CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004988
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate kinase II 
Protein Synonyms/Alias
 PK-2 
Gene Name
 pykA 
Gene Synonyms/Alias
 b1854; JW1843 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
26DRDNNLEKVIAAGANacetylation[1, 2]
48HGSPEDHKMRADKVRacetylation[2]
60KVREIAAKLGRHVAIacetylation[2]
60KVREIAAKLGRHVAIpupylation[3]
75LGDLQGPKIRVSTFKacetylation[1, 2]
82KIRVSTFKEGKVFLNacetylation[1, 2]
85VSTFKEGKVFLNIGDacetylation[2]
93VFLNIGDKFLLDANLacetylation[2]
93VFLNIGDKFLLDANLpupylation[3]
102LLDANLGKGEGDKEKacetylation[1, 2]
107LGKGEGDKEKVGIDYacetylation[2]
115EKVGIDYKGLPADVVacetylation[2]
137DDGRVQLKVLEVQGMacetylation[1, 2]
160GGPLSNNKGINKLGGacetylation[2]
177SAEALTEKDKADIKTacetylation[2]
179EALTEKDKADIKTAAacetylation[2]
343RVCLGAEKIPSINVSacetylation[1, 2]
351IPSINVSKHRLDVQFacetylation[1, 2, 4]
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] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222]
 [4] 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 38 38 Potassium (By similarity).
 METAL 40 40 Potassium (By similarity).
 METAL 70 70 Potassium (By similarity).
 METAL 225 225 Magnesium (By similarity).
 METAL 252 252 Magnesium (By similarity).
 BINDING 36 36 Substrate (By similarity).
 BINDING 251 251 Substrate; via amide nitrogen (By
 BINDING 252 252 Substrate; via amide nitrogen (By
 BINDING 284 284 Substrate (By similarity).
 MOD_RES 351 351 N6-acetyllysine.  
Keyword
 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
 480 AA 
Protein Sequence
MSRRLRRTKI VTTLGPATDR DNNLEKVIAA GANVVRMNFS HGSPEDHKMR ADKVREIAAK 60
LGRHVAILGD LQGPKIRVST FKEGKVFLNI GDKFLLDANL GKGEGDKEKV GIDYKGLPAD 120
VVPGDILLLD DGRVQLKVLE VQGMKVFTEV TVGGPLSNNK GINKLGGGLS AEALTEKDKA 180
DIKTAALIGV DYLAVSFPRC GEDLNYARRL ARDAGCDAKI VAKVERAEAV CSQDAMDDII 240
LASDVVMVAR GDLGVEIGDP ELVGIQKALI RRARQLNRAV ITATQMMESM ITNPMPTRAE 300
VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMARVCLG AEKIPSINVS KHRLDVQFDN 360
VEEAIAMSAM YAANHLKGVT AIITMTESGR TALMTSRISS GLPIFAMSRH ERTLNLTALY 420
RGVTPVHFDS ANDGVAAASE AVNLLRDKGY LMSGDLVIVT QGDVMSTVGS TNTTRILTVE 480 
Gene Ontology
 GO:0005829; C:cytosol; 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.