APS1_SCHPO
ID APS1_SCHPO Reviewed; 210 AA.
AC Q09790;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase aps1;
DE EC=3.6.1.52 {ECO:0000269|PubMed:10419486};
DE AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase;
DE Short=Ap6A hydrolase;
DE AltName: Full=Diadenosine hexaphosphate hydrolase (ADP-forming);
DE EC=3.6.1.-;
GN Name=aps1; ORFNames=SPAC13G6.14, SPAC24B11.03;
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], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10090752; DOI=10.1021/bi982951j;
RA Ingram S.W., Stratemann S.A., Barnes L.D.;
RT "Schizosaccharomyces pombe Aps1, a diadenosine 5',5'''-P1, P6-hexaphosphate
RT hydrolase that is a member of the nudix (MutT) family of hydrolases:
RT cloning of the gene and characterization of the purified enzyme.";
RL Biochemistry 38:3649-3655(1999).
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).
RN [3]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10419486; DOI=10.1074/jbc.274.31.21735;
RA Safrany S.T., Ingram S.W., Cartwright J.L., Falck J.R., McLennan A.G.,
RA Barnes L.D., Shears S.B.;
RT "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe
RT and Saccharomyces cerevisiae are homologues of the human diphosphoinositol
RT polyphosphate phosphohydrolase. Overlapping substrate specificities in a
RT MutT-type protein.";
RL J. Biol. Chem. 274:21735-21740(1999).
RN [4]
RP MUTAGENESIS OF GLU-93.
RX PubMed=12387729; DOI=10.1042/bj20020733;
RA Ingram S.W., Safrany S.T., Barnes L.D.;
RT "Disruption and overexpression of the Schizosaccharomyces pombe aps1 gene,
RT and effects on growth rate, morphology and intracellular diadenosine
RT 5',5''-P1,P5-pentaphosphate and diphosphoinositol polyphosphate
RT concentrations.";
RL Biochem. J. 369:519-528(2003).
CC -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-
CC InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4
CC (bisdiphosphoinositol tetrakisphosphate). Also catalyzes the hydrolysis
CC of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred
CC substrates. The major reaction products are ADP and p4a from Ap6A and
CC ADP and ATP from Ap5A. {ECO:0000269|PubMed:10090752}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC polyphosphate + phosphate.; EC=3.6.1.52;
CC Evidence={ECO:0000269|PubMed:10419486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = adenosine 5'-
CC tetraphosphate + ADP + 2 H(+); Xref=Rhea:RHEA:51724,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58450,
CC ChEBI:CHEBI:63740, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10090752};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = ADP + ATP +
CC 2 H(+); Xref=Rhea:RHEA:30527, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:62041, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10090752};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 nM for PP-InsP5 {ECO:0000269|PubMed:10419486};
CC KM=19 uM for Ap6A {ECO:0000269|PubMed:10090752};
CC KM=22 uM for Ap5A {ECO:0000269|PubMed:10090752};
CC Note=kcat is 2 sec(-1) for Ap6A. kcat is 1.7 sec(-1) for Ap5A.;
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:10090752};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10090752}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
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; AF125215; AAD20015.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91107.1; -; Genomic_DNA.
DR PIR; S62443; S62443.
DR RefSeq; NP_592840.1; NM_001018241.2.
DR AlphaFoldDB; Q09790; -.
DR BMRB; Q09790; -.
DR SMR; Q09790; -.
DR BioGRID; 279334; 31.
DR STRING; 4896.SPAC13G6.14.1; -.
DR iPTMnet; Q09790; -.
DR MaxQB; Q09790; -.
DR PaxDb; Q09790; -.
DR PRIDE; Q09790; -.
DR EnsemblFungi; SPAC13G6.14.1; SPAC13G6.14.1:pep; SPAC13G6.14.
DR GeneID; 2542890; -.
DR KEGG; spo:SPAC13G6.14; -.
DR PomBase; SPAC13G6.14; aps1.
DR VEuPathDB; FungiDB:SPAC13G6.14; -.
DR eggNOG; KOG2839; Eukaryota.
DR HOGENOM; CLU_037162_5_3_1; -.
DR InParanoid; Q09790; -.
DR OMA; EDQWPEM; -.
DR PhylomeDB; Q09790; -.
DR BRENDA; 3.6.1.B11; 5613.
DR Reactome; R-SPO-1855167; Synthesis of pyrophosphates in the cytosol.
DR SABIO-RK; Q09790; -.
DR PRO; PR:Q09790; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0034431; F:bis(5'-adenosyl)-hexaphosphatase activity; IDA:PomBase.
DR GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase activity; IDA:PomBase.
DR GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000298; F:endopolyphosphatase activity; IBA:GO_Central.
DR GO; GO:0052842; F:inositol diphosphate pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901911; P:adenosine 5'-(hexahydrogen pentaphosphate) catabolic process; IDA:PomBase.
DR GO; GO:1901909; P:diadenosine hexaphosphate catabolic process; IDA:PomBase.
DR GO; GO:1901907; P:diadenosine pentaphosphate catabolic process; IDA:PomBase.
DR GO; GO:1901906; P:diadenosine pentaphosphate metabolic process; IMP:PomBase.
DR GO; GO:0015959; P:diadenosine polyphosphate metabolic process; IDA:PomBase.
DR GO; GO:0071543; P:diphosphoinositol polyphosphate metabolic process; IMP:PomBase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..210
FT /note="Diphosphoinositol polyphosphate phosphohydrolase
FT aps1"
FT /id="PRO_0000057068"
FT DOMAIN 40..203
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 74..95
FT /note="Nudix box"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 93
FT /note="E->Q: Does not affect intracellular Ap5A level, but
FT strongly reduces DIPP enzyme activity."
FT /evidence="ECO:0000269|PubMed:12387729"
SQ SEQUENCE 210 AA; 23724 MW; 492F7BF9563A1C98 CRC64;
MLENNGSVIL MEPDHLRTAV NRSMTSREGR TKNRFNPITG ARLAAGVVAL SADKRKVLLV
SSAKKHPSWV VPKGGWEADE SVQQAALREG WEEGGLVGHI TRSLGSFKDK RPTDTIDRRK
KYLKQLMSKS SGNDVSTNTE LGAEAEKLLL PPRAECEFFE VIVERLEDNY PEMRKRRRKW
MSYQEAKEAL TSRKDILAAL EKSSIIKEEN
