CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002089
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GMP synthase [glutamine-hydrolyzing] 
Protein Synonyms/Alias
 GMP synthetase; GMPS; Glutamine amidotransferase 
Gene Name
 guaA 
Gene Synonyms/Alias
 b2507; JW2491 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
7*MTENIHKHRILILDacetylation[1]
134DALTADGKPLLDVWMacetylation[2]
212EALWTPAKIIDDAVAacetylation[2]
330ALKLEDVKWLAQGTIacetylation[2]
351SAASATGKAHVIKSHacetylation[2]
369GGLPKEMKMGLVEPLacetylation[2]
377MGLVEPLKELFKDEVacetylation[2]
381EPLKELFKDEVRKIGacetylation[2]
417VRVLGEVKKEYCDLLacetylation[2]
437IFIEELRKADLYDKVpupylation[3]
443RKADLYDKVSQAFTVacetylation[2]
465GVMGDGRKYDWVVSLacetylation[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] 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] 
Functional Description
 Catalyzes the synthesis of GMP from XMP. 
Sequence Annotation
 DOMAIN 9 207 Glutamine amidotransferase type-1.
 DOMAIN 208 400 GMPS ATP-PPase.
 NP_BIND 235 241 ATP.
 ACT_SITE 86 86 Nucleophile.
 ACT_SITE 181 181
 ACT_SITE 183 183  
Keyword
 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Glutamine amidotransferase; GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 525 AA 
Protein Sequence
MTENIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIRDFN PSGIILSGGP 60
ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV EASNEREFGY AQVEVVNDSA 120
LVRGIEDALT ADGKPLLDVW MSHGDKVTAI PSDFITVAST ESCPFAIMAN EEKRFYGVQF 180
HPEVTHTRQG MRMLERFVRD ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS 240
SVTAMLLHRA IGKNLTCVFV DNGLLRLNEA EQVLDMFGDH FGLNIVHVPA EDRFLSALAG 300
ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG KAHVIKSHHN 360
VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR HPFPGPGLGV RVLGEVKKEY 420
CDLLRRADAI FIEELRKADL YDKVSQAFTV FLPVRSVGVM GDGRKYDWVV SLRAVETIDF 480
MTAHWAHLPY DFLGRVSNRI INEVNGISRV VYDISGKPPA TIEWE 525 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IDA:EcoCyc.
 GO:0003921; F:GMP synthase activity; IDA:EcoCyc.
 GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
 GO:0006541; P:glutamine metabolic process; IEA:HAMAP. 
Interpro
 IPR017926; GATASE.
 IPR001674; GMP_synth_C.
 IPR004739; GMP_synth_N.
 IPR022955; GMP_synthase.
 IPR025777; GMPS_ATP_PPase_dom.
 IPR022310; NAD/GMP_synthase.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00117; GATase
 PF00958; GMP_synt_C
 PF02540; NAD_synthase 
SMART
  
PROSITE
 PS51273; GATASE_TYPE_1
 PS51553; GMPS_ATP_PPASE 
PRINTS