAACGACGGC
ATTTTGCATTATGTCATTCGTAATATGTTGAAGTAA

Protein Properties

Pfam Domain Function:

Aconitase (PF00330 )
Aconitase_C (PF00694 )

Protein Residues:

891

Protein Molecular Weight:

97676

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Aconitate hydratase 1
MSSTLREASKDTLQAKDKTYHYYSLPLAAKSLGDITRLPKSLKVLLENLLRWQDGNSVTE
EDIHALAGWLKNAHADREIAYRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPL
SPVDLVIDHSVTVDRFGDDEAFEENVRLEMERNHERYVFLKWGKQAFSRFSVVPPGTGIC
HQVNLEYLGKAVWSELQDGEWIAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ
PVSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADR
ATIANMSPEYGATCGFFPIDAVTLDYMRLSGRSEDQVELVEKYAKAQGMWRNPGDEPIFT
STLELDMNDVEASLAGPKRPQDRVALPDVPKAFAASNELEVNATHKDRQPVDYVMNGHQY
QLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYL
AKAKLTPYLDELGFNLVGYGCTTCIGNSGPLPDPIETAIKKSDLTVGAVLSGNRNFEGRI
HPLVKTNWLASPPLVVAYALAGNMNINLASEPIGHDRKGDPVYLKDIWPSAQEIARAVEQ
VSTEMFRKEYAEVFEGTAEWKGINVTRSDTYGWQEDSTYIRLSPFFDEMQATPAPVEDIH
GARILAMLGDSVTTDHISPAGSIKPDSPAGRYLQGRGVERKDFNSYGSRRGNHEVMMRGT
FANIRIRNEMVPGVEGGMTRHLPDSDVVSIYDAAMRYKQEQTPLAVIAGKEYGSGSSRDW
AAKGPRLLGIRVVIAESFERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEKIDIGDLQN
LQPGATVPVTLTRADGSQEVVPCRCRIDTATELTYYQNDGILHYVIRNMLK

References

External Links:

Resource	Link
Uniprot ID:	P25516
Uniprot Name:	ACON1_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	1742087
Ecogene ID:	EG11325
Ecocyc:	EG11325
ColiBase:	b1276
Kegg Gene:	b1276
EchoBASE ID:	EB1301
CCDB:	ACON1_ECOLI
BacMap:	16129237

General Reference:

Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
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
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
Prodromou, C., Artymiuk, P. J., Guest, J. R. (1992). "The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases." Eur J Biochem 204:599-609. Pubmed: 1541275
Prodromou, C., Haynes, M. J., Guest, J. R. (1991). "The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn)." J Gen Microbiol 137:2505-2515. Pubmed: 1838390

Aconitate hydratase 1 (P25516)