Tag | Content |
---|
CPLM ID | CPLM-002319 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ketol-acid reductoisomerase, mitochondrial |
Protein Synonyms/Alias | Acetohydroxy-acid reductoisomerase; Alpha-keto-beta-hydroxylacyl reductoisomerase |
Gene Name | ILV5 |
Gene Synonyms/Alias | YLR355C; L9638.7 |
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 |
---|
70 | RADWPREKLLDYFKN | acetylation | [1] | 115 | RKDGASWKAAIEDGW | acetylation | [1] | 126 | EDGWVPGKNLFTVED | acetylation | [1] | 136 | FTVEDAIKRGSYVMN | acetylation | [1] | 165 | KPLLTKGKTLYFSHG | acetylation | [1] | 178 | HGFSPVFKDLTHVEP | acetylation | [1] | 187 | LTHVEPPKDLDVILV | acetylation | [1] | 208 | RTVRSLFKEGRGINS | acetylation | [1] | 226 | VWNDVTGKAHEKAQA | acetylation | [1] | 336 | PIFKNALKPVFQDLY | acetylation | [1] | 347 | QDLYESTKNGTETKR | acetylation | [1] | 367 | SQPDYREKLEKELDT | acetylation | [1] | 370 | DYREKLEKELDTIRN | acetylation | [1] | 382 | IRNMEIWKVGKEVRK | acetylation | [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 84 93 NADP (Potential). NP_BIND 108 113 NADP (By similarity). NP_BIND 146 150 NADP (By similarity). REGION 363 395 Hydrophilic. ACT_SITE 171 171 Potential. METAL 255 255 Magnesium 1 (By similarity). METAL 255 255 Magnesium 2 (By similarity). METAL 259 259 Magnesium 1 (By similarity). MOD_RES 355 355 Phosphoserine. |
Keyword | Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Direct protein sequencing; Magnesium; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 395 AA |
Protein Sequence | MLRTQAARLI CNSRVITAKR TFALATRAAA YSRPAARFVK PMITTRGLKQ INFGGTVETV 60 YERADWPREK LLDYFKNDTF ALIGYGSQGY GQGLNLRDNG LNVIIGVRKD GASWKAAIED 120 GWVPGKNLFT VEDAIKRGSY VMNLLSDAAQ SETWPAIKPL LTKGKTLYFS HGFSPVFKDL 180 THVEPPKDLD VILVAPKGSG RTVRSLFKEG RGINSSYAVW NDVTGKAHEK AQALAVAIGS 240 GYVYQTTFER EVNSDLYGER GCLMGGIHGM FLAQYDVLRE NGHSPSEAFN ETVEEATQSL 300 YPLIGKYGMD YMYDACSTTA RRGALDWYPI FKNALKPVFQ DLYESTKNGT ETKRSLEFNS 360 QPDYREKLEK ELDTIRNMEI WKVGKEVRKL RPENQ 395 |
Gene Ontology | GO:0042645; C:mitochondrial nucleoid; IDA:SGD. GO:0050662; F:coenzyme binding; IEA:InterPro. GO:0003690; F:double-stranded DNA binding; IDA:SGD. GO:0004455; F:ketol-acid reductoisomerase activity; IMP:SGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0009082; P:branched-chain amino acid biosynthetic process; IMP:SGD. GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. GO:0000002; P:mitochondrial genome maintenance; IMP:SGD. GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |