YO283_YEAST
ID YO283_YEAST Reviewed; 230 AA.
AC Q12040; D6W2Y1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Broad-specificity phosphatase YOR283W;
DE EC=3.1.3.-;
GN OrderedLocusNames=YOR283W;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [5]
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 [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19753119; DOI=10.1371/journal.pone.0006993;
RA Ho C.K., Lam A.F., Symington L.S.;
RT "Identification of nucleases and phosphatases by direct biochemical screen
RT of the Saccharomyces cerevisiae proteome.";
RL PLoS ONE 4:E6993-E6993(2009).
RN [7]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=20427268; DOI=10.1074/jbc.m110.118315;
RA Kuznetsova E., Xu L., Singer A., Brown G., Dong A., Flick R., Cui H.,
RA Cuff M., Joachimiak A., Savchenko A., Yakunin A.F.;
RT "Structure and activity of the metal-independent fructose-1,6-
RT bisphosphatase YK23 from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 285:21049-21059(2010).
CC -!- FUNCTION: Metal-independent phosphatase active against a broad range of
CC phosphorylated substrates including nucleoside tri- and diphosphates,
CC phosphorylated organic acids, and amino acids. Shows no activity
CC against phytic acid, phosphorylated carbohydrates, and nucleoside
CC monophosphates. {ECO:0000269|PubMed:19753119,
CC ECO:0000269|PubMed:20427268}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-9. Active from pH 5.5 to pH 9.5.
CC {ECO:0000269|PubMed:19753119};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; X89633; CAA61787.1; -; Genomic_DNA.
DR EMBL; Z75191; CAA99510.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11047.1; -; Genomic_DNA.
DR PIR; S67185; S67185.
DR RefSeq; NP_014926.1; NM_001183702.1.
DR AlphaFoldDB; Q12040; -.
DR SMR; Q12040; -.
DR BioGRID; 34670; 37.
DR DIP; DIP-6512N; -.
DR IntAct; Q12040; 5.
DR MINT; Q12040; -.
DR STRING; 4932.YOR283W; -.
DR iPTMnet; Q12040; -.
DR MaxQB; Q12040; -.
DR PaxDb; Q12040; -.
DR PRIDE; Q12040; -.
DR EnsemblFungi; YOR283W_mRNA; YOR283W; YOR283W.
DR GeneID; 854457; -.
DR KEGG; sce:YOR283W; -.
DR SGD; S000005809; YOR283W.
DR VEuPathDB; FungiDB:YOR283W; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00940000163946; -.
DR HOGENOM; CLU_033323_9_2_1; -.
DR InParanoid; Q12040; -.
DR OMA; QTDHNVK; -.
DR BioCyc; YEAST:G3O-33769-MON; -.
DR PRO; PR:Q12040; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12040; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IDA:SGD.
DR GO; GO:0016311; P:dephosphorylation; IDA:SGD.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..230
FT /note="Broad-specificity phosphatase YOR283W"
FT /id="PRO_0000245254"
FT ACT_SITE 24
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 102
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT BINDING 36..37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102..105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62707"
SQ SEQUENCE 230 AA; 26177 MW; 29CC8BD6884D97C5 CRC64;
MTKEVPYYCD NDDNNIIRLF IIRHGQTEHN VKKILQGHKD TSINPTGEEQ ATKLGHYLRS
RGIHFDKVVS SDLKRCRQTT ALVLKHSKQE NVPTSYTSGL RERYMGVIEG MQITEAEKYA
DKHGEGSFRN FGEKSDDFVA RLTGCVEEEV AEASNEGVKN LALVSHGGAI RMILQWLKYE
NHQAHKIIVF NTSVTIVDYV KDSKQFIVRR VGNTQHLGDG EFVVSDLRLR
