CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003515
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonucleotide monophosphatase NagD 
Protein Synonyms/Alias
  
Gene Name
 nagD 
Gene Synonyms/Alias
 b0675; JW0661 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
129YNWDMMHKAAYFVANacetylation[1]
165ALCAGIEKISGRKPFacetylation[1]
170IEKISGRKPFYVGKPacetylation[1]
176RKPFYVGKPSPWIIRacetylation[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 dephosphorylation of an unusually broad range of substrate including deoxyribo- and ribonucleoside tri-, di-, and monophosphates, as well as polyphosphate and glucose-1-P (Glu1P). 
Sequence Annotation
 REGION 42 43 Substrate binding.
 REGION 202 205 Substrate binding.
 ACT_SITE 11 11
 METAL 9 9 Magnesium.
 METAL 11 11 Magnesium; via carbonyl oxygen.
 METAL 201 201 Magnesium.
 BINDING 11 11 Substrate.
 BINDING 176 176 Substrate.  
Keyword
 3D-structure; Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 250 AA 
Protein Sequence
MTIKNVICDI DGVLMHDNVA VPGAAEFLHG IMDKGLPLVL LTNYPSQTGQ DLANRFATAG 60
VDVPDSVFYT SAMATADFLR RQEGKKAYVV GEGALIHELY KAGFTITDVN PDFVIVGETR 120
SYNWDMMHKA AYFVANGARF IATNPDTHGR GFYPACGALC AGIEKISGRK PFYVGKPSPW 180
IIRAALNKMQ AHSEETVIVG DNLRTDILAG FQAGLETILV LSGVSSLDDI DSMPFRPSWI 240
YPSVAEIDVI 250 
Gene Ontology
 GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0005975; P:carbohydrate metabolic process; TAS:EcoCyc.
 GO:0034655; P:nucleobase-containing compound catabolic process; IDA:EcoCyc. 
Interpro
 IPR023214; HAD-like_dom.
 IPR006357; HAD-SF_hydro_IIA.
 IPR023215; NPhePase-like_dom. 
Pfam
 PF00702; Hydrolase 
SMART
  
PROSITE
  
PRINTS