Acetolactate synthase isozyme 3 large subunit (P00893)

Identification
Name:Acetolactate synthase isozyme 3 large subunit
Synonyms:
  • AHAS-III
  • ALS-III
  • Acetohydroxy-acid synthase III large subunit
Gene Name:ilvI
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:2 pyruvate = 2-acetolactate + CO(2)
Cellular Location:Not Available
SMPDB Pathways:
  • 2-Oxopent-4-enoate metabolism PW001890
  • 2-Oxopent-4-enoate metabolism 2 PW002035
  • Operon: acetolactate synthase III activation PW001881
  • Pantothenate and CoA biosynthesis PW000828
  • Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate PW000978
  • Valine Biosynthesis PW000812
  • isoleucine biosynthesis PW000818
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Ketobutyric acid + 1.0Hydrogen ion + 1.0Pyruvic acid → 1.02-Aceto-2-hydroxy-butyrate + 1.0Carbon dioxide
ReactionCard
1.0Thumb+2.0Thumb → 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 2.0Pyruvic acid → 1.0(S)-2-Acetolactate + 1.0Carbon dioxide
ReactionCard
1.0Thumb+1.0Thumb ↔ 2.0Thumb
1.02-Acetolactate + 1.0Carbon dioxide ↔ 2.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 2.0Thumb
1.0(S)-2-Acetolactate + 1.0Carbon dioxide ↔ 2.0Pyruvic acid
ReactionCard
2.0Thumb → 1.0Thumb+1.0Thumb
2.0Pyruvic acid → 1.02-Acetolactate + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Pyruvic acid → 1.0Carbon dioxide + 1.02-Acetolactate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Ketobutyric acid + 1.0Hydrogen ion + 1.0Pyruvic acid → 1.02-Aceto-2-hydroxy-butyrate + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB06855(S)-2-AcetolactateMetaboCard
ECMDB040012-Aceto-2-hydroxy-butyrateMetaboCard
ECMDB040022-AcetolactateMetaboCard
ECMDB000052-Ketobutyric acidMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01372Thiamine pyrophosphateMetaboCard
GO Classification:
Function
acetolactate synthase activity
adenyl nucleotide binding
binding
catalytic activity
cation binding
FAD or FADH2 binding
ion binding
magnesium ion binding
metal ion binding
nucleoside binding
purine nucleoside binding
thiamin pyrophosphate binding
transferase activity
transferase activity, transferring aldehyde or ketonic groups
vitamin binding
Process
branched chain family amino acid biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b0077
Gene OrientationClockwise
Centisome Percentage:1.85
Left Sequence End85630
Right Sequence End87354
Gene Sequence:
>1725 bp
ATGGAGATGTTGTCTGGAGCCGAGATGGTCGTCCGATCGCTTATCGATCAGGGCGTTAAA
CAAGTATTCGGTTATCCCGGAGGCGCAGTCCTTGATATTTATGATGCATTGCATACCGTG
GGTGGTATTGATCATGTATTAGTTCGTCATGAGCAGGCGGCGGTGCATATGGCCGATGGC
CTGGCGCGCGCGACCGGGGAAGTCGGCGTCGTGCTGGTAACGTCGGGTCCAGGGGCGACC
AATGCGATTACTGGCATCGCCACCGCTTATATGGATTCCATTCCATTAGTTGTCCTTTCC
GGGCAGGTAGCGACCTCGTTGATAGGTTACGATGCCTTTCAGGAGTGCGACATGGTGGGG
ATTTCGCGACCGGTGGTTAAACACAGTTTTCTGGTTAAGCAAACGGAAGACATTCCGCAG
GTGCTGAAAAAGGCTTTCTGGCTGGCGGCAAGTGGTCGCCCAGGACCAGTAGTCGTTGAT
TTACCGAAAGATATTCTTAATCCGGCGAACAAATTACCCTATGTCTGGCCGGAGTCGGTC
AGTATGCGTTCTTACAATCCCACTACTACCGGACATAAAGGGCAAATTAAGCGTGCTCTG
CAAACGCTGGTAGCGGCAAAAAAACCGGTTGTCTACGTAGGCGGTGGGGCAATCACGGCG
GGCTGCCATCAGCAGTTGAAAGAAACGGTGGAGGCGTTGAATCTGCCCGTTGTTTGCTCA
TTGATGGGGCTGGGGGCGTTTCCGGCAACGCATCGTCAGGCACTGGGCATGCTGGGAATG
CACGGTACCTACGAAGCCAATATGACGATGCATAACGCGGATGTGATTTTCGCCGTCGGG
GTACGATTTGATGACCGAACGACGAACAATCTGGCAAAGTACTGCCCAAATGCCACTGTT
CTGCATATCGATATTGATCCTACTTCCATTTCTAAAACCGTGACTGCGGATATCCCGATT
GTGGGGGATGCTCGCCAGGTCCTCGAACAAATGCTTGAACTCTTGTCGCAAGAATCCGCC
CATCAACCACTGGATGAGATCCGCGACTGGTGGCAGCAAATTGAACAGTGGCGCGCTCGT
CAGTGCCTGAAATATGACACTCACAGTGAAAAGATTAAACCGCAGGCGGTGATCGAGACT
CTTTGGCGGTTGACGAAGGGAGACGCTTACGTGACGTCCGATGTCGGGCAGCACCAGATG
TTTGCTGCACTTTATTATCCATTCGACAAACCGCGTCGCTGGATCAATTCCGGTGGCCTC
GGCACGATGGGTTTTGGTTTACCTGCGGCACTGGGCGTCAAAATGGCGTTGCCAGAAGAA
ACCGTGGTTTGCGTCACTGGCGACGGCAGTATTCAGATGAACATCCAGGAACTGTCTACC
GCGTTGCAATACGAGTTGCCCGTACTGGTGGTGAATCTCAATAACCGCTATCTGGGGATG
GTGAAGCAGTGGCAGGACATGATCTATTCCGGCCGTCATTCACAATCTTATATGCAATCG
CTACCCGATTTCGTCCGTCTGGCGGAAGCCTATGGGCATGTCGGGATCCAGATTTCTCAT
CCGCATGAGCTGGAAAGCAAACTTAGCGAGGCGCTGGAACAGGTGCGCAATAATCGCCTG
GTGTTTGTTGATGTTACCGTCGATGGCAGCGAGCACGTCTACCCGATGCAGATTCGCGGG
GGCGGAATGGATGAAATGTGGTTAAGCAAAACGGAGAGAACCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:574
Protein Molecular Weight:62984
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetolactate synthase isozyme 3 large subunit
MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADG
LARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVG
ISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILNPANKLPYVWPESV
SMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS
LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATV
LHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRAR
QCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGL
GTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM
VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRL
VFVDVTVDGSEHVYPMQIRGGGMDEMWLSKTERT
References
External Links:
ResourceLink
Uniprot ID:P00893
Uniprot Name:ILVI_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674319
Ecogene ID:EG10500
Ecocyc:EG10500
ColiBase:b0077
Kegg Gene:b0077
EchoBASE ID:EB0495
CCDB:ILVI_ECOLI
BacMap:90111084
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
  • Haughn, G. W., Squires, C. H., De Felice, M., Largo, C. T., Calvo, J. M. (1985). "Unusual organization of the ilvIH promoter of Escherichia coli." J Bacteriol 163:186-198. Pubmed: 3891724
  • 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
  • Squires, C. H., De Felice, M., Devereux, J., Calvo, J. M. (1983). "Molecular structure of ilvIH and its evolutionary relationship to ilvG in Escherichia coli K12." Nucleic Acids Res 11:5299-5313. Pubmed: 6308579
  • 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