Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 2-isopropylmalate synthase, putative (LeuA-1) |
Protein Synonyms/Alias | |
Gene Name | leuA-1 |
Gene Synonyms/Alias | SSO0127 |
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 | 39 | SVEVLDTTLRDGSQG | T | HTP | [1] | 38 | KSVEVLDTTLRDGSQ | T | HTP | [1] | 32 | LCSVSKKSVEVLDTT | S | HTP | [1] | 429 | KNYINLEYWKVINEN | Y | HTP | [1] | 424 | ELNIYKNYINLEYWK | 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 | |
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| Completeproteome; Lyase; Referenceproteome; Transferase. |
Protein Sequence | MALKMKYDFL LLSLKLLNLP IIFHLCSVSK KSVEVLDTTL RDGSQGANIS FTLNDKIKIA 60 LLLDELGVDY IEGGWPGSNP KDEEFFREIK KYRLSKAKIA AFGSTKRKDV SVKEDISLNS 120 IVKADVDVAV IFGKSWSLHA TEVLKVTKQD NLDIVYDSIN YLKSHGLKVI FDAEHFYQGF 180 KEDPEYALEV VKTAESAGAD VIALADTNGG TPPFEVYEIT KKVREVLQVK LGIHAHNDIG 240 CAVANSLMAI KAGARHVQGT INGIGERTGN ADLIQIIPTL ILKMGLNALN GQESLRKLRE 300 VSRIVYEILG LPPNPYQPYV GDNAFAHKAG VHVDAVMKVP RAYEHVDPSL VGNDRKFVIS 360 ELSGTANLVS YLQGLGIAVD KKDERLKKAL NKIKELEARG YSFDVGPASA ILITLKELNI 420 YKNYINLEYW KVINENNGLS IGIVKVNSQL EVAEGVGPVN AIDRALRMAL QRVYPEIGEV 480 KLIDYRVILP SEIKNTESVV RVTIEFTDNK MNWRTEGVSK SVVEASVMAL VDGLDYYLQL 540 KKTLKTAVDN YIV 553 |
| GO:0003852 F:2-isopropylmalate synthase activity IEA:InterPro GO:0016829 F:lyase activity IEA:UniProtKB-KW GO:0009098 P:leucine biosynthetic process IEA:InterPro |
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