Q117E1 (Q117E1_TRIEI) 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:

Tery_1005

Organism

Trichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP] EMBL ABG50383.1

Taxonomic identifier

203124 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriales › Trichodesmium

Protein attributes

Sequence length	205 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	18 – 23	6	Substrate binding By similarity HAMAP MF_01405
	Region	77 – 78	2	Substrate binding By similarity HAMAP MF_01405
Sites
	Metal binding	48	1	Magnesium or manganese By similarity HAMAP MF_01405
	Metal binding	77	1	Magnesium or manganese By similarity HAMAP MF_01405
	Binding site	159	1	Substrate By similarity HAMAP MF_01405
	Binding site	179	1	Substrate By similarity HAMAP MF_01405
	Binding site	185	1	Substrate By similarity HAMAP MF_01405

Sequences

	Sequence		Length	Mass (Da)
	Q117E1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: BAEB6617F7C93812	FASTA	205	22,632
	10 20 30 40 50 60 MKNFTPLKTT PRLLVVATGN LGKVVEMQEY MADLNLQLEL KPKDLEIEET GKTFLANACL 70 80 90 100 110 120 KASEVAKVTE KWAIADDSGL AVDALDGKPG IYSARYAPTV AEQIERVLRE LKDSQNRQAK 130 140 150 160 170 180 FVCALVIARP DGTIALKAEG ICYGEILYST RGNGGFGYDP IFYVPSEKKT FAEMSPETKR 190 200 SLSHRGKAFQ ILLPQIKEIF AIESV

References

[1]

"Complete sequence of Trichodesmium erythraeum IMS101." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IMS101.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000393 Genomic DNA. Translation: ABG50383.1.
RefSeq	YP_720856.1. NC_008312.1.
3D structure databases
ProteinModelPortal	Q117E1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q117E1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4245532.
GenomeReviews	Gene locus Tery_1005 in contig CP000393_GR.
KEGG	ter:Tery_1005.
NMPDR	fig|203124.1.peg.3732.
PATRIC	23985592. VBITriEry99848_1235.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0127.
HOGENOM	HBG697237.
OMA	GEAHNDA.
PhylomeDB	Q117E1.
Enzyme and pathway databases
BioCyc	TERY203124:TERY_1005-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

Q117E1_TRIEI

Accession

Primary (citable) accession number: Q117E1

Entry history

Integrated into UniProtKB/TrEMBL:	August 22, 2006
Last sequence update:	August 22, 2006
Last modified:	December 14, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)