Q7VXX8 (NTPA_BORPE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Non-canonical purine NTP pyrophosphatase
EC=3.6.1.19

Alternative name(s):
Non-standard purine NTP pyrophosphatase
Nucleoside-triphosphate diphosphatase
Nucleoside-triphosphate pyrophosphatase
Short name=NTPase

Gene names

Ordered Locus Names:

BP1593

Organism

Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) [Reference proteome] [HAMAP]

Taxonomic identifier

257313 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella pertussis

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP/dITP to their respective monophosphate derivatives. Might exclude non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions By similarity. HAMAP-Rule MF_01405
Catalytic activity	A nucleoside triphosphate + H2O = a nucleotide + diphosphate. HAMAP-Rule MF_01405
Cofactor	Binds 1 divalent metal cation ion per subunit; can use either magnesium or manganese By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the HAM1 NTPase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleoside triphosphate catabolic process Inferred from electronic annotation. Source: InterPro purine nucleotide metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro nucleoside-triphosphate diphosphatase activity Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	Non-canonical purine NTP pyrophosphatase HAMAP-Rule MF_01405		PRO_0000178139
Regions
	Region	17 – 22	6	Substrate binding By similarity
	Region	78 – 79	2	Substrate binding By similarity
Sites
	Metal binding	49	1	Magnesium or manganese By similarity
	Metal binding	78	1	Magnesium or manganese By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	187	1	Substrate By similarity
	Binding site	193	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VXX8 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: E28CCDC43979B94C	FASTA	213	22,591
	10 20 30 40 50 60 MSAEILNPNL RRVVLASNNA GKLREFSALF APLGIELVPQ SELGVSEAEE PHATFVENAL 70 80 90 100 110 120 AKARHASRHT GLPALADDSG LCVVALGGAP GVHSARYAQQ PGGARSDAAN NALLVRELAA 130 140 150 160 170 180 AGDRRAWYVA LLALVRTEND PCPLIGEGLW HGEIVDAPAG EHGFGYDPHF YLPQQGCTAA 190 200 210 QLAPEHKNRI SHRAQALAQL LDKLRATGPV DRP

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640415 Genomic DNA. Translation: CAE41882.1.
RefSeq	NP_880326.1. NC_002929.2.
3D structure databases
ProteinModelPortal	Q7VXX8.
ModBase	Search...
Protein-protein interaction databases
STRING	257313.BP1593.
Proteomic databases
PRIDE	Q7VXX8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE41882; CAE41882; BP1593.
GeneID	2666612.
KEGG	bpe:BP1593.
PATRIC	21156432. VBIBorPer7866_1710.
Phylogenomic databases
eggNOG	COG0127.
HOGENOM	HOG000293319.
KO	K02428.
OMA	DGTLVWP.
ProtClustDB	PRK00120.
Enzyme and pathway databases
BioCyc	BPER257313:BP1593-MONOMER.
Family and domain databases
HAMAP	MF_01405. Non_canon_purine_NTPase.
InterPro	IPR002637. Ham1p-like. IPR020922. Nucleoside-triphosphatase. [Graphical view]
PANTHER	PTHR11067. PTHR11067. 1 hit.
Pfam	PF01725. Ham1p_like. 1 hit. [Graphical view]
TIGRFAMs	TIGR00042. TIGR00042. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NTPA_BORPE

Accession

Primary (citable) accession number: Q7VXX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program