Reviewed, UniProtKB/Swiss-Prot Q27895 (NTP2_TOXGO)

Names and origin

Protein names

Recommended name:
    Nucleoside-triphosphatase 2
    EC=3.6.1.15
Alternative name(s):
    NTPase-II
    Nucleoside-triphosphatase II
    Nucleoside triphosphate hydrolase 2

Gene names

Name:

NTP1

Organism

Toxoplasma gondii

Taxonomic identifier

5811 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Coccidia › Eucoccidiorida › Eimeriorina › Sarcocystidae › Toxoplasma

Protein attributes

Sequence length	628 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite. NTPAse-II has a specific activity 4.5-fold lower than NTPAse-I in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate versus diphosphate substrates. While NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate, NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate for ATP).
Catalytic activity	NTP + H2O = NDP + phosphate.
Subunit structure	Homotetramer.
Subcellular location	Secreted. Parasitophorous vacuole. Note: Found in host cell parasitophorous vacuole.
Sequence similarities	Belongs to the GDA1/CD39 NTPase family.

Ontologies

Keywords
Cellular component	Secreted Vacuole
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	parasitophorous vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell vacuole Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleoside-triphosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25
	Chain	26 – 628	603	Nucleoside-triphosphatase 2		PRO_0000019912
Amino acid modifications
	Glycosylation	432	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	6	1	Y → H in strain: Beverley.
	Natural variant	91	1	K → R in strain: Beverley.
	Natural variant	101	1	Q → R in strain: Beverley.
Experimental info
	Sequence conflict	334	1	G → R in AAA30143. Ref.3
	Sequence conflict	370	1	V → L Ref.3
	Sequence conflict	372	1	V → L Ref.3
	Sequence conflict	399	1	H → N in AAA30143. Ref.3
	Sequence conflict	437	1	E → K in AAA30143. Ref.3
	Sequence conflict	488 – 489	2	FI → IV Ref.3
	Sequence conflict	492 – 494	3	REM → GGS Ref.3
	Sequence conflict	497	1	S → A Ref.3
	Sequence conflict	499	1	D → N Ref.3
	Sequence conflict	523	1	R → G in AAA30143. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q27895-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: DE943DFDAC641159	FASTA	628	69,585
	10 20 30 40 50 60 MWLPVYVPLL LVFGVSLSLP HGSLGTDSSS LRGVDADTEK RINVGKTHLQ TLRNLETRCH 70 80 90 100 110 120 DSLQALVVID AGSSSTRTNV FLAKTRSCPN KGRSIDPDSI QLIREGKRFT GLRVVLEEWL 130 140 150 160 170 180 DTYAGKDWES RPVDARLLFQ YVPQMHEGAK KLMQLLEEDT VAILDSQLNE EQKVQVKALG 190 200 210 220 230 240 IPVMLCSTAG VRDFHEWYRD ALFVLLRHLI NNPSPAHGYK FFTNPFWTRP ITGAEEGLFA 250 260 270 280 290 300 FITLNHLSRR LGEDPARCMI DEYGVKHCRN DLAGVVEVGG ASAQIVFPLQ EGTVLPSSVR 310 320 330 340 350 360 AVNLQRERLL PERYPSADVV SVSFMQLGMA SSAGLFLKEL CSNDEFLQGG ICSNPCLFKG 370 380 390 400 410 420 FQQSCSAGEV EVRPDGSASV NEDVRKNRLK PLATYCSVHN PEISFKVTNE MQCRENSIDP 430 440 450 460 470 480 TKPLAERMKI ENCSIIEGTG NFDKCVSQVE SILVAPKLPL PANIEAASSG FESVDQVFRF 490 500 510 520 530 540 ASSTAPMFIT GREMLASIDT LKDHRLLRSD FSGDVEELAE AAREFCSSEV IIRTDGPVIQ 550 560 570 580 590 600 LPNARGEQKL NSLNFDLCKT MALTVSLLRH MAAGENQPSF IKWEKSIAGP DGKPLADLGW 610 620 QVGVILHHVL FTEEWGRTAY EAGYSHNL

References

[1]	"Biochemical and molecular characterization of nucleoside triphosphate hydrolase isozymes from the parasitic protozoan Toxoplasma gondii." Asai T., Miura S., Sibley L.D., Okabayashi H., Takeuchi T. J. Biol. Chem. 270:11391-11397(1995) [PubMed: 7744775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION. Strain: Beverley and RH.
[2]	"Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii." Bermudes D., Peck K.R., Afifi M.A., Beckers C.J.M., Joiner K.A. J. Biol. Chem. 269:29252-29260(1994) [PubMed: 7961894] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: RH.
[3]	"Cloning, expression and nucleotide sequence of the gene fragment encoding an antigenic portion of the nucleoside triphosphate hydrolase of Toxoplasma gondii." Johnson A.M., Illana S., McDonald P.J., Asai T. Gene 85:215-220(1989) [PubMed: 2482826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-523. Strain: RH.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L39077 mRNA. Translation: AAC41569.1. L39079 mRNA. Translation: AAC41570.1. U96965 Genomic DNA. Translation: AAC80187.1. M33472 Genomic DNA. Translation: AAA30143.1.
PIR	A55421.
3D structure databases
SMR	Q27895. Positions 62-610.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.6.1.15. 262552.
Family and domain databases
InterPro	IPR000407. GDA1_CD39_NTPase. IPR017227. NTPase_alveloata. [Graphical view]
PANTHER	PTHR11782. GDA1_CD39_NTPase. 1 hit.
Pfam	PF01150. GDA1_CD39. 1 hit. [Graphical view]
PIRSF	PIRSF037506. NTPase. 1 hit.
PROSITE	PS01238. GDA1_CD39_NTPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NTP2_TOXGO

Accession

Primary (citable) accession number: Q27895
Secondary accession number(s): Q27798, Q27801

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 19, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)