Tag | Content |
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CPLM ID | CPLM-003179 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | P-protein |
Protein Synonyms/Alias | Chorismate mutase; CM; Prephenate dehydratase; PDT |
Gene Name | pheA |
Gene Synonyms/Alias | b2599; JW2580 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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20 | KISALDEKLLALLAE | acetylation | [1] | 39 | AVEVGKAKLLSHRPV | acetylation | [1] | 64 | ERLITLGKAHHLDAH | acetylation | [1] | 112 | RIAFLGPKGSYSHLA | acetylation | [1] | 227 | LNRYPHWKIEYTEST | acetylation | [1] | 240 | STSAAMEKVAQAKSP | acetylation | [1] | 286 | RFVVLARKAINVSDQ | acetylation | [1, 2] | 360 | AEMQKALKELGEITR | 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] [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. |
Sequence Annotation | DOMAIN 1 92 Chorismate mutase. DOMAIN 105 285 Prephenate dehydratase. DOMAIN 299 376 ACT. REGION 286 386 Regulatory (Phe-binding). BINDING 11 11 Substrate. BINDING 28 28 Substrate. BINDING 39 39 Substrate. BINDING 48 48 Substrate. BINDING 52 52 Substrate. BINDING 84 84 Substrate. BINDING 88 88 Substrate. |
Keyword | 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Cytoplasm; Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 386 AA |
Protein Sequence | MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID RERDLLERLI 60 TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN PHSARIAFLG PKGSYSHLAA 120 RQYAARHFEQ FIESGCAKFA DIFNQVETGQ ADYAVVPIEN TSSGAINDVY DLLQHTSLSI 180 VGEMTLTIDH CLLVSGTTDL STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK 240 VAQAKSPHVA ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL 300 LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL ESAEMQKALK 360 ELGEITRSMK VLGCYPSENV VPVDPT 386 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004106; F:chorismate mutase activity; IDA:EcoCyc. GO:0004664; F:prephenate dehydratase activity; IDA:EcoCyc. GO:0046417; P:chorismate metabolic process; IEA:InterPro. GO:0009094; P:L-phenylalanine biosynthetic process; IMP:EcoCyc. GO:0006571; P:tyrosine biosynthetic process; IMP:EcoCyc. |
Interpro | |
Pfam | |
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PROSITE | |
PRINTS | |