ID   PPN1_CANGA              Reviewed;         663 AA.
AC   Q6FMQ0;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Endopolyphosphatase;
DE            EC=3.6.1.10;
GN   Name=PPN1; OrderedLocusNames=CAGL0K06237g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic polyphosphate (polyP)
CC       chains of many hundreds of phosphate residues into shorter lengths.
CC       {ECO:0000250|UniProtKB:Q04119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate;
CC         Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10;
CC         Evidence={ECO:0000250|UniProtKB:Q04119};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q04119};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:Q04119};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04119}.
CC   -!- PTM: Processing by proteases in the vacuole may be required for
CC       activation. {ECO:0000250|UniProtKB:Q04119}.
CC   -!- SIMILARITY: Belongs to the endopolyphosphatase PPN1 family.
CC       {ECO:0000305}.
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DR   EMBL; CR380957; CAG61455.1; -; Genomic_DNA.
DR   RefSeq; XP_448494.1; XM_448494.1.
DR   AlphaFoldDB; Q6FMQ0; -.
DR   SMR; Q6FMQ0; -.
DR   STRING; 5478.XP_448494.1; -.
DR   EnsemblFungi; CAG61455; CAG61455; CAGL0K06237g.
DR   GeneID; 2890459; -.
DR   KEGG; cgr:CAGL0K06237g; -.
DR   CGD; CAL0134089; CAGL0K06237g.
DR   VEuPathDB; FungiDB:CAGL0K06237g; -.
DR   eggNOG; KOG3770; Eukaryota.
DR   HOGENOM; CLU_013424_1_0_1; -.
DR   InParanoid; Q6FMQ0; -.
DR   OMA; MKAILMG; -.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0000298; F:endopolyphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IEA:EnsemblFungi.
DR   CDD; cd00842; MPP_ASMase; 1.
DR   InterPro; IPR041805; ASMase/PPN1_MPP.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR012358; EndopolyPtase_N1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF027093; EndopolyPtase_N1; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..663
FT                   /note="Endopolyphosphatase"
FT                   /id="PRO_0000058544"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..663
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          534..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        526
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   663 AA;  76352 MW;  DC75EC4189E9646C CRC64;
     MAVNEKDVGR KSRVSVVLWV FIALGTLFLC KNAFTFSSES IHGLKISSDD SDSVDIERQI
     SLGLTPRKPV VITDLRTGNK RKLHGRFLHI TDMHPDEYYV AGTSIDNVCH SGEPTKGKDR
     AAKFGNAMSG CDSPMLLMDM TLDWIDKNLK DQIDFVVWTG DNIRHDNDRT YPRTEDEIFR
     MNAEVAEKIK KIFRTPNSPD PRDFAVPVVP SIGNNDVFPH NLFSLGPTLQ TREYYRLWGD
     FIPEEQQRMF DRDASFFTEV IPGKLAVLSF NTLYLFKANP LVDNCDSRKQ PGYQLLLWLG
     YVLDEIRERG MKVWISGHVP PIAKNYDSSC YDKFSLWMHE YRDVIIGGLY GHMNMDHFVP
     VDVQAIRENM EEQQMSLLSE DERLTKTIRE HAIAAREAHL MGAKPVNKES YLDGVLDTYY
     KGVLQEIEQA VDSDLDIEKK KKKKGKKKKG KKEKRTLEEI YDQHSIVQVS GSVIPTFNPS
     IRVWEYNISD ITDSSSIFGE NQLEYQSWDL FFEDLEHKMK NEFDDNESSF WAASAEQNKK
     KKKKNGKPDK SIPRKKPDEL PAGPGHIQQL FSPTKFVQYF ADLDSINSEY EKLIDKGLAE
     HDAINKAFNY EVEYTSKDEP YPMESLLVKD YLHLAADLAR DNGLWKIFKE RAFISTGYED
     ERN