UniProt Accession

 RDGB_ECOLI; P52061; Q2M9N9 

Genbank Protein ID

 U28377; U00096; AP009048 

Genbank Nucleotide ID

 AAA69121.1; AAC75991.1; BAE77017.1 

Protein Name

 dITP/XTP pyrophosphatase 

Protein Synonyms/Alias

 Non-canonical purine NTP pyrophosphatase; Non-standard purine NTP pyrophosphatase; Nucleoside-triphosphate diphosphatase; Nucleoside-triphosphate pyrophosphatase; NTPase 

Gene Name

 rdgB 

Gene Synonyms/Alias

 yggV; b2954; JW2921 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
3	*****MQKVVLATGN	pupylation	[1]
13	LATGNVGKVRELASL	acetylation	[2]
97	GEDATDQKNLQKLLE	acetylation	[2]
101	TDQKNLQKLLETMKD	acetylation	[2]
107	QKLLETMKDVPDDQR	acetylation	[2]
177	AELTREEKSAISHRG	acetylation	[2]
188	SHRGQALKLLLDALR	acetylation	[2]

Reference

 [1] 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]
 [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] 

Functional Description

 Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) to their respective monophosphate derivatives. Probably excludes non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions. 

Sequence Annotation

 REGION 8 13 Substrate binding (By similarity).
 REGION 69 70 Substrate binding (By similarity).
 METAL 40 40 Magnesium or manganese (By similarity).
 METAL 69 69 Magnesium or manganese (By similarity).
 BINDING 157 157 Substrate (By similarity).
 BINDING 177 177 Substrate (By similarity).
 BINDING 183 183 Substrate (By similarity).  

Keyword

 3D-structure; Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; Nickel; Nucleotide metabolism; Nucleotide-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 197 AA 

Protein Sequence

Gene Ontology

 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:EcoCyc.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0009143; P:nucleoside triphosphate catabolic process; IDA:EcoCyc.
 GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP. 

Interpro

 IPR002637; Ham1p-like.
 IPR020922; NTPase. 

Pfam

 PF01725; Ham1p_like 

SMART

  

PROSITE

  

PRINTS