ID G3PGK9_GASAC Unreviewed; 434 AA.
AC G3PGK9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:ENSGACP00000016733.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000016733.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000016733.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000016733.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G3PGK9; -.
DR Ensembl; ENSGACT00000016767.1; ENSGACP00000016733.1; ENSGACG00000012614.1.
DR GeneTree; ENSGT01100000263540; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000012614; Expressed in camera-type eye and 13 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..434
FT /note="nucleoside diphosphate phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003449745"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 205..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 434 AA; 47865 MW; 6BF9895086E37E77 CRC64;
MKLAGRLLLL LLLAVSGRSR VRLATSLLGL TDGFGSLLPK LSRPANHSRI FYAVMFDAGS
TGTRVHVYTF IQSGSEQLPI LDNEMFHSIK PGLSAYADSP ETAGHTVRTL LKVAKKTVPR
LEWKRCPLVL RATAGLRLLA EDKAQVLLQQ VQHVFDESPF LVPDDSVGVM NGTYEGLLAW
ISLNYLTGHL SAQTKNTVGI LDLGGGSTQI TFLPNQRKTI ESVPAADYVA RFGISNTSFE
LYTYSYLGNG LMAARLATLG ALGAEGTGLE WRVFRSSCLP KKFKGEWSFG ELTYRVSGDP
EGFAGYKLCY QEVLKAVKGI IHQPYKLEDS NVFYAFSYYF DRAVDAGLID GDHGGMLQVR
DFKKRAKEVC NEMSKSTPTS AFLCMDMTYI TCLLKDGFGF KESTVLKLTK KVNNVEASWA
LGAVLDHFHN LKIH
//
