CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002944
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glucose-1-phosphate adenylyltransferase 
Protein Synonyms/Alias
 ADP-glucose pyrophosphorylase; ADPGlc PPase; ADP-glucose synthase 
Gene Name
 glgC 
Gene Synonyms/Alias
 b3430; JW3393 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
6**MVSLEKNDHLMLAacetylation[1]
19LARQLPLKSVALILAacetylation[1]
50PAVHFGGKFRIIDFAacetylation[1]
109LPAQQRMKGENWYRGacetylation[1]
132LDIIRRYKAEYVVILacetylation[1]
195KIIEFVEKPANPPSMacetylation[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 synthesis of ADP-glucose, a sugar donor used in elongation reactions on alpha-glucans. 
Sequence Annotation
 BINDING 39 39 Allosteric activator.
 BINDING 114 114 Glucose-1-phosphate.
 BINDING 195 195 Glucose-1-phosphate.  
Keyword
 Allosteric enzyme; ATP-binding; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glycogen biosynthesis; Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 431 AA 
Protein Sequence
MVSLEKNDHL MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK FRIIDFALSN 60
CINSGIRRMG VITQYQSHTL VQHIQRGWSF FNEEMNEFVD LLPAQQRMKG ENWYRGTADA 120
VTQNLDIIRR YKAEYVVILA GDHIYKQDYS RMLIDHVEKG ARCTVACMPV PIEEASAFGV 180
MAVDENDKII EFVEKPANPP SMPNDPSKSL ASMGIYVFDA DYLYELLEED DRDENSSHDF 240
GKDLIPKITE AGLAYAHPFP LSCVQSDPDA EPYWRDVGTL EAYWKANLDL ASVVPELDMY 300
DRNWPIRTYN ESLPPAKFVQ DRSGSHGMTL NSLVSGGCVI SGSVVVQSVL FSRVRVNSFC 360
NIDSAVLLPE VWVGRSCRLR RCVIDRACVI PEGMVIGENA EEDARRFYRS EEGIVLVTRE 420
MLRKLGHKQE R 431 
Gene Ontology
 GO:0016208; F:AMP binding; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0005978; P:glycogen biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR005836; ADP_Glu_pyroP_CS.
 IPR011831; GlgC.
 IPR023049; GlgC_bac.
 IPR005835; NTP_transferase.
 IPR011004; Trimer_LpxA-like. 
Pfam
 PF00483; NTP_transferase 
SMART
  
PROSITE
 PS00808; ADP_GLC_PYROPHOSPH_1
 PS00809; ADP_GLC_PYROPHOSPH_2
 PS00810; ADP_GLC_PYROPHOSPH_3 
PRINTS