Tag | Content |
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CPLM ID | CPLM-002430 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | T-protein |
Protein Synonyms/Alias | Chorismate mutase; CM; Prephenate dehydrogenase; PDH |
Gene Name | tyrA |
Gene Synonyms/Alias | b2600; JW2581 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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17 | DQIDEVDKALLNLLA | acetylation | [1] | 25 | ALLNLLAKRLELVAE | acetylation | [1] | 37 | VAEVGEVKSRFGLPI | acetylation | [1] | 89 | SYSSENDKGFKTLCP | acetylation | [1] | 92 | SENDKGFKTLCPSLR | acetylation | [1] | 116 | QMGRLFEKMLTLSGY | acetylation | [1] | 167 | GKLPPLPKDCILVDL | acetylation | [1] | 318 | ERNLALIKRYYKRFG | acetylation | [1] | 345 | AFIDSFRKVEHWFGD | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | |
Sequence Annotation | DOMAIN 1 90 Chorismate mutase. DOMAIN 99 361 Prephenate/arogenate dehydrogenase. |
Keyword | Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Cytoplasm; Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome; Tyrosine biosynthesis. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 373 AA |
Protein Sequence | MVAELTALRD QIDEVDKALL NLLAKRLELV AEVGEVKSRF GLPIYVPERE ASMLASRRAE 60 AEALGVPPDL IEDVLRRVMR ESYSSENDKG FKTLCPSLRP VVIVGGGGQM GRLFEKMLTL 120 SGYQVRILEQ HDWDRAADIV ADAGMVIVSV PIHVTEQVIG KLPPLPKDCI LVDLASVKNG 180 PLQAMLVAHD GPVLGLHPMF GPDSGSLAKQ VVVWCDGRKP EAYQWFLEQI QVWGARLHRI 240 SAVEHDQNMA FIQALRHFAT FAYGLHLAEE NVQLEQLLAL SSPIYRLELA MVGRLFAQDP 300 QLYADIIMSS ERNLALIKRY YKRFGEAIEL LEQGDKQAFI DSFRKVEHWF GDYAQRFQSE 360 SRVLLRQAND NRQ 373 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004106; F:chorismate mutase activity; IDA:EcoCyc. GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro. GO:0008977; F:prephenate dehydrogenase activity; IDA:EcoCyc. GO:0046417; P:chorismate metabolic process; IEA:InterPro. GO:0009094; P:L-phenylalanine biosynthetic process; IDA:EcoCyc. GO:0006571; P:tyrosine biosynthetic process; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |