PPX1_SCHPO
ID PPX1_SCHPO Reviewed; 384 AA.
AC O14094;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative exopolyphosphatase;
DE Short=ExopolyPase;
DE EC=3.6.1.11;
DE AltName: Full=Metaphosphatase;
GN ORFNames=SPAC2F3.11;
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 [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).
CC -!- FUNCTION: Degradation of inorganic polyphosphates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16267.1; -; Genomic_DNA.
DR PIR; T38544; T38544.
DR RefSeq; NP_594390.1; NM_001019812.2.
DR AlphaFoldDB; O14094; -.
DR SMR; O14094; -.
DR BioGRID; 278344; 44.
DR STRING; 4896.SPAC2F3.11.1; -.
DR iPTMnet; O14094; -.
DR MaxQB; O14094; -.
DR PaxDb; O14094; -.
DR PRIDE; O14094; -.
DR EnsemblFungi; SPAC2F3.11.1; SPAC2F3.11.1:pep; SPAC2F3.11.
DR GeneID; 2541853; -.
DR KEGG; spo:SPAC2F3.11; -.
DR PomBase; SPAC2F3.11; -.
DR VEuPathDB; FungiDB:SPAC2F3.11; -.
DR eggNOG; KOG4129; Eukaryota.
DR HOGENOM; CLU_019358_1_0_1; -.
DR InParanoid; O14094; -.
DR OMA; HSRKRVA; -.
DR PhylomeDB; O14094; -.
DR PRO; PR:O14094; -.
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:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004309; F:exopolyphosphatase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006112; P:energy reserve metabolic process; IC:PomBase.
DR GO; GO:0006798; P:polyphosphate catabolic process; ISO:PomBase.
DR Gene3D; 3.10.310.20; -; 1.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
DR SMART; SM01131; DHHA2; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..384
FT /note="Putative exopolyphosphatase"
FT /id="PRO_0000158600"
FT BINDING 40
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 43297 MW; 643CC43C7AF185EA CRC64;
MKLGRFLENG REQIRNLLLN ASTVSSAPSF SFVSGNESAD LDSCASSIVY AYCLQRKQLG
RIVVPFFNIP RKELRLRPEL SYLLNLASIS SDDIVFLDDI VKLPKRIFSN PIYLVDHNSL
DRKDLENFNG SIAGIIDHHK DEGGSLHADP RIIEECGSCC TLVCRYFMPV IRSLYDSKVS
ELHQTATNLA VLALGPILID TGNLKNEKTT DTDVKIVNDL CSFVPKDWVR DEFFDTLKEK
KKSCKGFSFD DLLRRDLKQY FPDGIVVNYA SVGKGLDWIK KKRLGWEDEL KSFAEVQNSD
LVIVGLSLSK NDEFGRQLIL YKRTERGAGL ADSFLKLSKQ NLGLEIIEEK DNGDLSMWNQ
RNSAASRKKV VPLLMDSVKQ VASK
