CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007748
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ADP compounds hydrolase NudE 
Protein Synonyms/Alias
  
Gene Name
 nudE 
Gene Synonyms/Alias
 yrfE; b3397; JW3360 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
7*MSKSLQKPTILNVEacetylation[1]
111ANDLTFLKKLSMAPSacetylation[1]
181FLVREWLKGQGRV**acetylation[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
 Active on adenosine(5')triphospho(5')adenosine (Ap3A), ADP-ribose, NADH, adenosine(5')diphospho(5')adenosine (Ap2A). 
Sequence Annotation
 DOMAIN 45 172 Nudix hydrolase.
 MOTIF 80 101 Nudix box.
 METAL 95 95 Divalent metal cation (By similarity).
 METAL 99 99 Divalent metal cation (By similarity).
 BINDING 40 40 Substrate; via amide nitrogen and
 BINDING 118 118 Substrate; via carbonyl oxygen.  
Keyword
 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 186 AA 
Protein Sequence
MSKSLQKPTI LNVETVARSR LFTVESVDLE FSNGVRRVYE RMRPTNREAV MIVPIVDDHL 60
ILIREYAVGT ESYELGFSKG LIDPGESVYE AANRELKEEV GFGANDLTFL KKLSMAPSYF 120
SSKMNIVVAQ DLYPESLEGD EPEPLPQVRW PLAHMMDLLE DPDFNEARNV SALFLVREWL 180
KGQGRV 186 
Gene Ontology
 GO:0019144; F:ADP-sugar diphosphatase activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR020084; NUDIX_hydrolase_CS.
 IPR000086; NUDIX_hydrolase_dom.
 IPR015797; NUDIX_hydrolase_dom-like. 
Pfam
 PF00293; NUDIX 
SMART
  
PROSITE
 PS51462; NUDIX
 PS00893; NUDIX_BOX 
PRINTS