Acetolactate synthase catalytic subunit, mitochondrial (P07342)

Identification
NameAcetolactate synthase catalytic subunit, mitochondrial
Synonyms
  • Acetohydroxy-acid synthase catalytic subunit
  • AHAS
  • ALS
Gene NameILV2
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific Function2 pyruvate = 2-acetolactate + CO(2)
Cellular LocationMitochondrion
SMPDB Pathways
Pantothenate and CoA biosynthesisPW002463 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Butanoate metabolismec00650 Map00650
Pantothenate and CoA biosynthesisec00770 Map00770
Valine, leucine and isoleucine biosynthesisec00290 Map00290
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB000712-Ketobutyric acidShow
YMDB00175Pyruvic acidShow
YMDB00177(S)-2-AcetolactateShow
YMDB003942-Acetolactate Show
YMDB00428(S)-2-acetyl-2-hydroxybutanoateShow
YMDB00862hydronShow
YMDB00912Carbon dioxideShow
GO Classification
Component
Not Available
Function
adenyl nucleotide binding
FAD or FADH2 binding
ion binding
cation binding
metal ion binding
vitamin binding
catalytic activity
magnesium ion binding
transferase activity
thiamin pyrophosphate binding
transferase activity, transferring aldehyde or ketonic groups
acetolactate synthase activity
binding
nucleoside binding
purine nucleoside binding
Process
metabolic process
cellular amino acid biosynthetic process
branched chain family amino acid biosynthetic process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYMR108W
Gene Sequence>2064 bp ATGATCAGACAATCTACGCTAAAAAACTTCGCTATTAAGCGTTGCTTTCAACATATAGCA TACCGCAACACACCTGCCATGAGATCAGTAGCTCTCGCGCAGCGCTTTTATAGTTCGTCT TCCCGTTATTACAGTGCGTCTCCATTACCAGCCTCTAAAAGGCCAGAGCCTGCTCCAAGT TTCAATGTTGATCCATTAGAACAGCCCGCTGAACCTTCAAAATTGGCTAAGAAACTACGC GCTGAGCCTGACATGGATACCTCTTTCGTCGGTTTAACTGGTGGTCAAATATTTAACGAA ATGATGTCCAGACAAAACGTTGATACTGTATTTGGTTATCCAGGTGGTGCTATCCTACCT GTTTACGATGCCATTCATAACAGTGATAAATTCAACTTCGTTCTTCCAAAACACGAACAA GGTGCCGGTCACATGGCAGAAGGCTACGCCAGAGCTTCTGGTAAACCAGGTGTTGTCTTG GTTACTTCTGGGCCAGGTGCCACCAATGTCGTTACTCCAATGGCAGATGCCTTTGCAGAC GGGATTCCAATGGTTGTCTTTACAGGGCAAGTCCCAACTAGTGCTATCGGTACTGATGCT TTCCAAGAGGCTGACGTCGTTGGTATTTCTAGATCTTGTACGAAATGGAATGTCATGGTC AAGTCCGTGGAAGAATTGCCATTGCGTATTAACGAGGCTTTTGAAATTGCCACGAGCGGT AGACCGGGACCAGTCTTGGTCGATTTACCAAAGGATGTTACAGCAGCTATCTTAAGAAAT CCAATTCCAACAAAAACAACTCTTCCATCAAACGCACTAAACCAATTAACCAGTCGCGCA CAAGATGAATTTGTCATGCAAAGTATCAATAAAGCAGCAGATTTGATCAACTTGGCAAAG AAACCTGTCTTATACGTCGGTGCTGGTATTTTAAACCATGCAGATGGTCCAAGATTACTA AAAGAATTAAGTGACCGTGCTCAAATACCTGTCACCACTACTTTACAAGGTTTAGGTTCA TTCGACCAAGAAGATCCAAAATCATTGGATATGCTTGGTATGCACGGTTGTGCTACTGCC AACCTGGCAGTGCAAAATGCCGACTTGATAATTGCAGTTGGTGCTAGATTCGACGACCGT GTCACTGGTAATATTTCTAAATTCGCTCCAGAAGCTCGTCGTGCAGCTGCCGAGGGTAGA GGTGGTATTATTCATTTCGAGGTTAGTCCAAAAAACATAAACAAGGTTGTTCAAACTCAA ATAGCAGTGGAAGGTGATGCTACGACCAATCTGGGCAAAATGATGTCAAAGATTTTCCCA GTTAAGGAGAGGTCTGAATGGTTTGCTCAAATAAATAAATGGAAGAAGGAATACCCATAC GCTTATATGGAGGAGACTCCAGGATCTAAAATTAAACCACAGACGGTTATAAAGAAACTA TCCAAGGTTGCCAACGACACAGGAAGACATGTCATTGTTACAACGGGTGTGGGGCAACAT CAAATGTGGGCTGCTCAACACTGGACATGGAGAAATCCACATACTTTCATCACATCAGGT GGTTTAGGTACGATGGGTTACGGTCTCCCTGCCGCCATCGGTGCTCAAGTTGCAAAGCCA GAATCTTTGGTTATTGACATTGATGGTGACGCATCCTTTAACATGACTCTAACGGAATTG AGTTCTGCCGTTCAAGCTGGTACTCCAGTGAAGATTTTGATTTTGAACAATGAAGAGCAA GGTATGGTTACTCAATGGCAATCCCTGTTCTACGAACATCGTTATTCCCACACACATCAA TTGAACCCTGATTTCATAAAACTAGCGGAGGCTATGGGTTTAAAAGGTTTAAGAGTCAAG AAGCAAGAGGAATTGGACGCTAAGTTGAAAGAATTCGTTTCTACCAAGGGCCCAGTTTTG CTTGAAGTGGAAGTTGATAAAAAAGTTCCTGTTTTGCCAATGGTGGCAGGTGGTAGCGGT CTAGACGAGTTCATAAATTTTGACCCAGAAGTTGAAAGACAACAGACTGAATTACGTCAT AAGCGTACAGGCGGTAAGCACTGA
Protein Properties
Pfam Domain Function
Protein Residues687
Protein Molecular Weight74936.29688
Protein Theoretical pI8.87
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Acetolactate synthase catalytic subunit, mitochondrial MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPS FNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILP VYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFAD GIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSG RPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAK KPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATA NLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQ IAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKL SKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKP ESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQ LNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSG LDEFINFDPEVERQQTELRHKRTGGKH
References
External Links
ResourceLink
Saccharomyces Genome Database ILV2
Uniprot IDP07342
Uniprot NameILVB_YEAST
GenBank Gene IDAY692995
Genebank Protein ID51013441
PDB ID
1T9D
General Reference
  • Falco, S. C., Dumas, K. S., Livak, K. J. (1985). "Nucleotide sequence of the yeast ILV2 gene which encodes acetolactate synthase." Nucleic Acids Res 13:4011-4027.2989783
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Pang, S. S., Duggleby, R. G. (1999). "Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase." Biochemistry 38:5222-5231.10213630
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Pang, S. S., Duggleby, R. G., Guddat, L. W. (2002). "Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors." J Mol Biol 317:249-262.11902841
  • Pang, S. S., Guddat, L. W., Duggleby, R. G. (2003). "Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase." J Biol Chem 278:7639-7644.12496246