NTP1_TOXGO
ID NTP1_TOXGO Reviewed; 628 AA.
AC Q27893;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Nucleoside-triphosphatase 1;
DE EC=3.6.1.15;
DE AltName: Full=NTPase-I;
DE AltName: Full=Nucleoside triphosphate hydrolase 1;
DE AltName: Full=Nucleoside-triphosphatase I;
DE Flags: Precursor;
GN Name=NTP3;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC STRAIN=RH;
RX PubMed=7744775; DOI=10.1074/jbc.270.19.11391;
RA Asai T., Miura S., Sibley L.D., Okabayashi H., Takeuchi T.;
RT "Biochemical and molecular characterization of nucleoside triphosphate
RT hydrolase isozymes from the parasitic protozoan Toxoplasma gondii.";
RL J. Biol. Chem. 270:11391-11397(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RH;
RX PubMed=7961894; DOI=10.1016/s0021-9258(19)62038-7;
RA Bermudes D., Peck K.R., Afifi M.A., Beckers C.J.M., Joiner K.A.;
RT "Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms
RT secreted into the parasitophorous vacuole of Toxoplasma gondii.";
RL J. Biol. Chem. 269:29252-29260(1994).
CC -!- FUNCTION: May perform an important processing step in the conversion of
CC high energy nucleotides prior to uptake by the parasite and may
CC contribute to intracellular survival and virulence. NTPAse-I has a
CC specific activity 4.5-fold higher than NTPAse-II in hydrolysis of ATP.
CC The primary difference between these isozymes lies in their ability to
CC hydrolyze nucleoside triphosphate versus diphosphate substrates. While
CC NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate,
CC NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate
CC for ATP).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted. Parasitophorous vacuole. Note=Found in
CC host cell parasitophorous vacuole.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; L39078; AAA89203.1; -; mRNA.
DR EMBL; U96965; AAC80188.1; -; Genomic_DNA.
DR PDB; 4A57; X-ray; 2.00 A; A/B/C/D=26-628.
DR PDB; 4A59; X-ray; 2.20 A; A/B/C/D=26-628.
DR PDB; 4A5A; X-ray; 2.85 A; A/B/C/D=26-628.
DR PDBsum; 4A57; -.
DR PDBsum; 4A59; -.
DR PDBsum; 4A5A; -.
DR AlphaFoldDB; Q27893; -.
DR SMR; Q27893; -.
DR VEuPathDB; ToxoDB:TGARI_371290; -.
DR VEuPathDB; ToxoDB:TGCAST_358870; -.
DR VEuPathDB; ToxoDB:TGCOUG_395210; -.
DR VEuPathDB; ToxoDB:TGDOM2_278878; -.
DR VEuPathDB; ToxoDB:TGDOM2_400630; -.
DR VEuPathDB; ToxoDB:TGFOU_278882; -.
DR VEuPathDB; ToxoDB:TGGT1_277270; -.
DR VEuPathDB; ToxoDB:TGGT1_408820; -.
DR VEuPathDB; ToxoDB:TGMAS_363610; -.
DR VEuPathDB; ToxoDB:TGMAS_364050; -.
DR VEuPathDB; ToxoDB:TGME49_278882; -.
DR VEuPathDB; ToxoDB:TGP89_277720; -.
DR VEuPathDB; ToxoDB:TGPRC2_358870; -.
DR VEuPathDB; ToxoDB:TGRH88_066180; -.
DR VEuPathDB; ToxoDB:TGRUB_278882; -.
DR VEuPathDB; ToxoDB:TGVAND_278882; -.
DR VEuPathDB; ToxoDB:TGVEG_277270; -.
DR VEuPathDB; ToxoDB:TGVEG_278878; -.
DR BRENDA; 3.6.1.15; 6411.
DR GO; GO:0020003; C:symbiont-containing vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR InterPro; IPR017227; NTPase_alveloata.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PIRSF; PIRSF037506; NTPase; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..25
FT CHAIN 26..628
FT /note="Nucleoside-triphosphatase 1"
FT /id="PRO_0000019911"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 38..57
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 76..88
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 142..167
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:4A5A"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4A59"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 304..308
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 390..395
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 464..468
FT /evidence="ECO:0007829|PDB:4A5A"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 492..503
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 515..526
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 552..556
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 557..573
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:4A57"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:4A5A"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 601..609
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 612..619
FT /evidence="ECO:0007829|PDB:4A57"
FT TURN 620..623
FT /evidence="ECO:0007829|PDB:4A57"
FT HELIX 624..627
FT /evidence="ECO:0007829|PDB:4A57"
SQ SEQUENCE 628 AA; 69159 MW; 95867B943ADD3E6F CRC64;
MWLPVYVPLL LVFGVSLSLP QGSLGTDSSS LRGVDADTEK RINVGKKHLQ TLRNLETRCH
DSLQALVVID AGSSSTRTNV FLAKTRSCPN KGRSIDPDSI QLIGAGKRFA GLRVVLEEWL
DTYAGKDWES RPVDARLLFQ YVPQMHEGAK KLMQLLEEDT VAILDSQLNE KQKVQVKALG
IPVMLCSTAG VRDFHEWYRD ALFVLLRHLI NNPSPAHGYK FFTNPFWTRP ITGAEEGLFA
FITLNHLSRR LGEDPARCMI DEYGVKQCRN DLAGVVEVGG ASAQIVFPLQ EGTVLPSSVR
AVNLQRERLL PERYPSADVV SVSFMQLGMA SSAGLFLKEL CSNDEFLQGG ICSNPCLFKG
FQQSCSAGEV EVRPDGSASV NEDVRKNRLK PLATYCSVNN PEISFKVTNE MQCRENSIDP
TKPLAERMKI ENCSIIKGTG NFDKCVSQVE SILVAPKLPL PANIEAASSG FESVDQVFRF
ASSTAPMIVT GGGMLAAINT LKDHRLLRSD FSGDVEELAE AAREFCSSEV IIRTDGPVIQ
LPNARGEQKL NSLNFDLCKT MALTVSLLRH MAAGENQPSF IKWEKSIAGP DGKPLADLGW
QVGVILHHVL FTEEWGRNAY EAGYSHNL
