UniProt: A0A087XJZ5

Database: UniProt
Entry: A0A087XJZ5_POEFO

LinkDB:  A0A087XJZ5_POEFO 
Original site:  A0A087XJZ5_POEFO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (4)   
   EMBL (4)   
Protein domain (3)   
   InterPro (1)   
   Pfam (1)   
   PROSITE (1)   
All databases (17)   

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ID   A0A087XJZ5_POEFO        Unreviewed;       497 AA.
AC   A0A087XJZ5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 {ECO:0000256|ARBA:ARBA00039600};
DE            EC=3.6.1.5 {ECO:0000256|ARBA:ARBA00012148};
DE   AltName: Full=ATP diphosphohydrolase {ECO:0000256|ARBA:ARBA00044314};
DE   AltName: Full=Ecto-ATP diphosphohydrolase 1 {ECO:0000256|ARBA:ARBA00042147};
DE   AltName: Full=Ecto-apyrase {ECO:0000256|ARBA:ARBA00042196};
DE   AltName: Full=Lymphoid cell activation antigen {ECO:0000256|ARBA:ARBA00041335};
DE   AltName: Full=Nucleoside triphosphate diphosphohydrolase 1 {ECO:0000256|ARBA:ARBA00044280};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000006098.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000006098.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + ITP = 2 H(+) + IMP + 2 phosphate;
CC         Xref=Rhea:RHEA:77735, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402;
CC         Evidence={ECO:0000256|ARBA:ARBA00043682};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736;
CC         Evidence={ECO:0000256|ARBA:ARBA00043682};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + UTP = 2 H(+) + 2 phosphate + UMP;
CC         Xref=Rhea:RHEA:64896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865;
CC         Evidence={ECO:0000256|ARBA:ARBA00043678};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897;
CC         Evidence={ECO:0000256|ARBA:ARBA00043678};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036139};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000256|ARBA:ARBA00036139};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 H2O = AMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:20988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00043702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989;
CC         Evidence={ECO:0000256|ARBA:ARBA00043702};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00034440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00034440};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58069, ChEBI:CHEBI:60377;
CC         Evidence={ECO:0000256|ARBA:ARBA00043676};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC         Evidence={ECO:0000256|ARBA:ARBA00043676};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + 2 H2O = CMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:64908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:60377;
CC         Evidence={ECO:0000256|ARBA:ARBA00043680};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64909;
CC         Evidence={ECO:0000256|ARBA:ARBA00043680};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC         Evidence={ECO:0000256|ARBA:ARBA00043776};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC         Evidence={ECO:0000256|ARBA:ARBA00043776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00043654};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC         Evidence={ECO:0000256|ARBA:ARBA00043654};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + 2 H2O = GMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:64904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115;
CC         Evidence={ECO:0000256|ARBA:ARBA00043766};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905;
CC         Evidence={ECO:0000256|ARBA:ARBA00043766};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58280;
CC         Evidence={ECO:0000256|ARBA:ARBA00043688};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC         Evidence={ECO:0000256|ARBA:ARBA00043688};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58280, ChEBI:CHEBI:61402;
CC         Evidence={ECO:0000256|ARBA:ARBA00043752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331;
CC         Evidence={ECO:0000256|ARBA:ARBA00043752};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000256|ARBA:ARBA00043716};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC         Evidence={ECO:0000256|ARBA:ARBA00043716};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000256|ARBA:ARBA00043661};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901;
CC         Evidence={ECO:0000256|ARBA:ARBA00043661};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:58043;
CC         Evidence={ECO:0000256|ARBA:ARBA00043714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC         Evidence={ECO:0000256|ARBA:ARBA00043714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC         5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00043753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796;
CC         Evidence={ECO:0000256|ARBA:ARBA00043753};
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00043686};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC         Evidence={ECO:0000256|ARBA:ARBA00043686};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR   EMBL; AYCK01009257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01009258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01009259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01009260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007562454.1; XM_007562392.2.
DR   AlphaFoldDB; A0A087XJZ5; -.
DR   STRING; 48698.ENSPFOP00000006098; -.
DR   Ensembl; ENSPFOT00000006108.2; ENSPFOP00000006098.2; ENSPFOG00000006089.2.
DR   GeneID; 103145114; -.
DR   KEGG; pfor:103145114; -.
DR   CTD; 953; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   GeneTree; ENSGT01100000263542; -.
DR   OMA; YWVREVE; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF32; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 1; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU003833};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         203..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   497 AA;  55607 MW;  6C9EB0BE46C9EBF5 CRC64;
     MSAQREMKEK NPWHTPLTII ITVIGVIAIV ALVTVAVLQN RPVPQKYKYG IVLDAGSSHT
     ALYIYEWPAE KDNNTGRVEQ KHSCKVKGKG ISSYAAEPEK AGMSLTECMR EAEMQVPSRR
     HQETPLYLGA TAGMRLLNIE NREASDKVFE AVEKALQGFP FSYQGARILS GQEEGAFGWV
     TVNYLDDRLK QGLETTGALD LGGASTQISF VPHEYDISES PSNSVAFRLY GNDYNLYTHS
     FLCYGKDQVL RMALAHQTRS GPVTMSDPCF HPGYSVTRNY NALYDSPCVS ERKPKEAPLN
     FTHTGVGNFF RCQEVVKTLF NFTSCKYSRC SFNGIFQPPL QGSFGAFSAY YFVMNFLNLT
     DSSIPLETVK ANLANYCGTP WNQIKQQHPE VKEKYLAEYC FSGTYIVTLL TEGYNFTKET
     FSKIKFIKEI KGSDAGWTLG YMLNLTNMIP AEAPDSPPLP HAGYVSIVTV IALLLFILFI
     LSLRPIWPKC SKKPQIV
//

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