Q4ZZ80 (Q4ZZ80_PSEU2) 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:

Psyr_0472

Organism

Pseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP] EMBL AAY35542.1

Taxonomic identifier

205918 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas syringae

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

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
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	10 – 15	6	Substrate binding By similarity HAMAP MF_01405
	Region	70 – 71	2	Substrate binding By similarity HAMAP MF_01405
Sites
	Metal binding	41	1	Magnesium or manganese By similarity HAMAP MF_01405
	Metal binding	70	1	Magnesium or manganese By similarity HAMAP MF_01405
	Binding site	157	1	Substrate By similarity HAMAP MF_01405
	Binding site	177	1	Substrate By similarity HAMAP MF_01405
	Binding site	183	1	Substrate By similarity HAMAP MF_01405

Sequences

	Sequence		Length	Mass (Da)
	Q4ZZ80 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 66FCA62653A316A3	FASTA	197	21,165
	10 20 30 40 50 60 MNLTQLVLAS HNGGKLKELQ AMLGDSVTLR SVSEFSLVEP EETGLSFVEN AILKARNAAR 70 80 90 100 110 120 LSGLPALADD SGLAVDFLGG APGIYSARYA DGQGDAANNA KLLEALKDVP DEQRGAQFVC 130 140 150 160 170 180 VLALVRHADD PLPILCEGLW HGRILHAASG EHGFGYDPLF WVPERNCSSA ELGPTEKNQL 190 SHRARAMVLL RQRLGLQ

References

[1]

"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000." Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E. Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed: 16043691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000075 Genomic DNA. Translation: AAY35542.1.
RefSeq	YP_233580.1. NC_007005.1.
3D structure databases
ProteinModelPortal	Q4ZZ80.
SMR	Q4ZZ80. Positions 3-194.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4ZZ80.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3365948.
GenomeReviews	Gene locus Psyr_0472 in contig CP000075_GR.
KEGG	psb:Psyr_0472.
NMPDR	fig|205918.4.peg.805.
PATRIC	19981371. VBIPseSyr42314_0491.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0127.
HOGENOM	HBG697237.
OMA	YSKRYDQ.
PhylomeDB	Q4ZZ80.
ProtClustDB	PRK00120.
Enzyme and pathway databases
BioCyc	PSYR205918:PSYR_0472-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

Q4ZZ80_PSEU2

Accession

Primary (citable) accession number: Q4ZZ80

Entry history

Integrated into UniProtKB/TrEMBL:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	December 14, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)