DPNP_SCHPO
ID DPNP_SCHPO Reviewed; 353 AA.
AC O94505;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE EC=3.1.3.7 {ECO:0000269|PubMed:10850973};
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
DE AltName: Full=DPNPase;
DE AltName: Full=Halotolerance protein tol1;
DE AltName: Full=Target of lithium protein 1;
GN Name=tol1; ORFNames=SPCC1753.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=10850973; DOI=10.1128/jb.182.13.3619-3625.2000;
RA Miyamoto R., Sugiura R., Kamitani S., Yada T., Lu Y., Sio S.O., Asakura M.,
RA Matsuhisa A., Shuntoh H., Kuno T.;
RT "Tol1, a fission yeast phosphomonoesterase, is an in vivo target of
RT lithium, and its deletion leads to sulfite auxotrophy.";
RL J. Bacteriol. 182:3619-3625(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 {ECO:0000269|PubMed:10850973}.
CC -!- FUNCTION: Confers resistance to lithium. {ECO:0000269|PubMed:10850973}.
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 Evidence={ECO:0000269|PubMed:10850973};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10850973};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D86083; BAA96866.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA22778.1; -; Genomic_DNA.
DR PIR; T41127; T41127.
DR RefSeq; NP_588230.1; NM_001023220.2.
DR AlphaFoldDB; O94505; -.
DR SMR; O94505; -.
DR BioGRID; 275528; 21.
DR STRING; 4896.SPCC1753.04.1; -.
DR MaxQB; O94505; -.
DR PaxDb; O94505; -.
DR PRIDE; O94505; -.
DR EnsemblFungi; SPCC1753.04.1; SPCC1753.04.1:pep; SPCC1753.04.
DR GeneID; 2538954; -.
DR KEGG; spo:SPCC1753.04; -.
DR PomBase; SPCC1753.04; tol1.
DR VEuPathDB; FungiDB:SPCC1753.04; -.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_1_1_1; -.
DR InParanoid; O94505; -.
DR OMA; MSYQQER; -.
DR PhylomeDB; O94505; -.
DR PRO; PR:O94505; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:PomBase.
DR GO; GO:0052829; F:inositol-1,3,4-trisphosphate 1-phosphatase activity; IDA:PomBase.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IDA:PomBase.
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:0048015; P:phosphatidylinositol-mediated signaling; IC:PomBase.
DR GO; GO:0000103; P:sulfate assimilation; IMP:PomBase.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..353
FT /note="3'(2'),5'-bisphosphate nucleotidase"
FT /id="PRO_0000142536"
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 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 138..141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 353 AA; 38748 MW; F88CCAB21C653349 CRC64;
MSFDAEKQLA IAAVRRASYL TEKVFNQLIK EKSAAGALTK DDKSPVTIGD FGAQAIVISM
LKDAFPNDPI VGEEDSDFLR ENTQTCSRVW ELVQETIQHA TEYKELGQIK SAEEMMSIID
QGSYHGGRNG RMWTLDPIDG TKGFLRGAQY AICLALIENG KPVVSAIGCP NLPYDFNQPE
TSPKGIIMSA VRNHGCFQYS LHNEKLEPVQ VHMQDVQNTK DSKFCEGVEA GHSMQGTQEE
IAKYLGITRG PTKMDSQAKY ASLARGDGDI YLRLPTKMTF EEKIWDHAGG SLLVEEAGGV
VSDMFGKPLD FGVGRTLKNN NGVIAAYKGI FEKVIEATAA VTSKDPHFQK VAQ
