PPN1_DEBHA
ID PPN1_DEBHA Reviewed; 713 AA.
AC Q6BKG0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Endopolyphosphatase;
DE EC=3.6.1.10;
GN Name=PPN1; OrderedLocusNames=DEHA2F22264g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89712.2; -; Genomic_DNA.
DR RefSeq; XP_461311.2; XM_461311.2.
DR AlphaFoldDB; Q6BKG0; -.
DR SMR; Q6BKG0; -.
DR STRING; 4959.XP_461311.2; -.
DR EnsemblFungi; CAG89712; CAG89712; DEHA2F22264g.
DR GeneID; 2904257; -.
DR KEGG; dha:DEHA2F22264g; -.
DR VEuPathDB; FungiDB:DEHA2F22264g; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_1_0_1; -.
DR InParanoid; Q6BKG0; -.
DR OMA; MKAILMG; -.
DR OrthoDB; 1116351at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.60.21.10; -; 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..713
FT /note="Endopolyphosphatase"
FT /id="PRO_0000058546"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..713
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 399..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 713 AA; 81885 MW; 1DD7BA09E78B4897 CRC64;
MSVLIDEKSH RSSGSTRSRI VVTVVGVLLM VSGLAVMLGH QSGSANEALG MEYEKPSVEV
LDLEATEVEQ LTKLGLSPKP KLKIVKGGDE QVLHGRFLHI TDMHPDKYYK TGADVGSLCH
SGKGSAGKYG DAVLGCDSPM VLMEDTLKWV KENLKDKIDF VVWTGDNVRH DNDRRYPRTE
SNIFDMNQRV SELMYETFKE ENPRGGRPRQ LKIPLVPSLG NNDVFPHNLF SPGPTLQTRE
LFKIWHDFVP AAQLHIFNRG AYFFKEIIPN ELAVLSINTL YLFQSNPLVD NCDRKKDPGH
KLFEWLGYTL KEMRARNMKV WLSGHVPPNE KNYDISCLRK YIVWMHEYRD VIIGGLYGHM
NIDHFIPLDS KEAYKSIKNK FGKLGFDYEL SFENDLYVSD DDDNSDSDSD DDDEDTSLEE
SYSNFNSPIL KDGFEDSVNF KNMDDIRIQG GVPNGKVGYM ENVRKEYYAN VKGKKKSGYV
SERYSIAHVT ASVVPTFNSG LRVWEYNITG LQNLLTSDNQ PRFAPWNEFF EGLEKLMETQ
VEADYDDEFI TFGQQVEIFK NDNTFPPKMP KSKSLGPAYI PQAFTPERYV QYYADLANIN
RGEKEFSYEF EYATDDKVYD MDSLTVDDWI SLARRLGKPV KEKKNKSNKK SKKKKKNKDK
RLLENSEPLK QDGSKDSRLE QDRVQQSARL ENLWQHYLKY SFVSSEYENM GMG
