DPNP_DICDI
ID DPNP_DICDI Reviewed; 332 AA.
AC Q55F34;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
DE AltName: Full=Inositol polyphosphate 1-phosphatase;
DE Short=IPPase;
DE AltName: Full=Inositol-1,4-bisphosphate 1-phosphatase;
DE EC=3.1.3.57;
GN ORFNames=DDB_G0268652;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. Is also able to hydrolyze
CC inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (By
CC similarity). {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-
CC phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000004; EAL72915.1; -; Genomic_DNA.
DR RefSeq; XP_646836.1; XM_641744.1.
DR AlphaFoldDB; Q55F34; -.
DR SMR; Q55F34; -.
DR STRING; 44689.DDB0238884; -.
DR PaxDb; Q55F34; -.
DR PRIDE; Q55F34; -.
DR EnsemblProtists; EAL72915; EAL72915; DDB_G0268652.
DR GeneID; 8616518; -.
DR KEGG; ddi:DDB_G0268652; -.
DR dictyBase; DDB_G0268652; ippB.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_2_1_1; -.
DR InParanoid; Q55F34; -.
DR OMA; MSYQQER; -.
DR PhylomeDB; Q55F34; -.
DR PRO; PR:Q55F34; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
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 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Reference proteome.
FT CHAIN 1..332
FT /note="3'(2'),5'-bisphosphate nucleotidase"
FT /id="PRO_0000327519"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131..134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 36888 MW; 56F8D137C9244277 CRC64;
MSLCNLAKIR SVAIKAVEKA CIACLDIQKQ LISEDTINKK DQSPVTVGDY TVQALVINEL
LKGLDEEYPI IAEEDSKTLS SQKDVESKVL SFFNRYSNES FVESQLSSLL DKGNKKKDLN
SSNRWWTLDP IDGTLGFLRK DQYAVALALM EDNKPILGIL GCPNLPVSKG STEKGCIFVG
LKNKGSFMIK LSNLDQEEPI KVSNQSDPTK AIFTESFVSR GFGHELNQKI SNSMGVTAEP
LKIDSQCKYA MVARGDSDCY LRLTQLDYKE CIWDHAAGHI IVEEAGGIVT DFKKQQLDYS
KGFKLENNVG IVCSNKLLND SLFDSIKKSI QF
