Q02U26 (Q02U26_PSEAB) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

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

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

Gene names

Ordered Locus Names:

PA14_05050

Organism

Pseudomonas aeruginosa (strain UCBPP-PA14) [Complete proteome] [HAMAP]

Taxonomic identifier

208963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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 MF_01405
Catalytic activity	A nucleoside triphosphate + H2O = a nucleotide + diphosphate. HAMAP MF_01405 SAAS SAAS020922
Cofactor	Binds 1 divalent metal cation ion per subunit; can use either magnesium or manganese By similarity. HAMAP MF_01405 SAAS SAAS020922
Subunit structure	Homodimer By similarity. HAMAP MF_01405 SAAS SAAS020922
Sequence similarities	Belongs to the HAM1 NTPase family. HAMAP MF_01405 RuleBase RU003781

Ontologies

Keywords
Biological process	Nucleotide metabolism HAMAP MF_01405 SAAS SAAS020922
Ligand	Magnesium HAMAP MF_01405 SAAS SAAS020922 Manganese HAMAP MF_01405 SAAS SAAS020922 Metal-binding HAMAP MF_01405 SAAS SAAS020922 Nucleotide-binding HAMAP MF_01405 SAAS SAAS020922
Molecular function	Hydrolase HAMAP MF_01405 SAAS SAAS020922 RuleBase RU003781
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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	11 – 16	6	Substrate binding By similarity HAMAP MF_01405
	Region	71 – 72	2	Substrate binding By similarity HAMAP MF_01405
Sites
	Metal binding	42	1	Magnesium or manganese By similarity HAMAP MF_01405
	Metal binding	71	1	Magnesium or manganese By similarity HAMAP MF_01405
	Binding site	158	1	Substrate By similarity HAMAP MF_01405
	Binding site	178	1	Substrate By similarity HAMAP MF_01405
	Binding site	184	1	Substrate By similarity HAMAP MF_01405

Sequences

	Sequence		Length	Mass (Da)
	Q02U26 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 778471EE9BD53531	FASTA	197	21,242
	10 20 30 40 50 60 MIKLEQLVLA SHNAGKLKEL QAMLGASVKV RSIGEFSQVE PEETGLSFVE NAILKARNAA 70 80 90 100 110 120 RLSGLPALAD DSGLAVDFLG GAPGIYSARY ADGRGDAANN AKLLEAMKDV PDAERGAQFV 130 140 150 160 170 180 SVLALVRHAD DPLPILCEGI WEGRILREAR GAHGFGYDPL FWVPERDCSS AELAPEEKNR 190 LSHRARAMAL LKQRLGL

References

[1]

"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial." Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M. Genome Biol. 7:R90.1-R90.14(2006) [PubMed: 17038190] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000438 Genomic DNA. Translation: ABJ15353.1.
RefSeq	YP_788560.1. NC_008463.1.
3D structure databases
ProteinModelPortal	Q02U26.
SMR	Q02U26. Positions 4-195.
ModBase	Search...
Protein-protein interaction databases
STRING	Q02U26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4383776.
GenomeReviews	Gene locus PA14_05050 in contig CP000438_GR.
KEGG	pau:PA14_05050.
PATRIC	19846864. VBIPseAer79785_0416.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0127.
HOGENOM	HBG697237.
OMA	YSKRYDQ.
ProtClustDB	PRK00120.
Enzyme and pathway databases
BioCyc	PAER208963:PA14_05050-MONOMER.
Family and domain databases
HAMAP	MF_01405. Non_canon_purine_NTPase. [Tree]
InterPro	IPR002637. Ham1p-like. IPR020922. Nucleoside-triphosphatase. [Graphical view]
KO	K02428.
PANTHER	PTHR11067. Ham1p_like. 1 hit.
Pfam	PF01725. Ham1p_like. 1 hit. [Graphical view]
TIGRFAMs	TIGR00042. TIGR00042. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q02U26_PSEAB

Accession

Primary (citable) accession number: Q02U26

Entry history

Integrated into UniProtKB/TrEMBL:	November 14, 2006
Last sequence update:	November 14, 2006
Last modified:	December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)