GPP2_YEAST
ID GPP2_YEAST Reviewed; 250 AA.
AC P40106; D3DLW7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glycerol-1-phosphate phosphohydrolase 2 {ECO:0000305};
DE EC=3.1.3.21 {ECO:0000269|PubMed:8662716};
DE AltName: Full=(DL)-glycerol-3-phosphatase 2 {ECO:0000303|PubMed:8662716};
DE AltName: Full=Hyperosmolarity-responsive protein 2 {ECO:0000303|PubMed:7500933};
GN Name=GPP2 {ECO:0000303|PubMed:8662716};
GN Synonyms=HOR2 {ECO:0000303|PubMed:7500933}; OrderedLocusNames=YER062C;
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 [MRNA].
RC STRAIN=RS16;
RX PubMed=7500933; DOI=10.1007/bf00290358;
RA Hirayama T., Maeda T., Saito H., Shinozaki K.;
RT "Cloning and characterization of seven cDNAs for hyperosmolarity-responsive
RT (HOR) genes of Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 249:127-138(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND INDUCTION.
RX PubMed=8662716; DOI=10.1074/jbc.271.23.13875;
RA Norbeck J., Paehlman A.-K., Akhtar N., Blomberg A., Adler L.;
RT "Purification and characterization of two isoenzymes of DL-glycerol-3-
RT phosphatase from Saccharomyces cerevisiae. Identification of the
RT corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of
RT Gpp2p expression by the osmosensing mitogen-activated protein kinase signal
RT transduction pathway.";
RL J. Biol. Chem. 271:13875-13881(1996).
RN [5]
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 [6]
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).
CC -!- FUNCTION: Glycerol-1-phosphate phosphohydrolase involved in glycerol
CC biosynthesis. Plays a role in osmoadaptation.
CC {ECO:0000269|PubMed:8662716}.
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; EC=3.1.3.21;
CC Evidence={ECO:0000269|PubMed:8662716};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21;
CC Evidence={ECO:0000269|PubMed:8662716};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:8662716};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 mM for (DL)-glycerol 3-phosphate {ECO:0000269|PubMed:8662716};
CC Vmax=46 umol/min/mg enzyme {ECO:0000269|PubMed:8662716};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:8662716};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8662716}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By osmotic stress (at protein level).
CC {ECO:0000269|PubMed:8662716}.
CC -!- MISCELLANEOUS: Present with 5000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D50469; BAA09058.1; -; mRNA.
DR EMBL; U18813; AAB64598.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07721.1; -; Genomic_DNA.
DR PIR; S50565; S50565.
DR RefSeq; NP_010984.3; NM_001178953.3.
DR AlphaFoldDB; P40106; -.
DR SMR; P40106; -.
DR BioGRID; 36804; 93.
DR DIP; DIP-1366N; -.
DR IntAct; P40106; 8.
DR MINT; P40106; -.
DR STRING; 4932.YER062C; -.
DR iPTMnet; P40106; -.
DR MaxQB; P40106; -.
DR PaxDb; P40106; -.
DR PRIDE; P40106; -.
DR EnsemblFungi; YER062C_mRNA; YER062C; YER062C.
DR GeneID; 856791; -.
DR KEGG; sce:YER062C; -.
DR SGD; S000000864; GPP2.
DR VEuPathDB; FungiDB:YER062C; -.
DR eggNOG; KOG2914; Eukaryota.
DR GeneTree; ENSGT00940000176698; -.
DR HOGENOM; CLU_045011_13_4_1; -.
DR InParanoid; P40106; -.
DR OMA; TNIYTPR; -.
DR BioCyc; MetaCyc:YER062C-MON; -.
DR BioCyc; YEAST:YER062C-MON; -.
DR BRENDA; 3.1.3.21; 984.
DR PRO; PR:P40106; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40106; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0000121; F:glycerol-1-phosphatase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:SGD.
DR GO; GO:0006114; P:glycerol biosynthetic process; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IDA:SGD.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Isopeptide bond;
KW Magnesium; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response; Ubl conjugation.
FT CHAIN 1..250
FT /note="Glycerol-1-phosphate phosphohydrolase 2"
FT /id="PRO_0000087561"
FT ACT_SITE 18
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 20
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41277"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P41277"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P41277"
SQ SEQUENCE 250 AA; 27814 MW; D69F343B10417313 CRC64;
MGLTTKPLSL KVNAALFDVD GTIIISQPAI AAFWRDFGKD KPYFDAEHVI QVSHGWRTFD
AIAKFAPDFA NEEYVNKLEA EIPVKYGEKS IEVPGAVKLC NALNALPKEK WAVATSGTRD
MAQKWFEHLG IRRPKYFITA NDVKQGKPHP EPYLKGRNGL GYPINEQDPS KSKVVVFEDA
PAGIAAGKAA GCKIIGIATT FDLDFLKEKG CDIIVKNHES IRVGGYNAET DEVEFIFDDY
LYAKDDLLKW
