CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005070
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoenolpyruvate carboxykinase [ATP] 
Protein Synonyms/Alias
 PEP carboxykinase; PEPCK; Phosphoenolpyruvate carboxylase 
Gene Name
 pckA 
Gene Synonyms/Alias
 pck; b3403; JW3366 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
87DTFWWADKGKGKNDNacetylation[1, 2, 3]
89FWWADKGKGKNDNKPacetylation[3]
95GKGKNDNKPLSPETWacetylation[3]
106PETWQHLKGLVTRQLacetylation[3]
164DEELAGFKPDFIVMNacetylation[3]
181KCTNPQWKEQGLNSEacetylation[3]
213WYGGEMKKGMFSMMNacetylation[2, 3]
240CSANVGEKGDVAVFFacetylation[2]
288FEGGCYAKTIKLSKEacetylation[3]
294AKTIKLSKEAEPEIYacetylation[2, 3]
328IDFDDGSKTENTRVSacetylation[3]
346YHIDNIVKPVSKAGHacetylation[2, 3]
390FLSGFTAKLAGTERGacetylation[2, 3]
448TGWNGTGKRISIKDTacetylation[3]
453TGKRISIKDTRAIIDacetylation[2]
509SPEQWQEKAETLAKLacetylation[3]
515EKAETLAKLFIDNFDacetylation[2, 3]
523LFIDNFDKYTDTPAGacetylation[1, 2, 3]
Reference
 [1] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [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]
 [3] 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
 NP_BIND 248 255 ATP.
 MOD_RES 87 87 N6-acetyllysine.
 MOD_RES 523 523 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Calcium; Complete proteome; Cytoplasm; Decarboxylase; Direct protein sequencing; Gluconeogenesis; Lyase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 540 AA 
Protein Sequence
MRVNNGLTPQ ELEAYGISDV HDIVYNPSYD LLYQEELDPS LTGYERGVLT NLGAVAVDTG 60
IFTGRSPKDK YIVRDDTTRD TFWWADKGKG KNDNKPLSPE TWQHLKGLVT RQLSGKRLFV 120
VDAFCGANPD TRLSVRFITE VAWQAHFVKN MFIRPSDEEL AGFKPDFIVM NGAKCTNPQW 180
KEQGLNSENF VAFNLTERMQ LIGGTWYGGE MKKGMFSMMN YLLPLKGIAS MHCSANVGEK 240
GDVAVFFGLS GTGKTTLSTD PKRRLIGDDE HGWDDDGVFN FEGGCYAKTI KLSKEAEPEI 300
YNAIRRDALL ENVTVREDGT IDFDDGSKTE NTRVSYPIYH IDNIVKPVSK AGHATKVIFL 360
TADAFGVLPP VSRLTADQTQ YHFLSGFTAK LAGTERGITE PTPTFSACFG AAFLSLHPTQ 420
YAEVLVKRMQ AAGAQAYLVN TGWNGTGKRI SIKDTRAIID AILNGSLDNA ETFTLPMFNL 480
AIPTELPGVD TKILDPRNTY ASPEQWQEKA ETLAKLFIDN FDKYTDTPAG AALVAAGPKL 540 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0005509; F:calcium ion binding; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IDA:EcoCyc.
 GO:0006094; P:gluconeogenesis; IMP:EcoCyc. 
Interpro
 IPR001272; PEP_carboxykinase_ATP.
 IPR013035; PEP_carboxykinase_C.
 IPR008210; PEP_carboxykinase_N.
 IPR015994; PEPCK_ATP_CS. 
Pfam
 PF01293; PEPCK_ATP 
SMART
  
PROSITE
 PS00532; PEPCK_ATP 
PRINTS