PPX1_YEAST
ID PPX1_YEAST Reviewed; 397 AA.
AC P38698; D3DLF0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Polyphosphatase {ECO:0000303|PubMed:7860598};
DE Short=PolyPase {ECO:0000303|PubMed:7860598};
DE EC=3.6.1.11 {ECO:0000269|PubMed:7860598};
DE AltName: Full=Exopolyphosphatase {ECO:0000303|PubMed:17599355};
DE AltName: Full=Metaphosphatase {ECO:0000305};
GN Name=PPX1 {ECO:0000303|PubMed:7860598}; OrderedLocusNames=YHR201C;
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 [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=S288c / SNY243;
RX PubMed=7860598; DOI=10.1128/jb.177.4.898-906.1995;
RA Wurst H., Shiba T., Kornberg A.;
RT "The gene for a major exopolyphosphatase of Saccharomyces cerevisiae.";
RL J. Bacteriol. 177:898-906(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [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] {ECO:0007744|PDB:2QB6, ECO:0007744|PDB:2QB7, ECO:0007744|PDB:2QB8}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP; MAGNESIUM AND
RP MANGANESE.
RX PubMed=17599355; DOI=10.1016/j.jmb.2007.05.066;
RA Ugochukwu E., Lovering A.L., Mather O.C., Young T.W., White S.A.;
RT "The crystal structure of the cytosolic exopolyphosphatase from
RT Saccharomyces cerevisiae reveals the basis for substrate specificity.";
RL J. Mol. Biol. 371:1007-1021(2007).
CC -!- FUNCTION: Polyphosphatase (polyPase) involved in the degradation of
CC inorganic polyphosphates (polyP) that is able to degrade a range of
CC chains from three to several hundreds of residues in a highly
CC processive manner. {ECO:0000269|PubMed:7860598}.
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 Evidence={ECO:0000269|PubMed:7860598};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17599355};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17599355};
CC -!- MISCELLANEOUS: Present with 3170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR EMBL; L28711; AAA65933.1; -; Genomic_DNA.
DR EMBL; U00030; AAB68368.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06894.1; -; Genomic_DNA.
DR PIR; S46691; S46691.
DR RefSeq; NP_012071.1; NM_001179332.1.
DR PDB; 2QB6; X-ray; 1.80 A; A/B=1-397.
DR PDB; 2QB7; X-ray; 1.60 A; A/B=1-397.
DR PDB; 2QB8; X-ray; 1.90 A; A/B=1-397.
DR PDBsum; 2QB6; -.
DR PDBsum; 2QB7; -.
DR PDBsum; 2QB8; -.
DR AlphaFoldDB; P38698; -.
DR SMR; P38698; -.
DR BioGRID; 36635; 198.
DR DIP; DIP-5633N; -.
DR IntAct; P38698; 3.
DR MINT; P38698; -.
DR STRING; 4932.YHR201C; -.
DR MaxQB; P38698; -.
DR PaxDb; P38698; -.
DR PRIDE; P38698; -.
DR EnsemblFungi; YHR201C_mRNA; YHR201C; YHR201C.
DR GeneID; 856608; -.
DR KEGG; sce:YHR201C; -.
DR SGD; S000001244; PPX1.
DR VEuPathDB; FungiDB:YHR201C; -.
DR eggNOG; KOG4129; Eukaryota.
DR GeneTree; ENSGT00450000040262; -.
DR HOGENOM; CLU_019358_1_0_1; -.
DR InParanoid; P38698; -.
DR OMA; HSRKRVA; -.
DR BioCyc; YEAST:YHR201C-MON; -.
DR BRENDA; 3.6.1.11; 984.
DR EvolutionaryTrace; P38698; -.
DR PRO; PR:P38698; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38698; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004309; F:exopolyphosphatase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006798; P:polyphosphate catabolic process; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..397
FT /note="Polyphosphatase"
FT /id="PRO_0000158601"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:2QB8"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0007744|PDB:2QB6"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:2QB8"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0007744|PDB:2QB6"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:2QB8"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0007744|PDB:2QB6"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2QB8"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2QB8"
FT BINDING 381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2QB8"
FT CONFLICT 193
FT /note="P -> L (in Ref. 1; AAA65933)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="L -> F (in Ref. 1; AAA65933)"
FT /evidence="ECO:0000305"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 40..58
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2QB7"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:2QB7"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:2QB7"
FT TURN 203..207
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 235..251
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 280..289
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 318..328
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:2QB7"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:2QB7"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:2QB7"
SQ SEQUENCE 397 AA; 45051 MW; 9494CB47790E07B8 CRC64;
MSPLRKTVPE FLAHLKSLPI SKIASNDVLT ICVGNESADM DSIASAITYS YCQYIYNEGT
YSEEKKKGSF IVPIIDIPRE DLSLRRDVMY VLEKLKIKEE ELFFIEDLKS LKQNVSQGTE
LNSYLVDNND TPKNLKNYID NVVGIIDHHF DLQKHLDAEP RIVKVSGSCS SLVFNYWYEK
LQGDREVVMN IAPLLMGAIL IDTSNMRRKV EESDKLAIER CQAVLSGAVN EVSAQGLEDS
SEFYKEIKSR KNDIKGFSVS DILKKDYKQF NFQGKGHKGL EIGLSSIVKR MSWLFNEHGG
EADFVNQCRR FQAERGLDVL VLLTSWRKAG DSHRELVILG DSNVVRELIE RVSDKLQLQL
FGGNLDGGVA MFKQLNVEAT RKQVVPYLEE AYSNLEE
