ID   DPNP_ORYSA              Reviewed;         358 AA.
AC   P0C5A3; Q40639;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE            EC=3.1.3.7;
DE   AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
DE   AltName: Full=DPNPase;
OS   Oryza sativa (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4530;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tallahamsa;
RX   PubMed=7493934; DOI=10.1074/jbc.270.49.29105;
RA   Peng Z., Verma D.P.S.;
RT   "A rice HAL2-like gene encodes a Ca(2+)-sensitive 3'(2'),5'-
RT   diphosphonucleoside 3'(2')-phosphohydrolase and complements yeast met22 and
RT   Escherichia coli cysQ mutations.";
RL   J. Biol. Chem. 270:29105-29110(1995).
CC   -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to
CC       adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC       5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-
CC       activation pathway by converting PAPS to APS.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Inhibited by Ca(2+), Li(+), and Na(+) and
CC       activated by K(+).
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; U33283; AAC49121.1; -; mRNA.
DR   PIR; T03305; T03305.
DR   AlphaFoldDB; P0C5A3; -.
DR   SMR; P0C5A3; -.
DR   BRENDA; 3.1.3.7; 4460.
DR   ExpressionAtlas; P0C5A3; baseline and differential.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR   InterPro; IPR006239; Bisphos_HAL2.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..358
FT                   /note="3'(2'),5'-bisphosphate nucleotidase"
FT                   /id="PRO_0000296248"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  37480 MW;  EFE813C18BEDB5FD CRC64;
     MSQAAGNPYA AELAAAKKAV TLAARLCQAV QKDILQSGVQ SKADQSPVTV ADYGSQILVS
     LVLKMEAPAS SSFSMVAEED SEELRKEGAE EILENITELV NETIVDDGTY SIYFSKEGIL
     SAIDDGKSEG GPSGRHWVLD PIDGTKGFLR GDQYAIALAL LDEGKVVLGV LACPNLSLGS
     IGNLNGGSSG DQVGALFSAT IGCGAEVESL QGSPAQKISV CSIDNPVEAS FFESYEGAHS
     LRDLTGSIAE KLGVQAPPVR IDSQAKYGAL ARGDGAIYLR FPHKGYREKI WDHAAGSIVV
     TEAGGLVTDA SGNDLDFSKG RFLDLDTGII ATNKQLMPSL LKAVQDAIKE QNQAASPL