CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002495
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acetolactate synthase catalytic subunit, mitochondrial 
Protein Synonyms/Alias
 Acetohydroxy-acid synthase catalytic subunit; AHAS; ALS 
Gene Name
 ILV2 
Gene Synonyms/Alias
 SMR1; YMR108W; YM9718.07 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
74EQPAEPSKLAKKLRAacetylation[1]
215GISRSCTKWNVMVKSacetylation[1]
251PVLVDLPKDVTAAILacetylation[1]
387RVTGNISKFAPEARRacetylation[1]
453EWFAQINKWKKEYPYacetylation[1]
615LAEAMGLKGLRVKKQacetylation[1]
628KQEELDAKLKEFVSTacetylation[1]
630EELDAKLKEFVSTKGacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
  
Sequence Annotation
 NP_BIND 355 376 FAD.
 NP_BIND 407 426 FAD.
 REGION 499 579 Thiamine pyrophosphate binding.
 METAL 550 550 Magnesium.
 METAL 577 577 Magnesium.
 METAL 579 579 Magnesium; via carbonyl oxygen.
 BINDING 139 139 Thiamine pyrophosphate.
 BINDING 241 241 FAD.  
Keyword
 3D-structure; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Magnesium; Metal-binding; Mitochondrion; Reference proteome; Thiamine pyrophosphate; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 687 AA 
Protein Sequence
MIRQSTLKNF AIKRCFQHIA YRNTPAMRSV ALAQRFYSSS SRYYSASPLP ASKRPEPAPS 60
FNVDPLEQPA EPSKLAKKLR AEPDMDTSFV GLTGGQIFNE MMSRQNVDTV FGYPGGAILP 120
VYDAIHNSDK FNFVLPKHEQ GAGHMAEGYA RASGKPGVVL VTSGPGATNV VTPMADAFAD 180
GIPMVVFTGQ VPTSAIGTDA FQEADVVGIS RSCTKWNVMV KSVEELPLRI NEAFEIATSG 240
RPGPVLVDLP KDVTAAILRN PIPTKTTLPS NALNQLTSRA QDEFVMQSIN KAADLINLAK 300
KPVLYVGAGI LNHADGPRLL KELSDRAQIP VTTTLQGLGS FDQEDPKSLD MLGMHGCATA 360
NLAVQNADLI IAVGARFDDR VTGNISKFAP EARRAAAEGR GGIIHFEVSP KNINKVVQTQ 420
IAVEGDATTN LGKMMSKIFP VKERSEWFAQ INKWKKEYPY AYMEETPGSK IKPQTVIKKL 480
SKVANDTGRH VIVTTGVGQH QMWAAQHWTW RNPHTFITSG GLGTMGYGLP AAIGAQVAKP 540
ESLVIDIDGD ASFNMTLTEL SSAVQAGTPV KILILNNEEQ GMVTQWQSLF YEHRYSHTHQ 600
LNPDFIKLAE AMGLKGLRVK KQEELDAKLK EFVSTKGPVL LEVEVDKKVP VLPMVAGGSG 660
LDEFINFDPE VERQQTELRH KRTGGKH 687 
Gene Ontology
 GO:0005948; C:acetolactate synthase complex; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0003984; F:acetolactate synthase activity; IDA:SGD.
 GO:0050660; F:flavin adenine dinucleotide binding; IDA:SGD.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
 GO:0009082; P:branched-chain amino acid biosynthetic process; IMP:SGD.
 GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR012846; Acetolactate_synth_lsu.
 IPR012000; Thiamin_PyroP_enz_cen_dom.
 IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
 IPR000399; TPP-bd_CS.
 IPR011766; TPP_enzyme-bd_C. 
Pfam
 PF02775; TPP_enzyme_C
 PF00205; TPP_enzyme_M
 PF02776; TPP_enzyme_N 
SMART
  
PROSITE
 PS00187; TPP_ENZYMES 
PRINTS