Acetolactate synthase isozyme 2 large subunit (P00892)

Identification
Name:Acetolactate synthase isozyme 2 large subunit
Synonyms:
  • AHAS-II
  • ALS-II
  • Acetohydroxy-acid synthase II large subunit
Gene Name:ilvG
Enzyme Class:
Biological Properties
General Function:Amino acid transport and metabolism
Specific Function:Catalyzes the first step in the biosynthesis of branched-chain amino acids
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 2.0Thumb
1.02-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
Metabolites:
ECMDB IDNameView
ECMDB040012-Aceto-2-hydroxy-butyrateMetaboCard
ECMDB040022-AcetolactateMetaboCard
ECMDB000052-Ketobutyric acidMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00243Pyruvic acidMetaboCard
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:Not Available
Gene OrientationNot Available
Centisome Percentage:Not Available
Left Sequence EndNot Available
Right Sequence EndNot Available
Gene Sequence:
>1647 bp
ATGAATGGCGCACAGTGGGTGGTACATGCGTTGCGGGCACAGGGTGTGAACACCGTTTTC
GGTTATCCGGGTGGCGCAATTATGCCGGTTTACGATGCATTGTATGACGGCGGCGTGGAG
CACTTGCTATGCCGACATGAGCAGGGTGCGGCAATGGCGGCTATCGGTTATGCTCGTGCT
ACCGGCAAAACTGGCGTATGTATCGCCACGTCTGGTCCGGGCGCAACCAACCTGATAACC
GGGCTTGCGGACGCACTGTTAGATTCCATCCCTGTTGTTGCCATCACCGGTCAAGTGTCC
GCACCGTTTATCGGCACTGACGCATTTCAGGAAGTGGATGTCCTGGGATTGTCGTTAGCC
TGTACCAAGCATAGCTTTCTGGTGCAGTCGCTGGAAGAGTTGCCGCGCATCATGGCTGAA
GCATTCGACGTTGCCTGCTCAGGTCGTCCTGGTCCGGTTCTGGTCGATATCCCAAAAGAT
ATCCAGTTAGCCAGCGGTGACCTGGAACCGTGGTTCACCACCGTTGAAAACGAAGTGACT
TTCCCACATGCCGAAGTTGAGCAAGCGCGCCAGATGCTGGCAAAAGCGCAAAAACCGATG
CTGTACGTTGGCGGTGGCGTGGGTATGGCGCAGGCAGTTCCGGCTTTGCGTGAATTTCTC
GCTGCCACAAAAATGCCTGCCACCTGTACGCTGAAAGGGCTGGGCGCAGTAGAAGCAGAT
TATCCGTACTATCTGGGCATGCTGGGGATGCACGGCACCAAAGCGGCAAACTTCGCGGTG
CAGGAGTGTGACCTGCTGATCGCCGTGGGCGCACGTTTTGATGACCGGGTGACCGGCAAA
CTGAACACCTTCGCGCCACACGCCAGTGTTATCCATATGGATATCGACCCGGCAGAAATG
AACAAGCTGCGTCAGGCACATGTGGCATTACAAGGTGATTTAAATGCTCTGTTACCAGCA
TTACAGCAGCCGTTAAATCAATATGACTGGCAGCAACACTGCGCGCAGCTGCGTGATGAA
CATTCCTGGCGTTACGACCATCCCGGTGACGCTATCTACGCGCCGTTGTTGTTAAAACAA
CTGTCGGATCGTAAACCTGCGGATTGCGTCGTGACCACAGATGTGGGGCAGCACCAGATG
TGGGCTGCGCAGCACATCGCCCACACTCGCCCGGAAAATTTCATCACCTCCAGCGGTTTA
GGTACCATGGGTTTTGGTTTACCGGCGGCGGTTGGCGCACAAGTCGCGCGACCGAACGAT
ACCGTTGTCTGTATCTCCGGTGACGGCTCTTTCATGATGAATGTGCAAGAGCTGGGCACC
GTAAAACGCAAGCAGTTACCGTTGAAAATCGTCTTACTCGATAACCAACGGTTAGGGATG
GTTCGACAATGGCAGCAACTGTTTTTTCAGGAACGATACAGCGAAACCACCCTTACTGAT
AACCCCGATTTCCTCATGTTAGCCAGCGCCTTCGGCATCCATGGCCAACACATCACCCGG
AAAGACCAGGTTGAAGCGGCACTCGACACCATGCTGAACAGTGATGGGCCATACCTGCTT
CATGTCTCAATCGACGAACTTGAGAACGTCTGGCCGCTGGTGCCGCCTGGCGCCAGTAAT
TCAGAAATGTTGGAGAAATTATCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:548
Protein Molecular Weight:59284
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetolactate synthase isozyme 2 large subunit
MNGAQWVVHALRAQGVNTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARA
TGKTGVCIATSGPGATNLITGLADALLDSIPVVAITGQVSAPFIGTDAFQEVDVLGLSLA
CTKHSFLVQSLEELPRIMAEAFDVACSGRPGPVLVDIPKDIQLASGDLEPWFTTVENEVT
FPHAEVEQARQMLAKAQKPMLYVGGGVGMAQAVPALREFLAATKMPATCTLKGLGAVEAD
YPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPHASVIHMDIDPAEM
NKLRQAHVALQGDLNALLPALQQPLNQYDWQQHCAQLRDEHSWRYDHPGDAIYAPLLLKQ
LSDRKPADCVVTTDVGQHQMWAAQHIAHTRPENFITSSGLGTMGFGLPAAVGAQVARPND
TVVCISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTD
NPDFLMLASAFGIHGQHITRKDQVEAALDTMLNSDGPYLLHVSIDELENVWPLVPPGASN
SEMLEKLS
References
External Links:
ResourceLink
Uniprot ID:P00892
Uniprot Name:ILVG_ECOLI
GenBank Gene ID:M10313
Genebank Protein ID:146458
CCDB:ILVG_ECOLI
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
  • Coppola, G., Huang, F., Riley, J., Cox, J. L., Hantzopoulos, P., Zhou, L. B., Calhoun, D. H. (1991). "Sequence and transcriptional activity of the Escherichia coli K-12 chromosome region between rrnC and ilvGMEDA." Gene 97:21-27. Pubmed: 1995430
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • Hill, C. M., Pang, S. S., Duggleby, R. G. (1997). "Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits." Biochem J 327 ( Pt 3):891-898. Pubmed: 9581571
  • Kuramitsu, S., Ogawa, T., Ogawa, H., Kagamiyama, H. (1985). "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence." J Biochem 97:993-999. Pubmed: 3897211
  • Lawther, R. P., Calhoun, D. H., Adams, C. W., Hauser, C. A., Gray, J., Hatfield, G. W. (1981). "Molecular basis of valine resistance in Escherichia coli K-12." Proc Natl Acad Sci U S A 78:922-925. Pubmed: 7015336
  • Lawther, R. P., Hatfield, G. W. (1980). "Multivalent translational control of transcription termination at attenuator of ilvGEDA operon of Escherichia coli K-12." Proc Natl Acad Sci U S A 77:1862-1866. Pubmed: 6154938
  • Lawther, R. P., Wek, R. C., Lopes, J. M., Pereira, R., Taillon, B. E., Hatfield, G. W. (1987). "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12." Nucleic Acids Res 15:2137-2155. Pubmed: 3550695