Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable 2-isopropylmalate synthase |
Protein Synonyms/Alias | |
Gene Name | leuA |
Gene Synonyms/Alias | SSO2407 |
Created Date | 3-June-2014 |
Organism | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) |
NCBI Taxa ID | 273057 |
Phosphorylation | Position | Peptide | Code | Type | References | 91 | EEVLNKIYESVKYAK | Y | HTP | [1] | 93 | VLNKIYESVKYAKDH | S | HTP | [1] | 82 | MKYKLKMTKEEVLNK | T | HTP | [1] | 96 | KIYESVKYAKDHGMI | Y | HTP | [1] | 77 | TSELHMKYKLKMTKE | Y | HTP | [1] | |
Reference | [1]Change of carbon source causes dramatic effects in the phospho-proteome of the archaeon Sulfolobus solfataricus. Esser D,Pham TK,Reimann J,Albers SV,Siebers B,Wright PC J. Proteome Res. 2012, Oct, 5;11(10):4823-33. [ PMID:22639831] |
Functional Description From UniProt | FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (By similarity) |
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| Amino-acidbiosynthesis; Branched-chainaminoacidbiosynthesis; Completeproteome; Leucinebiosynthesis; Referenceproteome; Transferase |
Protein Sequence | MIARKLADLG VDVIEAGFPA SSEGEFIATR KIFEEIGDQV EVIGLSRSNK NDIDKTISTG 60 ISSIHLFIAT SELHMKYKLK MTKEEVLNKI YESVKYAKDH GMIVEFSPED ATRTEEDFLF 120 TAIRTAIEAG ADRINIPDTV GTMHPFKYYD MIKKIVNFVG ERIIVSVHCH NDFGLATANS 180 LAGVYAGARQ AHVTVNGIGE RAGNASLEEV VMGIKKLLNY ETNVKTWKLY EVSRFVAEMT 240 GVPVPYFKAI VGDNAFGHES GIHVHGVIEN PFTYEPISPE EVGNFRRLAL GKHSGIHGLR 300 KLLEEQGIYL SDDKLKIVLA EIKKLAESGN KVTVEDAKNI ALKLMNS 347 |
| GO:0003852 F:2-isopropylmalate synthase activity IEA:UniProtKB-EC GO:0009098 P:leucine biosynthetic process IEA:UniProtKB-UniPathway |
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