B4S3H0 (B4S3H0_PROA2) 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:

Paes_1691

Organism

Prosthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP] EMBL ACF46709.1

Taxonomic identifier

290512 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Prosthecochloris

Protein attributes

Sequence length	221 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	15 – 20	6	Substrate binding By similarity HAMAP MF_01405
	Region	84 – 85	2	Substrate binding By similarity HAMAP MF_01405
Sites
	Metal binding	50	1	Magnesium or manganese By similarity HAMAP MF_01405
	Metal binding	84	1	Magnesium or manganese By similarity HAMAP MF_01405
	Binding site	179	1	Substrate By similarity HAMAP MF_01405
	Binding site	199	1	Substrate By similarity HAMAP MF_01405
	Binding site	205	1	Substrate By similarity HAMAP MF_01405

Sequences

	Sequence		Length	Mass (Da)
	B4S3H0 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: B37A7BDD0FB18E85	FASTA	221	24,133
	10 20 30 40 50 60 MTASRAEKTA IVLATNNPDK VREIKPMLMG LSSSVQVYSL SDLGVDRAIE ETESTLEGNA 70 80 90 100 110 120 KLKADAIFNH LSDRFENLIS LADDTGLEVD ALKGAPGVYS ARFAPMPEGR EPSYEDNVQH 130 140 150 160 170 180 LLTTMQHTLE RSATFRTVIA IKGRLSEKNG ISEIEETVEG KVAGSIAKEK TGNGGFGYDP 190 200 210 220 IFWVNSAQAT FAEMTTEEKN RLSHRSLAVQ KAVETLRDIL S

References

[1]

"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F. , Overmann J., Bryant D.A., Richardson P. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 271 / SK 413.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001108 Genomic DNA. Translation: ACF46709.1.
RefSeq	YP_002016356.1. NC_011059.1.
3D structure databases
ProteinModelPortal	B4S3H0.
ModBase	Search...
Protein-protein interaction databases
STRING	B4S3H0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6460446.
GenomeReviews	Gene locus Paes_1691 in contig CP001108_GR.
KEGG	paa:Paes_1691.
PATRIC	23043272. VBIProAes37017_1804.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG697237.
OMA	YSKRYDQ.
ProtClustDB	PRK14826.
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

B4S3H0_PROA2

Accession

Primary (citable) accession number: B4S3H0

Entry history

Integrated into UniProtKB/TrEMBL:	September 23, 2008
Last sequence update:	September 23, 2008
Last modified:	December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)