Identification |
---|
Name: | 2-isopropylmalate synthase |
---|
Synonyms: | - Alpha-IPM synthase
- Alpha-isopropylmalate synthase
|
---|
Gene Name: | leuA |
---|
Enzyme Class: | |
---|
Biological Properties |
---|
General Function: | Involved in 2-isopropylmalate synthase activity |
---|
Specific Function: | Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) |
---|
Cellular Location: | Not Available |
---|
SMPDB Pathways: | - Leucine Biosynthesis PW000811
- Operon: leucine biosynthesis PW001880
- Secondary Metabolite: Leucine biosynthesis PW000980
- Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate PW000978
|
---|
KEGG Pathways: | |
---|
KEGG Reactions: | |
1.0 | + | 1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
| | | |
|
---|
SMPDB Reactions: | |
1.03-Methyl-2-oxovaleric acid | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
| |
|
---|
EcoCyc Reactions: | |
1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
| |
|
---|
Metabolites: | |
---|
GO Classification: | Function |
---|
2-isopropylmalate synthase activity | catalytic activity | transferase activity | transferase activity, transferring acyl groups | transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer | Process |
---|
branched chain family amino acid metabolic process | carboxylic acid metabolic process | cellular amino acid and derivative metabolic process | cellular amino acid metabolic process | cellular metabolic process | leucine biosynthetic process | leucine metabolic process | metabolic process | organic acid metabolic process | oxoacid metabolic process |
|
---|
Gene Properties |
---|
Blattner: | b0074 |
---|
Gene Orientation | Counterclockwise |
---|
Centisome Percentage: | 1.77 |
---|
Left Sequence End | 81958 |
---|
Right Sequence End | 83529 |
---|
Gene Sequence: | >1572 bp
ATGAGCCAGCAAGTCATTATTTTCGATACCACATTGCGCGACGGTGAACAGGCGTTACAG
GCAAGCTTGAGTGTGAAAGAAAAACTGCAAATTGCGCTGGCCCTTGAGCGTATGGGTGTT
GACGTGATGGAAGTCGGTTTCCCCGTCTCTTCGCCGGGCGATTTTGAATCGGTGCAAACC
ATCGCCCGCCAGGTTAAAAACAGCCGCGTATGTGCGTTAGCTCGCTGCGTGGAAAAAGAT
ATCGACGTGGCGGCCGAATCCCTGAAAGTCGCCGAAGCCTTCCGTATTCATACCTTTATT
GCCACTTCGCCAATGCACATCGCCACCAAGCTGCGCAGCACGCTGGACGAGGTGATCGAA
CGCGCTATCTATATGGTGAAACGCGCCCGTAATTACACCGATGATGTTGAATTTTCTTGC
GAAGATGCCGGGCGTACACCCATTGCCGATCTGGCGCGAGTGGTCGAAGCGGCGATTAAT
GCCGGTGCCACCACCATCAACATTCCGGACACCGTGGGCTACACCATGCCGTTTGAGTTC
GCCGGAATCATCAGCGGCCTGTATGAACGCGTGCCTAACATCGACAAAGCCATTATCTCC
GTACATACCCACGACGATTTGGGCCTGGCGGTCGGAAACTCACTGGCGGCGGTACATGCC
GGTGCACGCCAGGTGGAAGGCGCAATGAACGGGATCGGCGAGCGTGCCGGAAACTGTTCC
CTGGAAGAAGTCATCATGGCGATCAAAGTTCGTAAGGATATTCTCAACGTCCACACCGCC
ATTAATCACCAGGAGATATGGCGCACCAGCCAGTTAGTTAGCCAGATTTGTAATATGCCG
ATCCCGGCAAACAAAGCCATTGTTGGCAGCGGCGCATTCGCACACTCCTCCGGTATACAC
CAGGATGGCGTGCTGAAAAACCGCGAAAACTACGAAATCATGACACCAGAATCTATTGGT
CTGAACCAAATCCAGCTGAATCTGACCTCTCGTTCGGGGCGTGCGGCGGTGAAACATCGC
ATGGATGAGATGGGGTATAAAGAAAGTGAATATAATTTAGACAATTTGTACGATGCTTTC
CTGAAGCTGGCGGACAAAAAAGGTCAGGTGTTTGATTACGATCTGGAGGCGCTGGCCTTC
ATCGGTAAGCAGCAAGAAGAGCCGGAGCATTTCCGTCTGGATTACTTCAGCGTGCAGTCT
GGCTCTAACGATATCGCCACCGCCGCCGTCAAACTGGCCTGTGGCGAAGAAGTCAAAGCA
GAAGCCGCCAACGGTAACGGTCCGGTCGATGCCGTCTATCAGGCAATTAACCGCATCACT
GAATATAACGTCGAACTGGTGAAATACAGCCTGACCGCCAAAGGCCACGGTAAAGATGCG
CTGGGTCAGGTGGATATCGTCGCTAACTACAACGGTCGCCGCTTCCACGGCGTCGGCCTG
GCTACCGATATTGTCGAGTCATCTGCCAAAGCCATGGTGCACGTTCTGAACAATATCTGG
CGTGCCGCAGAAGTCGAAAAAGAGTTGCAACGCAAAGCTCAACACAACGAAAACAACAAG
GAAACCGTGTGA |
---|
Protein Properties |
---|
Pfam Domain Function: | |
---|
Protein Residues: | 523 |
---|
Protein Molecular Weight: | 57297 |
---|
Protein Theoretical pI: | 5 |
---|
Signaling Regions: | |
---|
Transmembrane Regions: | |
---|
Protein Sequence: | >2-isopropylmalate synthase
MSQQVIIFDTTLRDGEQALQASLSVKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQT
IARQVKNSRVCALARCVEKDIDVAAESLKVAEAFRIHTFIATSPMHIATKLRSTLDEVIE
RAIYMVKRARNYTDDVEFSCEDAGRTPIADLARVVEAAINAGATTINIPDTVGYTMPFEF
AGIISGLYERVPNIDKAIISVHTHDDLGLAVGNSLAAVHAGARQVEGAMNGIGERAGNCS
LEEVIMAIKVRKDILNVHTAINHQEIWRTSQLVSQICNMPIPANKAIVGSGAFAHSSGIH
QDGVLKNRENYEIMTPESIGLNQIQLNLTSRSGRAAVKHRMDEMGYKESEYNLDNLYDAF
LKLADKKGQVFDYDLEALAFIGKQQEEPEHFRLDYFSVQSGSNDIATAAVKLACGEEVKA
EAANGNGPVDAVYQAINRITEYNVELVKYSLTAKGHGKDALGQVDIVANYNGRRFHGVGL
ATDIVESSAKAMVHVLNNIWRAAEVEKELQRKAQHNENNKETV |
---|
References |
---|
External Links: | |
---|
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
- 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
- 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
- Wessler, S. R., Calvo, J. M. (1981). "Control of leu operon expression in Escherichia coli by a transcription attenuation mechanism." J Mol Biol 149:579-597. Pubmed: 6171647
- Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901
|
---|