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Database: UniProt
Entry: A0A3Q0RKI5_AMPCI
LinkDB: A0A3Q0RKI5_AMPCI
Original site: A0A3Q0RKI5_AMPCI 
ID   A0A3Q0RKI5_AMPCI        Unreviewed;       379 AA.
AC   A0A3Q0RKI5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=nucleoside diphosphate phosphatase {ECO:0000256|ARBA:ARBA00038863};
DE            EC=3.6.1.6 {ECO:0000256|ARBA:ARBA00038863};
DE   AltName: Full=Guanosine-diphosphatase ENTPD5 {ECO:0000256|ARBA:ARBA00042111};
DE   AltName: Full=Uridine-diphosphatase ENTPD5 {ECO:0000256|ARBA:ARBA00042507};
GN   Name=ENTPD5 {ECO:0000313|Ensembl:ENSACIP00000009235.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000009235.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000009235.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036163};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000256|ARBA:ARBA00036163};
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; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036856};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC         Evidence={ECO:0000256|ARBA:ARBA00036856};
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; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC         Evidence={ECO:0000256|ARBA:ARBA00036354};
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; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036844};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC         Evidence={ECO:0000256|ARBA:ARBA00036844};
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; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036381};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC         Evidence={ECO:0000256|ARBA:ARBA00036381};
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; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00035811};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC         Evidence={ECO:0000256|ARBA:ARBA00035811};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
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DR   AlphaFoldDB; A0A3Q0RKI5; -.
DR   Ensembl; ENSACIT00000009511.1; ENSACIP00000009235.1; ENSACIG00000007138.1.
DR   GeneTree; ENSGT01100000263540; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0005576; C:extracellular region; 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:SF35; NUCLEOSIDE DIPHOSPHATE PHOSPHATASE ENTPD5; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   BINDING         172..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   379 AA;  42048 MW;  79F7394CE5DEC011 CRC64;
     REEFIFFGKL YLCGSSPVNT SRVFYGIMFD AGSTGTRIHI YKFIQKDPGK CLPVLVNEMY
     HAVKPGLSSY KDDPEEGGNT IRQLLKIAKK TVPEDDWRRT PVVLKATAGL RLLPEDKARA
     LLREVRHGFS LPSDSLTLSS LSSVMCSTCC LFAIGHLYSN TKRTVGILDL GGGSTQITFL
     PKSKKTIQSA PSNYIASFNL FDHTYQLYTH SYLGNGLFAA RYATVGALGA DGLDWKIFTS
     SCLPKKFRGN GTFSGTIYKV SGIPDGYAGY KLCYYEVMKV IKGIVHQPYE VRGSSVFYAF
     SYYFDKAVES GLIDGSRGGT VEVRDFKKRA KEVCNKMTKY GAINPFLCMD LTYITCLLKE
     GFGFKDSTVL HVSFGSWAN
//
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