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Database: UniProt
Entry: A0A1S3SAB6_SALSA
LinkDB: A0A1S3SAB6_SALSA
Original site: A0A1S3SAB6_SALSA 
ID   A0A1S3SAB6_SALSA        Unreviewed;       432 AA.
AC   A0A1S3SAB6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=LOC106608092 {ECO:0000313|RefSeq:XP_014061274.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014061274.1};
RN   [1] {ECO:0000313|RefSeq:XP_014061274.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014061274.1};
RG   RefSeq;
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   RefSeq; XP_014061274.1; XM_014205799.1.
DR   AlphaFoldDB; A0A1S3SAB6; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa06.
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:UP000087266};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..432
FT                   /note="nucleoside diphosphate phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010313880"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         202..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   432 AA;  47840 MW;  402731F7C53FEE98 CRC64;
     MSLQAPLLPA VVLSLVLVVL ALTGLSHAQL QPKASVLDFS ASLGNLLPSL SRPANSSRIF
     YGVMFDAGST GTRIHVYTFI QKDPEELPVL DNEMFHSIKP GLSAYADIPE MGGYTVRQLL
     KVAKKTVPQL DWKRTPLVLK ATAGLRLLPP EKAQALLEQV QDVFDESPFF VPDDSVSIMD
     GTNEGHLYAD TRETVGILDL GGGSTQITFL PKFKKTIVSS PADYIARFDM FNSAYELYTH
     SYLGNGLMAA RLAALGALGA EGLEWRVFKS SCLPKKFREE WRFGGLTYTV SGIPDGYAGY
     KLCYQEVLKV VKGIVHQPYE LKNTSVLYAF SYYFDRAVDA GLIDGTQGGM LEVRDFKKGA
     KEGENEVCNK MSKYRPVSPF LCMDMTYITC LLKDGFGFKE NTVLQLTKKV NNVETSWALG
     AMFKHFQNLK IH
//
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