CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
20KISALDEKLLALLAEacetylation[1]
39AVEVGKAKLLSHRPVacetylation[1]
64ERLITLGKAHHLDAHacetylation[1]
112RIAFLGPKGSYSHLAacetylation[1]
227LNRYPHWKIEYTESTacetylation[1]
240STSAAMEKVAQAKSPacetylation[1]
286RFVVLARKAINVSDQacetylation[1, 2]
360AEMQKALKELGEITRacetylation[1]
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
 IPR008242; Chor_mutase/pphenate_deHydtase.
 IPR002701; Chorismate_mutase.
 IPR020822; Chorismate_mutase_type_II.
 IPR010952; CM_P_1.
 IPR001086; Preph_deHydtase.
 IPR018528; Preph_deHydtase_CS. 
Pfam
 PF01817; CM_2
 PF00800; PDT 
SMART
 SM00830; CM_2 
PROSITE
 PS51671; ACT
 PS51168; CHORISMATE_MUT_2
 PS00857; PREPHENATE_DEHYDR_1
 PS00858; PREPHENATE_DEHYDR_2
 PS51171; PREPHENATE_DEHYDR_3 
PRINTS