Tag | Content |
---|
CPLM ID | CPLM-015048 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Shikimate kinase |
Protein Synonyms/Alias | SK |
Gene Name | aroK |
Gene Synonyms/Alias | RPA0504 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
---|
100 | RLLDGGTKVLATGGG | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate (By similarity). |
Sequence Annotation | NP_BIND 38 43 ATP (By similarity). METAL 42 42 Magnesium (By similarity). BINDING 60 60 Substrate (By similarity). BINDING 84 84 Substrate (By similarity). BINDING 106 106 Substrate; via amide nitrogen (By BINDING 144 144 ATP (By similarity). BINDING 163 163 Substrate (By similarity). |
Keyword | Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 203 AA |
Protein Sequence | MPRMSETVPT AAAGRSPQEA EIVAALGDRP VVLIGMMGAG KSTVGRRLAL RLGLPFLDAD 60 TEIESAAAMT IPEIFETHGE PHFRDGEARV ISRLLDGGTK VLATGGGAFM REETRDRIRE 120 KAISMWLEAE ADVILRRVKR RADRPLLKTP DPAGTIARLI AERYPLYREA DITIASRDVP 180 HEKIVDECVA ALHDYLCAAP PQP 203 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0004765; F:shikimate kinase activity; IEA:HAMAP. GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:HAMAP. GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |