CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005191
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoenolpyruvate synthase 
Protein Synonyms/Alias
 PEP synthase; Pyruvate, water dikinase 
Gene Name
 ppsA 
Gene Synonyms/Alias
 pps; b1702; JW1692 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
75RIYELLDKTDIDDVTacetylation[1]
86DDVTQLAKAGAQIRQacetylation[1]
277APTQEHGKQVKIEDVacetylation[1]
280QEHGKQVKIEDVPQEacetylation[1]
304EEVQELAKQAVQIEKacetylation[1]
311KQAVQIEKHYGRPMDacetylation[1]
323PMDIEWAKDGHTGKLacetylation[1]
329AKDGHTGKLFIVQARacetylation[1]
357YTLHSQGKIIAEGRAacetylation[1]
406PDWEPIMKKASAIVTacetylation[1]
485TMPDLPLKVMMNVGNacetylation[1]
546NEIREMMKGFDSPREacetylation[1]
573LGAAFYPKRVIVRLSacetylation[1]
583IVRLSDFKSNEYANLacetylation[1]
655VRTVDQAKAVVEELAacetylation[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] 
Functional Description
 Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. 
Sequence Annotation
 ACT_SITE 421 421 Tele-phosphohistidine intermediate (By
 ACT_SITE 751 751 Proton donor (By similarity).
 METAL 680 680 Magnesium (By similarity).
 METAL 704 704 Magnesium (By similarity).
 BINDING 511 511 Substrate (By similarity).
 BINDING 578 578 Substrate (By similarity).
 BINDING 680 680 Substrate (By similarity).
 BINDING 701 701 Substrate; via carbonyl oxygen (By
 BINDING 702 702 Substrate; via amide nitrogen (By
 BINDING 703 703 Substrate (By similarity).
 BINDING 704 704 Substrate; via amide nitrogen (By  
Keyword
 ATP-binding; Complete proteome; Direct protein sequencing; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 792 AA 
Protein Sequence
MSNNGSSPLV LWYNQLGMND VDRVGGKNAS LGEMITNLSG MGVSVPNGFA TTADAFNQFL 60
DQSGVNQRIY ELLDKTDIDD VTQLAKAGAQ IRQWIIDTPF QPELENAIRE AYAQLSADDE 120
NASFAVRSSA TAEDMPDASF AGQQETFLNV QGFDAVLVAV KHVFASLFND RAISYRVHQG 180
YDHRGVALSA GVQRMVRSDL ASSGVMFSID TESGFDQVVF ITSAWGLGEM VVQGAVNPDE 240
FYVHKPTLAA NRPAIVRRTM GSKKIRMVYA PTQEHGKQVK IEDVPQEQRD IFSLTNEEVQ 300
ELAKQAVQIE KHYGRPMDIE WAKDGHTGKL FIVQARPETV RSRGQVMERY TLHSQGKIIA 360
EGRAIGHRIG AGPVKVIHDI SEMNRIEPGD VLVTDMTDPD WEPIMKKASA IVTNRGGRTC 420
HAAIIARELG IPAVVGCGDA TERMKDGENV TVSCAEGDTG YVYAELLEFS VKSSSVETMP 480
DLPLKVMMNV GNPDRAFDFA CLPNEGVGLA RLEFIINRMI GVHPRALLEF DDQEPQLQNE 540
IREMMKGFDS PREFYVGRLT EGIATLGAAF YPKRVIVRLS DFKSNEYANL VGGERYEPDE 600
ENPMLGFRGA GRYVSDSFRD CFALECEAVK RVRNDMGLTN VEIMIPFVRT VDQAKAVVEE 660
LARQGLKRGE NGLKIIMMCE IPSNALLAEQ FLEYFDGFSI GSNDMTQLAL GLDRDSGVVS 720
ELFDERNDAV KALLSMAIRA AKKQGKYVGI CGQGPSDHED FAAWLMEEGI DSLSLNPDTV 780
VQTWLSLAEL KK 792 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0008986; F:pyruvate, water dikinase activity; IDA:EcoCyc.
 GO:0006094; P:gluconeogenesis; IMP:EcoCyc.
 GO:0006090; P:pyruvate metabolic process; IEA:InterPro. 
Interpro
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR008279; PEP-util_enz_mobile_dom.
 IPR006319; PEP_synth.
 IPR018274; PEP_util_AS.
 IPR000121; PEP_util_C.
 IPR023151; PEP_util_CS.
 IPR002192; PPDK_PEP-bd.
 IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. 
Pfam
 PF00391; PEP-utilizers
 PF02896; PEP-utilizers_C
 PF01326; PPDK_N 
SMART
  
PROSITE
 PS00742; PEP_ENZYMES_2
 PS00370; PEP_ENZYMES_PHOS_SITE 
PRINTS