UniProt Accession

 YFBR_ECOLI; P76491; Q2MAM2 

Genbank Protein ID

 U00096; AP009048 

Genbank Nucleotide ID

 AAC75351.1; BAE76684.1 

Protein Name

 5'-nucleotidase YfbR 

Protein Synonyms/Alias

 5'-deoxyribonucleotidase; Nucleoside 5'-monophosphate phosphohydrolase 

Gene Name

 yfbR 

Gene Synonyms/Alias

 b2291; JW2288 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
94	SQIAQEYKAIEKIAQ	acetylation	[1]
98	QEYKAIEKIAQQKLV	acetylation	[1]
130	HAYSDEEKSLVKQAD	acetylation	[1]
134	DEEKSLVKQADALCA	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

 Nucleotidase that shows strict specificity toward deoxyribonucleoside 5'-monophosphates and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates. Might be involved in the regulation of all dNTP pools in E.coli. 

Sequence Annotation

  

Keyword

 3D-structure; Cobalt; Complete proteome; Copper; Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleotide-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 199 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008253; F:5'-nucleotidase activity; IEA:EC.
 GO:0050897; F:cobalt ion binding; IDA:EcoCyc.
 GO:0008252; F:nucleotidase activity; IDA:EcoCyc.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
 GO:0006226; P:dUMP biosynthetic process; IMP:EcoCyc. 

Interpro

 IPR022971; dCMP_phosphohydrolase.
 IPR003607; HD/PDEase_dom.
 IPR006674; HD_domain. 

Pfam

 PF01966; HD 

SMART

 SM00471; HDc 

PROSITE

  

PRINTS