PYP1_YEAST
ID PYP1_YEAST Reviewed; 241 AA.
AC P53981; D6W1G7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Polyol phosphate phosphatase PYP1 {ECO:0000303|PubMed:30240188};
DE EC=3.1.3.50 {ECO:0000269|PubMed:30240188};
GN Name=PYP1 {ECO:0000303|PubMed:30240188};
GN OrderedLocusNames=YNL010W {ECO:0000312|SGD:S000004955}; ORFNames=N2866;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 DISRUPTION PHENOTYPE.
RX PubMed=30240188; DOI=10.1021/acschembio.8b00804;
RA Xu Y.F., Lu W., Chen J.C., Johnson S.A., Gibney P.A., Thomas D.G.,
RA Brown G., May A.L., Campagna S.R., Yakunin A.F., Botstein D.,
RA Rabinowitz J.D.;
RT "Discovery and Functional Characterization of a Yeast Sugar Alcohol
RT Phosphatase.";
RL ACS Chem. Biol. 13:3011-3020(2018).
CC -!- FUNCTION: Hydrolyzes sugar alcohol (polyol) phosphates
CC (PubMed:30240188). Dephosphorylates a variety of substrates, including:
CC sn-glycerol 1-phosphate (D-glycerol 3-phosphate), D-ribitol 5-
CC phosphate, D-sorbitol 6-phosphate (D-glucitol 6-phosphate), and D-
CC erythrose 4-phosphate (PubMed:30240188). Prevents accumulation of toxic
CC levels of polyol phosphates, which can impair glycolysis by inhibiting
CC glucose-6-phosphate isomerase (PubMed:30240188).
CC {ECO:0000269|PubMed:30240188}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribitol 5-phosphate + H2O = phosphate + ribitol;
CC Xref=Rhea:RHEA:47648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15963,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57695;
CC Evidence={ECO:0000269|PubMed:30240188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47649;
CC Evidence={ECO:0000269|PubMed:30240188};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol 6-phosphate + H2O = D-sorbitol + phosphate;
CC Xref=Rhea:RHEA:24580, ChEBI:CHEBI:15377, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60084; EC=3.1.3.50;
CC Evidence={ECO:0000269|PubMed:24374639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24581;
CC Evidence={ECO:0000269|PubMed:30240188};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57685;
CC Evidence={ECO:0000269|PubMed:24374639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46085;
CC Evidence={ECO:0000269|PubMed:30240188};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O = D-erythrose + phosphate;
CC Xref=Rhea:RHEA:66376, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:27904, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000269|PubMed:24374639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66377;
CC Evidence={ECO:0000269|PubMed:30240188};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q58989};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Impairs the ability to metabolize cellular polyol
CC phosphates which may build up to toxic levels in cells.
CC {ECO:0000269|PubMed:30240188}.
CC -!- MISCELLANEOUS: Present with 12600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Unlike the glycerol-1-phosphate phosphohydrolases, this enzyme
CC cannot hydrolyze L-glycerol 3-phosphate (sn-glycerol 3-phosphate) and
CC is therefore not associated with EC 3.1.3.21 / RHEA:11476.
CC {ECO:0000269|PubMed:30240188}.
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DR EMBL; Z71286; CAA95870.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10533.1; -; Genomic_DNA.
DR PIR; S62922; S62922.
DR RefSeq; NP_014388.3; NM_001182849.3.
DR AlphaFoldDB; P53981; -.
DR SMR; P53981; -.
DR BioGRID; 35815; 128.
DR IntAct; P53981; 5.
DR MINT; P53981; -.
DR STRING; 4932.YNL010W; -.
DR iPTMnet; P53981; -.
DR MaxQB; P53981; -.
DR PaxDb; P53981; -.
DR PRIDE; P53981; -.
DR EnsemblFungi; YNL010W_mRNA; YNL010W; YNL010W.
DR GeneID; 855722; -.
DR KEGG; sce:YNL010W; -.
DR SGD; S000004955; YNL010W.
DR VEuPathDB; FungiDB:YNL010W; -.
DR eggNOG; ENOG502QRU0; Eukaryota.
DR GeneTree; ENSGT00940000176373; -.
DR HOGENOM; CLU_058495_1_0_1; -.
DR InParanoid; P53981; -.
DR OMA; VPFHEFD; -.
DR BioCyc; YEAST:G3O-33051-MON; -.
DR BRENDA; 3.1.3.21; 984.
DR PRO; PR:P53981; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53981; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000121; F:glycerol-1-phosphatase activity; IDA:SGD.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; IDA:SGD.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0110130; F:ribitol-5-phosphatase activity; IDA:SGD.
DR GO; GO:0050286; F:sorbitol-6-phosphatase activity; IDA:SGD.
DR GO; GO:0052646; P:alditol phosphate metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..241
FT /note="Polyol phosphate phosphatase PYP1"
FT /id="PRO_0000203466"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 241 AA; 27481 MW; 38F5D7FF14018637 CRC64;
MVKAVIFTDF DGTVTLEDSN DYLTDTLGFG KEKRLKVFEG VLDDTKSFRQ GFMEMLESIH
TPFPECIKIL EKKIRLDPGF KDTFEWAQEN DVPVIVVSSG MKPIIKVLLT RLVGQESIHK
IDIVSNEVEI DAHDQWKIIY KDESPFGHDK SRSIDAYKKK FESTLKAGEQ RPVYFYCGDG
VSDLSAAKEC DLLFAKRGKD LVTYCKKQNV PFHEFDTFKD ILASMKQVLA GEKTVAELME
N
