NTP2_TOXGO
ID NTP2_TOXGO Reviewed; 628 AA.
AC Q27895; Q27798; Q27801;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Nucleoside-triphosphatase 2;
DE EC=3.6.1.15;
DE AltName: Full=NTPase-II;
DE AltName: Full=Nucleoside triphosphate hydrolase 2;
DE AltName: Full=Nucleoside-triphosphatase II;
DE Flags: Precursor;
GN Name=NTP1;
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=Beverley, and 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 [MRNA].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-523.
RC STRAIN=RH;
RX PubMed=2482826; DOI=10.1016/0378-1119(89)90484-8;
RA Johnson A.M., Illana S., McDonald P.J., Asai T.;
RT "Cloning, expression and nucleotide sequence of the gene fragment encoding
RT an antigenic portion of the nucleoside triphosphate hydrolase of Toxoplasma
RT gondii.";
RL Gene 85:215-220(1989).
CC -!- FUNCTION: May perform an important processing step in the conversion of
CC high energy nucleotides prior to uptake by the parasite. NTPAse-II has
CC a specific activity 4.5-fold lower than NTPAse-I 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; L39077; AAC41569.1; -; mRNA.
DR EMBL; L39079; AAC41570.1; -; mRNA.
DR EMBL; U96965; AAC80187.1; -; Genomic_DNA.
DR EMBL; M33472; AAA30143.1; -; Genomic_DNA.
DR PIR; A55421; A55421.
DR PDB; 4A5B; X-ray; 2.48 A; A/B=26-628.
DR PDB; 4JEP; X-ray; 3.10 A; A/B=26-628.
DR PDB; 4KH4; X-ray; 3.00 A; A/B=26-628.
DR PDB; 4KH5; X-ray; 3.00 A; A/B=26-628.
DR PDB; 4KH6; X-ray; 2.40 A; A/B=26-628.
DR PDBsum; 4A5B; -.
DR PDBsum; 4JEP; -.
DR PDBsum; 4KH4; -.
DR PDBsum; 4KH5; -.
DR PDBsum; 4KH6; -.
DR AlphaFoldDB; Q27895; -.
DR SMR; Q27895; -.
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_277270; -.
DR VEuPathDB; ToxoDB:TGME49_278878; -.
DR VEuPathDB; ToxoDB:TGP89_277720; -.
DR VEuPathDB; ToxoDB:TGPRC2_358870; -.
DR VEuPathDB; ToxoDB:TGRH88_066160; -.
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 BRENDA; 3.6.1.5; 6411.
DR BRENDA; 3.6.1.6; 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 2"
FT /id="PRO_0000019912"
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 VARIANT 6
FT /note="Y -> H (in strain: Beverley)"
FT VARIANT 91
FT /note="K -> R (in strain: Beverley)"
FT VARIANT 101
FT /note="Q -> R (in strain: Beverley)"
FT CONFLICT 334
FT /note="G -> R (in Ref. 3; AAA30143)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="V -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="V -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="H -> N (in Ref. 3; AAA30143)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="E -> K (in Ref. 3; AAA30143)"
FT /evidence="ECO:0000305"
FT CONFLICT 488..489
FT /note="FI -> IV (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..494
FT /note="REM -> GGS (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="S -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="D -> N (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="R -> G (in Ref. 3; AAA30143)"
FT /evidence="ECO:0000305"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 38..55
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 76..88
FT /evidence="ECO:0007829|PDB:4KH6"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:4KH6"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 142..167
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4A5B"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4JEP"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4KH4"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:4KH4"
FT TURN 304..308
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:4JEP"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:4KH6"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 390..395
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:4JEP"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:4KH6"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:4KH4"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 464..468
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 492..503
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 515..526
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:4KH5"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:4KH6"
FT TURN 552..556
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 557..572
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:4KH6"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:4KH4"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:4KH4"
FT HELIX 600..609
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 612..619
FT /evidence="ECO:0007829|PDB:4KH6"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:4KH6"
FT HELIX 624..627
FT /evidence="ECO:0007829|PDB:4KH6"
SQ SEQUENCE 628 AA; 69585 MW; DE943DFDAC641159 CRC64;
MWLPVYVPLL LVFGVSLSLP HGSLGTDSSS LRGVDADTEK RINVGKTHLQ TLRNLETRCH
DSLQALVVID AGSSSTRTNV FLAKTRSCPN KGRSIDPDSI QLIREGKRFT GLRVVLEEWL
DTYAGKDWES RPVDARLLFQ YVPQMHEGAK KLMQLLEEDT VAILDSQLNE EQKVQVKALG
IPVMLCSTAG VRDFHEWYRD ALFVLLRHLI NNPSPAHGYK FFTNPFWTRP ITGAEEGLFA
FITLNHLSRR LGEDPARCMI DEYGVKHCRN DLAGVVEVGG ASAQIVFPLQ EGTVLPSSVR
AVNLQRERLL PERYPSADVV SVSFMQLGMA SSAGLFLKEL CSNDEFLQGG ICSNPCLFKG
FQQSCSAGEV EVRPDGSASV NEDVRKNRLK PLATYCSVHN PEISFKVTNE MQCRENSIDP
TKPLAERMKI ENCSIIEGTG NFDKCVSQVE SILVAPKLPL PANIEAASSG FESVDQVFRF
ASSTAPMFIT GREMLASIDT LKDHRLLRSD FSGDVEELAE AAREFCSSEV IIRTDGPVIQ
LPNARGEQKL NSLNFDLCKT MALTVSLLRH MAAGENQPSF IKWEKSIAGP DGKPLADLGW
QVGVILHHVL FTEEWGRTAY EAGYSHNL
