ID PPN1_KLULA Reviewed; 681 AA.
AC Q6CWT7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Endopolyphosphatase;
DE EC=3.6.1.10;
GN Name=PPN1; OrderedLocusNames=KLLA0B01606g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH01995.1; -; Genomic_DNA.
DR RefSeq; XP_451602.1; XM_451602.1.
DR AlphaFoldDB; Q6CWT7; -.
DR SMR; Q6CWT7; -.
DR STRING; 284590.Q6CWT7; -.
DR GlyCosmos; Q6CWT7; 4 sites, No reported glycans.
DR PaxDb; 284590-Q6CWT7; -.
DR GeneID; 2897267; -.
DR KEGG; kla:KLLA0_B01606g; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_1_0_1; -.
DR InParanoid; Q6CWT7; -.
DR OMA; WAERYSV; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000298; F:endopolyphosphatase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR10340:SF59; METALLOPHOS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF027093; EndopolyPtase_N1; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..681
FT /note="Endopolyphosphatase"
FT /id="PRO_0000058547"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..681
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 549..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 681 AA; 78413 MW; 329D965217E51EEF CRC64;
MKELQLPEKR KSNTGLSWFP SPRILQVFLV LLGAIVAFLS FSATSSIISS SPKHHSCHDN
VEEAAVKYHY STISSDELPI SNERLASLGL TPNQPVKITD IGGKEKSIKG RFLHITDMHP
DLYYKENTSI DDTCHRGKPK NDGDRAARFG NAMKGCDGPP DLMYYTLDWI HKNLSDEIDF
IIWTGDNVRH DNDRRIPRTE QQIFDMNRQV SELFLKTFKD HESDDPRDLK VKIIPSLGNN
DVFPHNLFSP GPTLQTRELY DIWSQFIPPA QQNTFDRYAS FFVEAIPGKL AVISLNTLYM
FKGNPLVDNC SNKKQPGYKM LLWVGFTLQE LRDRGMKVWL SGHVPPIPKN FDSSCSDKLA
LWLHEYSDII IGGFYGHMNM DHFIPVDGEK AWDDIANSMA ISEYSGFFEQ DFLEDAIAAR
EIRAEGAKPV KKVNYMNGVR DAYYSRISED VKKLSEKDPL YERYSIVHIG TSIIPTFNPG
FRIWEYNITE LQTEEEVLHS HQPWDSFFEH LDVEIQKIIE EAEEAEEVEA FEDDEQIDSE
IPDVLISKKK KKKGKKGKKN KNSKNWWKTD KTFPKKKPKN LPPGPAYENQ LFSPLRFVQY
YADLKEIDKQ YLKLLKEGKS EDEAASIAFK YQIEYASDDK PYPMKTTLVK DYIELASELS
GNDKLWDTFL ERAFCSSGYE D
//
