ID   PPX1_YEAST              Reviewed;         397 AA.
AC   P38698; D3DLF0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 170.
DE   RecName: Full=Polyphosphatase {ECO:0000303|PubMed:7860598};
DE            Short=PolyPase {ECO:0000303|PubMed:7860598};
DE            EC=3.6.1.11 {ECO:0000269|PubMed:7860598};
DE   AltName: Full=Exopolyphosphatase {ECO:0000303|PubMed:17599355};
DE   AltName: Full=Metaphosphatase {ECO:0000305};
GN   Name=PPX1 {ECO:0000303|PubMed:7860598}; OrderedLocusNames=YHR201C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=S288c / SNY243;
RX   PubMed=7860598; DOI=10.1128/jb.177.4.898-906.1995;
RA   Wurst H., Shiba T., Kornberg A.;
RT   "The gene for a major exopolyphosphatase of Saccharomyces cerevisiae.";
RL   J. Bacteriol. 177:898-906(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=31175919; DOI=10.1016/j.biochi.2019.06.001;
RA   Andreeva N., Ledova L., Ryazanova L., Tomashevsky A., Kulakovskaya T.,
RA   Eldarov M.;
RT   "Ppn2 endopolyphosphatase overexpressed in Saccharomyces cerevisiae:
RT   Comparison with Ppn1, Ppx1, and Ddp1 polyphosphatases.";
RL   Biochimie 163:101-107(2019).
RN   [6] {ECO:0007744|PDB:2QB6, ECO:0007744|PDB:2QB7, ECO:0007744|PDB:2QB8}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATP; MAGNESIUM AND MANGANESE.
RX   PubMed=17599355; DOI=10.1016/j.jmb.2007.05.066;
RA   Ugochukwu E., Lovering A.L., Mather O.C., Young T.W., White S.A.;
RT   "The crystal structure of the cytosolic exopolyphosphatase from
RT   Saccharomyces cerevisiae reveals the basis for substrate specificity.";
RL   J. Mol. Biol. 371:1007-1021(2007).
CC   -!- FUNCTION: Polyphosphatase (polyPase) involved in the degradation of
CC       inorganic polyphosphates (polyP) that is able to degrade a range of
CC       chains from three to several hundreds of residues in a highly
CC       processive manner (PubMed:7860598). Exclusively shows
CC       exopolyphosphatase activity, cleaving inside the polyP chain
CC       (PubMed:31175919). {ECO:0000269|PubMed:31175919,
CC       ECO:0000269|PubMed:7860598}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + H2O = [phosphate](n-1) + phosphate + H(+);
CC         Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC         ChEBI:CHEBI:43474; EC=3.6.1.11;
CC         Evidence={ECO:0000269|PubMed:31175919, ECO:0000269|PubMed:7860598};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21529;
CC         Evidence={ECO:0000269|PubMed:31175919};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:17599355};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:17599355, ECO:0000269|PubMed:31175919};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=240 umol/min/mg enzyme with polyP(208) as substrate for the
CC         exopolyphosphatase reaction {ECO:0000269|PubMed:31175919};
CC   -!- MISCELLANEOUS: Present with 3170 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR   EMBL; L28711; AAA65933.1; -; Genomic_DNA.
DR   EMBL; U00030; AAB68368.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06894.1; -; Genomic_DNA.
DR   PIR; S46691; S46691.
DR   RefSeq; NP_012071.1; NM_001179332.1.
DR   PDB; 2QB6; X-ray; 1.80 A; A/B=1-397.
DR   PDB; 2QB7; X-ray; 1.60 A; A/B=1-397.
DR   PDB; 2QB8; X-ray; 1.90 A; A/B=1-397.
DR   AlphaFoldDB; P38698; -.
DR   MDposit; P38698; -.
DR   SMR; P38698; -.
DR   BioGRID; 36635; 204.
DR   DIP; DIP-5633N; -.
DR   FunCoup; P38698; 293.
DR   IntAct; P38698; 4.
DR   STRING; 4932.YHR201C; -.
DR   iPTMnet; P38698; -.
DR   PaxDb; 4932-YHR201C; -.
DR   PeptideAtlas; P38698; -.
DR   EnsemblFungi; YHR201C_mRNA; YHR201C; YHR201C.
DR   GeneID; 856608; -.
DR   KEGG; sce:YHR201C; -.
DR   AGR; SGD:S000001244; -.
DR   SGD; S000001244; PPX1.
DR   VEuPathDB; FungiDB:YHR201C; -.
DR   eggNOG; KOG4129; Eukaryota.
DR   HOGENOM; CLU_019358_1_0_1; -.
DR   InParanoid; P38698; -.
DR   OMA; AAFCHQK; -.
DR   OrthoDB; 374045at2759; -.
DR   BioCyc; YEAST:YHR201C-MONOMER; -.
DR   BRENDA; 3.6.1.11; 984.
DR   BioGRID-ORCS; 856608; 0 hits in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
DR   EvolutionaryTrace; P38698; -.
DR   PRO; PR:P38698; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38698; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IMP:SGD.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IDA:SGD.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IDA:SGD.
DR   FunFam; 3.90.1640.10:FF:000011; Exopolyphosphatase; 1.
DR   FunFam; 3.10.310.20:FF:000004; PPX1p Exopolyphosphatase; 1.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   PANTHER; PTHR12112:SF39; EG:152A3.5 PROTEIN (FBGN0003116_PN PROTEIN); 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..397
FT                   /note="Polyphosphatase"
FT                   /id="PRO_0000158601"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007744|PDB:2QB8"
FT   BINDING         41
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0007744|PDB:2QB6"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007744|PDB:2QB8"
FT   BINDING         127
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0007744|PDB:2QB6"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007744|PDB:2QB8"
FT   BINDING         148
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0007744|PDB:2QB6"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0007744|PDB:2QB8"
FT   BINDING         286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0007744|PDB:2QB8"
FT   BINDING         381
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0007744|PDB:2QB8"
FT   CONFLICT        193
FT                   /note="P -> L (in Ref. 1; AAA65933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="L -> F (in Ref. 1; AAA65933)"
FT                   /evidence="ECO:0000305"
FT   HELIX           8..17
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           40..58
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           79..84
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          141..147
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           169..180
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           185..202
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   TURN            203..207
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           212..226
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           235..251
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           259..264
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          267..272
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          275..278
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          280..289
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           291..297
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           301..314
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          318..328
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          331..340
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           342..356
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          358..364
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           365..367
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   STRAND          369..374
FT                   /evidence="ECO:0007829|PDB:2QB7"
FT   HELIX           381..393
FT                   /evidence="ECO:0007829|PDB:2QB7"
SQ   SEQUENCE   397 AA;  45051 MW;  9494CB47790E07B8 CRC64;
     MSPLRKTVPE FLAHLKSLPI SKIASNDVLT ICVGNESADM DSIASAITYS YCQYIYNEGT
     YSEEKKKGSF IVPIIDIPRE DLSLRRDVMY VLEKLKIKEE ELFFIEDLKS LKQNVSQGTE
     LNSYLVDNND TPKNLKNYID NVVGIIDHHF DLQKHLDAEP RIVKVSGSCS SLVFNYWYEK
     LQGDREVVMN IAPLLMGAIL IDTSNMRRKV EESDKLAIER CQAVLSGAVN EVSAQGLEDS
     SEFYKEIKSR KNDIKGFSVS DILKKDYKQF NFQGKGHKGL EIGLSSIVKR MSWLFNEHGG
     EADFVNQCRR FQAERGLDVL VLLTSWRKAG DSHRELVILG DSNVVRELIE RVSDKLQLQL
     FGGNLDGGVA MFKQLNVEAT RKQVVPYLEE AYSNLEE
//