CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002981
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoglycerate kinase 
Protein Synonyms/Alias
  
Gene Name
 pgk 
Gene Synonyms/Alias
 b2926; JW2893 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
5***MSVIKMTDLDLAacetylation[1, 2]
14TDLDLAGKRVFIRADacetylation[1, 2]
27ADLNVPVKDGKVTSDacetylation[1, 2]
30NVPVKDGKVTSDARIacetylation[1, 2]
49PTIELALKQGAKVMVacetylation[1, 2]
82LPVVNYLKDKLSNPVacetylation[1, 2]
84VVNYLKDKLSNPVRLacetylation[1, 2, 3]
93SNPVRLVKDYLDGVDacetylation[1, 2]
116LENVRFNKGEKKDDEacetylation[2, 4]
119VRFNKGEKKDDETLSacetylation[2]
120RFNKGEKKDDETLSKacetylation[1, 2]
127KDDETLSKKYAALCDacetylation[2]
128DDETLSKKYAALCDVacetylation[1]
156ASTHGIGKFADVACAacetylation[1, 2]
176AELDALGKALKEPARacetylation[1, 2]
179DALGKALKEPARPMVacetylation[1, 2]
193VAIVGGSKVSTKLTVacetylation[2]
197GGSKVSTKLTVLDSLacetylation[1, 2]
206TVLDSLSKIADQLIVacetylation[1]
243ADLVDEAKRLLTTCNacetylation[1, 2]
272ETAPATLKSVNDVKAacetylation[1, 2]
278LKSVNDVKADEQILDacetylation[1, 2]
299QELAEILKNAKTILWacetylation[1, 2]
302AEILKNAKTILWNGPacetylation[1, 2]
373FLEFVEGKVLPAVAMacetylation[1]
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]
 [4] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508
Functional Description
  
Sequence Annotation
 NP_BIND 340 343 ATP (By similarity).
 REGION 21 23 Substrate binding (By similarity).
 REGION 59 62 Substrate binding (By similarity).
 BINDING 36 36 Substrate (By similarity).
 BINDING 113 113 Substrate (By similarity).
 BINDING 146 146 Substrate (By similarity).
 BINDING 197 197 ATP (By similarity).
 BINDING 314 314 ATP (By similarity).
 MOD_RES 84 84 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 387 AA 
Protein Sequence
MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAS LPTIELALKQ GAKVMVTSHL 60
GRPTEGEYNE EFSLLPVVNY LKDKLSNPVR LVKDYLDGVD VAEGELVVLE NVRFNKGEKK 120
DDETLSKKYA ALCDVFVMDA FGTAHRAQAS THGIGKFADV ACAGPLLAAE LDALGKALKE 180
PARPMVAIVG GSKVSTKLTV LDSLSKIADQ LIVGGGIANT FIAAQGHDVG KSLYEADLVD 240
EAKRLLTTCN IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN 300
AKTILWNGPV GVFEFPNFRK GTEIVANAIA DSEAFSIAGG GDTLAAIDLF GIADKISYIS 360
TGGGAFLEFV EGKVLPAVAM LEERAKK 387 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004618; F:phosphoglycerate kinase activity; IEA:HAMAP.
 GO:0006096; P:glycolysis; IEA:HAMAP. 
Interpro
 IPR001576; Phosphoglycerate_kinase.
 IPR015901; Phosphoglycerate_kinase_C.
 IPR015911; Phosphoglycerate_kinase_CS.
 IPR015824; Phosphoglycerate_kinase_N. 
Pfam
 PF00162; PGK 
SMART
  
PROSITE
 PS00111; PGLYCERATE_KINASE 
PRINTS
 PR00477; PHGLYCKINASE.