A8FFY5 (A8FFY5_BACP2) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Non-canonical purine NTP pyrophosphatase HAMAP-Rule MF_01405
EC=3.6.1.19 HAMAP-Rule MF_01405

Alternative name(s):
Non-standard purine NTP pyrophosphatase HAMAP-Rule MF_01405
Nucleoside-triphosphate diphosphatase HAMAP-Rule MF_01405
Nucleoside-triphosphate pyrophosphatase HAMAP-Rule MF_01405

Gene names

Name:	ysnA EMBL ABV63152.1
Ordered Locus Names:	BPUM_2490

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP] EMBL ABV63152.1

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus pumilus

Protein attributes

Sequence length	197 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 SAAS SAAS020922
Cofactor	Binds 1 divalent metal cation ion per subunit; can use either magnesium or manganese By similarity. HAMAP-Rule MF_01405 SAAS SAAS020922
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_01405 SAAS SAAS020922
Sequence similarities	Belongs to the HAM1 NTPase family. HAMAP-Rule MF_01405 RuleBase RU003781

Ontologies

Keywords
Biological process	Nucleotide metabolism HAMAP-Rule MF_01405 SAAS SAAS020922
Ligand	Magnesium HAMAP-Rule MF_01405 SAAS SAAS020922 Manganese HAMAP-Rule MF_01405 SAAS SAAS020922 Metal-binding HAMAP-Rule MF_01405 SAAS SAAS020922 Nucleotide-binding HAMAP-Rule MF_01405 SAAS SAAS020922
Molecular function	Hydrolase HAMAP-Rule MF_01405 RuleBase RU003781 SAAS SAAS020922
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
Regions
	Region	8 – 13	6	Substrate binding By similarity HAMAP-Rule MF_01405
	Region	70 – 71	2	Substrate binding By similarity HAMAP-Rule MF_01405
Sites
	Metal binding	41	1	Magnesium or manganese By similarity HAMAP-Rule MF_01405
	Metal binding	70	1	Magnesium or manganese By similarity HAMAP-Rule MF_01405
	Binding site	156	1	Substrate By similarity HAMAP-Rule MF_01405
	Binding site	176	1	Substrate By similarity HAMAP-Rule MF_01405
	Binding site	182	1	Substrate By similarity HAMAP-Rule MF_01405

Sequences

	Sequence		Length	Mass (Da)
	A8FFY5 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 6BAF01A735BAE2D3	FASTA	197	21,370
	10 20 30 40 50 60 MKTAIIATHN AGKAKEFKAI LEPKGFTVKT LADIGFIEEI EETGHTFEEN AVIKAEAIQA 70 80 90 100 110 120 KAGEMVIADD SGLSIDYLGG KPGVYSARYA GEHKNDAENV EKVLSELQGI EKEDRTARFR 130 140 150 160 170 180 CALAVSIPGK ETKTVEGSVE GFIAEEPIGE NGFGYDPIFI VKDKDQTMAE LSPEEKNKIS 190 HRAVALQKLS SLLDANE

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV63152.1.
RefSeq	YP_001487712.1. NC_009848.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	315750.BPUM_2490.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV63152; ABV63152; BPUM_2490.
GeneID	5621760.
KEGG	bpu:BPUM_2490.
PATRIC	18968904. VBIBacPum16546_2546.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0127.
HOGENOM	HOG000293319.
KO	K02428.
OMA	DGTLVWP.
ProtClustDB	PRK14822.
Enzyme and pathway databases
BioCyc	BPUM315750:GH6N-2578-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

A8FFY5_BACP2

Accession

Primary (citable) accession number: A8FFY5

Entry history

Integrated into UniProtKB/TrEMBL:	November 13, 2007
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)