| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 3-isopropylmalate dehydrogenase |
Protein Synonyms/Alias | IMDH |
Gene Name | leuB |
Gene Synonyms/Alias | leuC; OrderedLocusNames=BSU28270 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | | 4 | ****MKKRIALLPGD | R | HTP | [1] | |
Reference | [1]Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Elsholz AK,Turgay K,Michalik S,Hessling B,Gronau K,Oertel D,Mäder U,Bernhardt J,Becher D,Hecker M,Gerth U Proc. Natl. Acad. Sci. U.S.A. 2012, May, 8;109(19):7451-6. [ PMID:22517742] |
Functional Description From UniProt | FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate |
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| Amino-acidbiosynthesis; Branched-chainaminoacidbiosynthesis; Completeproteome; Cytoplasm; Leucinebiosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase; Referenceproteome |
Protein Sequence | MKKRIALLPG DGIGPEVLES ATDVLKSVAE RFNHEFEFEY GLIGGAAIDE HHNPLPEETV 60
AACKNADAIL LGAVGGPKWD QNPSELRPEK GLLSIRKQLD LFANLRPVKV FESLSDASPL 120
KKEYIDNVDF VIVRELTGGL YFGQPSKRYV NTEGEQEAVD TLFYKRTEIE RVIREGFKMA 180
AARKGKVTSV DKANVLESSR LWREVAEDVA QEFPDVKLEH MLVDNAAMQL IYAPNQFDVV 240
VTENMFGDIL SDEASMLTGS LGMLPSASLS SSGLHLFEPV HGSAPDIAGK GMANPFAAIL 300
SAAMLLRTSF GLEEEAKAVE DAVNKVLASG KRTRDLARSE EFSSTQAITE EVKAAIMSEN 360
TISNV 365 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0003862 F:3-isopropylmalate dehydrogenase activity IEA:UniProtKB-HAMAP GO:0000287 F:magnesium ion binding IEA:InterPro GO:0051287 F:NAD binding IEA:InterPro GO:0009098 P:leucine biosynthetic process IEA:UniProtKB-HAMAP |
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