CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002997
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CTP synthase 
Protein Synonyms/Alias
 CTP synthetase; UTP--ammonia ligase 
Gene Name
 pyrG 
Gene Synonyms/Alias
 b2780; JW2751 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
233LFCNVPEKAVISLKDacetylation[1, 2]
239EKAVISLKDVDSIYKacetylation[1, 2, 3]
246KDVDSIYKIPGLLKSacetylation[2]
262GLDDYICKRFSLNCPacetylation[2]
306IELPDAYKSVIEALKacetylation[2]
313KSVIEALKHGGLKNRacetylation[2]
342TRGVEILKGLDAILVacetylation[2]
479EVNNMLLKQIEDAGLacetylation[2]
534PLFAGFVKAASEFQKacetylation[2]
541KAASEFQKRQAK***acetylation[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] 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
 Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. 
Sequence Annotation
 DOMAIN 291 542 Glutamine amidotransferase type-1.
 REGION 2 253 Aminator domain.
 ACT_SITE 379 379 Nucleophile (Probable).
 ACT_SITE 515 515 By similarity.
 ACT_SITE 517 517 By similarity.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Glutamine amidotransferase; Ligase; Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 545 AA 
Protein Sequence
MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPIQHGEV 60
FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL RKERRGDYLG ATVQVIPHIT 120
NAIKERVLEG GEGHDVVLVE IGGTVGDIES LPFLEAIRQM AVEIGREHTL FMHLTLVPYM 180
AASGEVKTKP TQHSVKELLS IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD 240
VDSIYKIPGL LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE 300
LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP GGFGYRGVEG 360
MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN STEFVPDCKY PVVALITEWR 420
DENGNVEVRS EKSDLGGTMR LGAQQCQLVD DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ 480
IEDAGLRVAG RSGDDQLVEI IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ 540
KRQAK 545 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003883; F:CTP synthase activity; IDA:EcoCyc.
 GO:0042802; F:identical protein binding; IDA:EcoCyc.
 GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006241; P:CTP biosynthetic process; IDA:EcoCyc.
 GO:0006541; P:glutamine metabolic process; IEA:HAMAP. 
Interpro
 IPR004468; CTP_synthase.
 IPR017456; CTP_synthase_N.
 IPR017926; GATASE.
 IPR027417; P-loop_NTPase. 
Pfam
 PF06418; CTP_synth_N
 PF00117; GATase 
SMART
  
PROSITE
 PS51273; GATASE_TYPE_1 
PRINTS