PNPP_YEAST
ID PNPP_YEAST Reviewed; 312 AA.
AC P19881; D6VRC0; Q07689;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=4-nitrophenylphosphatase;
DE Short=PNPPase;
DE EC=3.1.3.41;
GN Name=PHO13; OrderedLocusNames=YDL236W;
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].
RX PubMed=2558283; DOI=10.1007/bf00260867;
RA Kaneko Y., Toh-e A., Banno I., Oshima Y.;
RT "Molecular characterization of a specific p-nitrophenylphosphatase gene,
RT PHO13, and its mapping by chromosome fragmentation in Saccharomyces
RT cerevisiae.";
RL Mol. Gen. Genet. 220:133-139(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: PHO13 is dispensable for vegetative growth and sporulation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-nitrophenyl phosphate + H2O = 4-nitrophenol + H(+) +
CC phosphate; Xref=Rhea:RHEA:21664, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57917,
CC ChEBI:CHEBI:61146; EC=3.1.3.41;
CC -!- ACTIVITY REGULATION: Activity enhanced by Mg(2+) ion but inhibited by
CC Ca(2+), Zn(2+) and Be(2+) ions. Inorganic phosphate and ATP are
CC competitive inhibitors, whereas pyrophosphate and AMP have no effect.
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: Present with 2980 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X51611; CAB56540.1; -; Genomic_DNA.
DR EMBL; Z74284; CAA98816.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11630.1; -; Genomic_DNA.
DR PIR; S67800; S67800.
DR RefSeq; NP_010045.1; NM_001180296.1.
DR AlphaFoldDB; P19881; -.
DR SMR; P19881; -.
DR BioGRID; 31875; 91.
DR DIP; DIP-1665N; -.
DR IntAct; P19881; 3.
DR MINT; P19881; -.
DR STRING; 4932.YDL236W; -.
DR iPTMnet; P19881; -.
DR MaxQB; P19881; -.
DR PaxDb; P19881; -.
DR PRIDE; P19881; -.
DR EnsemblFungi; YDL236W_mRNA; YDL236W; YDL236W.
DR GeneID; 851362; -.
DR KEGG; sce:YDL236W; -.
DR SGD; S000002395; PHO13.
DR VEuPathDB; FungiDB:YDL236W; -.
DR eggNOG; KOG2882; Eukaryota.
DR GeneTree; ENSGT00940000174879; -.
DR HOGENOM; CLU_043473_0_0_1; -.
DR InParanoid; P19881; -.
DR OMA; PPMHRET; -.
DR BioCyc; YEAST:YDL236W-MON; -.
DR BRENDA; 3.1.3.18; 984.
DR PRO; PR:P19881; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P19881; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IDA:SGD.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IDA:SGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IDA:SGD.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01452; PGP_euk; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..312
FT /note="4-nitrophenylphosphatase"
FT /id="PRO_0000058481"
FT CONFLICT 50
FT /note="N -> D (in Ref. 1; CAB56540)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="S -> P (in Ref. 1; CAB56540)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="A -> T (in Ref. 1; CAB56540)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="T -> A (in Ref. 1; CAB56540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 34625 MW; BBF36D5547018CD5 CRC64;
MTAQQGVPIK ITNKEIAQEF LDKYDTFLFD CDGVLWLGSQ ALPYTLEILN LLKQLGKQLI
FVTNNSTKSR LAYTKKFASF GIDVKEEQIF TSGYASAVYI RDFLKLQPGK DKVWVFGESG
IGEELKLMGY ESLGGADSRL DTPFDAAKSP FLVNGLDKDV SCVIAGLDTK VNYHRLAVTL
QYLQKDSVHF VGTNVDSTFP QKGYTFPGAG SMIESLAFSS NRRPSYCGKP NQNMLNSIIS
AFNLDRSKCC MVGDRLNTDM KFGVEGGLGG TLLVLSGIET EERALKISHD YPRPKFYIDK
LGDIYTLTNN EL
