A2BUR0 (A2BUR0_PROM5) 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:

P9515_03121

Organism

Prochlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP] EMBL ABM71521.1

Taxonomic identifier

167542 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	191 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 EMBL ABM71521.1
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	8 – 13	6	Substrate binding By similarity HAMAP MF_01405
	Region	67 – 68	2	Substrate binding By similarity HAMAP MF_01405
Sites
	Metal binding	38	1	Magnesium or manganese By similarity HAMAP MF_01405
	Metal binding	67	1	Magnesium or manganese By similarity HAMAP MF_01405
	Binding site	149	1	Substrate By similarity HAMAP MF_01405
	Binding site	169	1	Substrate By similarity HAMAP MF_01405
	Binding site	175	1	Substrate By similarity HAMAP MF_01405

Sequences

	Sequence		Length	Mass (Da)
	A2BUR0 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: 558AAF82B958906C	FASTA	191	21,428
	10 20 30 40 50 60 MKILYLASKN FGKIKEYKKL LSNVNCQLLL QPESIEVEEN GNTFRENAIK KACEVSKKTG 70 80 90 100 110 120 NYAIADDSGI CIDALDGKPG IYSSRYAEND QRRIERVLKE LDGEKNRCAF FIANVCVCSP 130 140 150 160 170 180 SGDLILESEA KCFGNIIEKP RGNSGFGYDP IFEEVSSRLT FAEMNNELKD ECSHRGKALK 190 KIIPQLLEIF A

References

[1]

"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000552 Genomic DNA. Translation: ABM71521.1.
RefSeq	YP_001010628.1. NC_008817.1.
3D structure databases
ProteinModelPortal	A2BUR0.
ModBase	Search...
Protein-protein interaction databases
STRING	A2BUR0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4718670.
GenomeReviews	Gene locus P9515_03121 in contig CP000552_GR.
KEGG	pmc:P9515_03121.
PATRIC	23014154. VBIProMar113831_0317.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0127.
HOGENOM	HBG697237.
OMA	ESSTRLT.
PhylomeDB	A2BUR0.
ProtClustDB	PRK00120.
Enzyme and pathway databases
BioCyc	PMAR167542:P9515ORF_0325-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

A2BUR0_PROM5

Accession

Primary (citable) accession number: A2BUR0

Entry history

Integrated into UniProtKB/TrEMBL:	February 20, 2007
Last sequence update:	February 20, 2007
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)