CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003397
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate kinase I 
Protein Synonyms/Alias
 PK-1 
Gene Name
 pykF 
Gene Synonyms/Alias
 b1676; JW1666 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
13IVCTIGPKTESEEMLacetylation[1, 2]
22ESEEMLAKMLDAGMNacetylation[2]
56NLRNVMSKTGKTAAIacetylation[1]
59NVMSKTGKTAAILLDacetylation[2]
68AAILLDTKGPEIRTMacetylation[1, 2]
76GPEIRTMKLEGGNDVacetylation[1, 2, 3]
145EGNKVICKVLNNGDLacetylation[1, 2]
156NGDLGENKGVNLPGVacetylation[2]
173ALPALAEKDKQDLIFacetylation[2]
208IEIREHLKAHGGENIacetylation[1]
266AQKMMIEKCIRARKVacetylation[2]
272EKCIRARKVVITATQacetylation[1]
286QMLDSMIKNPRPTRAacetylation[1, 2]
317MLSGESAKGKYPLEAacetylation[1, 2]
319SGESAKGKYPLEAVSacetylation[1, 2, 3]
368GAVETAEKLDAPLIVacetylation[1, 2]
382VVATQGGKSARAVRKacetylation[1, 2]
389KSARAVRKYFPDATIacetylation[1, 2]
404LALTTNEKTAHQLVLacetylation[2]
413AHQLVLSKGVVPQLVacetylation[2]
421GVVPQLVKEITSTDDacetylation[1, 2]
434DDFYRLGKELALQSGacetylation[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
  
Sequence Annotation
 METAL 34 34 Potassium (By similarity).
 METAL 36 36 Potassium (By similarity).
 METAL 66 66 Potassium (By similarity).
 METAL 67 67 Potassium; via carbonyl oxygen (By
 METAL 222 222 Magnesium (By similarity).
 METAL 246 246 Magnesium (By similarity).
 BINDING 32 32 Substrate (By similarity).
 BINDING 245 245 Substrate; via amide nitrogen (By
 BINDING 246 246 Substrate; via amide nitrogen (By
 BINDING 278 278 Substrate (By similarity).
 MOD_RES 76 76 N6-acetyllysine.
 MOD_RES 319 319 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Complete proteome; Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 470 AA 
Protein Sequence
MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL RNVMSKTGKT 60
AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI GNSEMVAVTY EGFTTDLSVG 120
NTVLVDDGLI GMEVTAIEGN KVICKVLNNG DLGENKGVNL PGVSIALPAL AEKDKQDLIF 180
GCEQGVDFVA ASFIRKRSDV IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI 240
MVARGDLGVE IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN 300
AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR KLRITEAVCR 360
GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT TNEKTAHQLV LSKGVVPQLV 420
KEITSTDDFY RLGKELALQS GLAHKGDVVV MVSGALVPSG TTNTASVHVL 470 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030955; F:potassium ion binding; IEA:InterPro.
 GO:0004743; F:pyruvate kinase activity; IEA:EC.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. 
Interpro
 IPR001697; Pyr_Knase.
 IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
 IPR011037; Pyrv_Knase-like_insert_dom.
 IPR015794; Pyrv_Knase_a/b.
 IPR018209; Pyrv_Knase_AS.
 IPR015793; Pyrv_Knase_brl.
 IPR015795; Pyrv_Knase_C.
 IPR015806; Pyrv_Knase_insert_dom. 
Pfam
 PF00224; PK
 PF02887; PK_C 
SMART
  
PROSITE
 PS00110; PYRUVATE_KINASE 
PRINTS
 PR01050; PYRUVTKNASE.