B7GN27 (NTPA_BIFLS) 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:

Blon_0412, BLIJ_0420

Organism

Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) [Complete proteome] [HAMAP]

Taxonomic identifier

391904 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium › Bifidobacterium longum › Bifidobacterium longum subsp. infantis

Protein attributes

Sequence length	252 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
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 – 252	252	Non-canonical purine NTP pyrophosphatase HAMAP-Rule MF_01405		PRO_1000184578
Regions
	Region	7 – 12	6	Substrate binding By similarity
	Region	74 – 75	2	Substrate binding By similarity
Sites
	Metal binding	74	1	Magnesium or manganese By similarity
	Binding site	196	1	Substrate By similarity
	Binding site	230	1	Substrate By similarity
	Binding site	236	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7GN27 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 0C3290BF5D6A6DD4	FASTA	252	26,368
	10 20 30 40 50 60 MQIVVATHNE GKLVEIRRIL EEDLGVDAEN IELVSAGSLH LPDPVETGVT FQENALLKAR 70 80 90 100 110 120 AVAIRTGLPA VADDSGLIVD VMGNAPGILS ARWAGAHGHD KANNALLLAQ IGDIPDDKRT 130 140 150 160 170 180 ARFRCAAALV VPDTEAGADV TGGVAADGIT VHTTAADGST APVHARYAIK SETVELGDMP 190 200 210 220 230 240 GRIIREARGE HGFGYDPLFV PDDQPAGRVS TEPDHEGEPL TSAEMTSAEK NAISHRGKAL 250 KALVPAIEAL LH

References

[1]

"The genome sequence of Bifidobacterium longum subsp. infantis reveals adaptations for milk utilization within the infant microbiome." Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., Richardson P.M., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.

[2]

"Bifidobacteria can protect from enteropathogenic infection through production of acetate." Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., Morita H., Hattori M., Ohno H. Nature 469:543-547(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001095 Genomic DNA. Translation: ACJ51533.1. AP010889 Genomic DNA. Translation: BAJ68014.1.
RefSeq	YP_002321911.1. NC_011593.1. YP_005584184.1. NC_017219.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	391904.Blon_0412.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACJ51533; ACJ51533; Blon_0412. BAJ68014; BAJ68014; BLIJ_0420.
GeneID	12167331. 7053505.
KEGG	bln:Blon_0412. blon:BLIJ_0420.
PATRIC	21121758. VBIBifLon71229_0413.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0127.
HOGENOM	HOG000293319.
KO	K02428.
ProtClustDB	PRK00120.
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]
ProtoNet	Search...

Entry information

Entry name

NTPA_BIFLS

Accession

Primary (citable) accession number: B7GN27
Secondary accession number(s): E8MPT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program