GPP1_YEAST
ID GPP1_YEAST Reviewed; 250 AA.
AC P41277; D6VVM8; P38012;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Glycerol-1-phosphate phosphohydrolase 1 {ECO:0000305};
DE EC=3.1.3.21 {ECO:0000269|PubMed:8662716};
DE AltName: Full=(DL)-glycerol-3-phosphatase 1 {ECO:0000303|PubMed:8662716};
DE AltName: Full=Related to HOR2 protein 2 {ECO:0000303|PubMed:7500933};
GN Name=GPP1 {ECO:0000303|PubMed:8662716};
GN Synonyms=RHR2 {ECO:0000303|PubMed:7500933};
GN OrderedLocusNames=YIL053W {ECO:0000312|SGD:S000001315};
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 PROTEIN SEQUENCE OF 86-97 AND 173-188.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
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 [6]
RP PROTEIN SEQUENCE OF 2-8.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA Norbeck J., Blomberg A.;
RT "Metabolic and regulatory changes associated with growth of Saccharomyces
RT cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol
RT dissimilation via the dihydroxyacetone pathway.";
RL J. Biol. Chem. 272:5544-5554(1997).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9150920; DOI=10.1002/elps.1150180316;
RA Larsson T., Norbeck J., Karlsson H., Karlsson K.-A., Blomberg A.;
RT "Identification of two-dimensional gel electrophoresis resolved yeast
RT proteins by matrix-assisted laser desorption ionization mass
RT spectrometry.";
RL Electrophoresis 18:418-423(1997).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=10931288; DOI=10.1046/j.1365-2958.2000.01955.x;
RA Siderius M., Van Wuytswinkel O., Reijenga K.A., Kelders M., Mager W.H.;
RT "The control of intracellular glycerol in Saccharomyces cerevisiae
RT influences osmotic stress response and resistance to increased
RT temperature.";
RL Mol. Microbiol. 36:1381-1390(2000).
RN [9]
RP INDUCTION.
RX PubMed=11113971;
RX DOI=10.1002/1097-0061(200012)16:16<1483::aid-yea642>3.0.co;2-k;
RA Costenoble R., Valadi H., Gustafsson L., Niklasson C., Franzen C.J.;
RT "Microaerobic glycerol formation in Saccharomyces cerevisiae.";
RL Yeast 16:1483-1495(2000).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=11058591; DOI=10.1074/jbc.m007164200;
RA Pahlman A.K., Granath K., Ansell R., Hohmann S., Adler L.;
RT "The yeast glycerol 3-phosphatases Gpp1p and Gpp2p are required for
RT glycerol biosynthesis and differentially involved in the cellular responses
RT to osmotic, anaerobic, and oxidative stress.";
RL J. Biol. Chem. 276:3555-3563(2001).
RN [11]
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 [12]
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 [13]
RP INDUCTION.
RX PubMed=15066826; DOI=10.1128/aem.70.4.2307-2317.2004;
RA Sonderegger M., Jeppsson M., Hahn-Hagerdal B., Sauer U.;
RT "Molecular basis for anaerobic growth of Saccharomyces cerevisiae on
RT xylose, investigated by global gene expression and metabolic flux
RT analysis.";
RL Appl. Environ. Microbiol. 70:2307-2317(2004).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [15]
RP FUNCTION.
RX PubMed=15113568; DOI=10.1016/j.ymben.2004.02.005;
RA Nguyen H.T., Dieterich A., Athenstaedt K., Truong N.H., Stahl U.,
RA Nevoigt E.;
RT "Engineering of Saccharomyces cerevisiae for the production of L-glycerol
RT 3-phosphate.";
RL Metab. Eng. 6:155-163(2004).
RN [16]
RP FUNCTION, AND INDUCTION.
RX PubMed=16358322; DOI=10.1002/yea.1307;
RA Granath K., Modig T., Forsmark A., Adler L., Liden G.;
RT "The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic
RT glycerol metabolism in Saccharomyces cerevisiae.";
RL Yeast 22:1257-1268(2005).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [18]
RP FUNCTION.
RX PubMed=18438874; DOI=10.1002/bit.21777;
RA Popp A., Nguyen H.T., Boulahya K., Bideaux C., Alfenore S., Guillouet S.E.,
RA Nevoigt E.;
RT "Fermentative production of L-glycerol 3-phosphate utilizing a
RT Saccharomyces cerevisiae strain with an engineered glycerol biosynthetic
RT pathway.";
RL Biotechnol. Bioeng. 100:497-505(2008).
RN [19]
RP INDUCTION.
RX PubMed=17425669; DOI=10.1111/j.1567-1364.2007.00234.x;
RA Wiebe M.G., Rintala E., Tamminen A., Simolin H., Salusjarvi L., Toivari M.,
RA Kokkonen J.T., Kiuru J., Ketola R.A., Jouhten P., Huuskonen A.,
RA Maaheimo H., Ruohonen L., Penttila M.;
RT "Central carbon metabolism of Saccharomyces cerevisiae in anaerobic,
RT oxygen-limited and fully aerobic steady-state conditions and following a
RT shift to anaerobic conditions.";
RL FEMS Yeast Res. 8:140-154(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [21]
RP INDUCTION.
RX PubMed=20803479; DOI=10.1002/yea.1819;
RA Bouwman J., Kiewiet J., Lindenbergh A., van Eunen K., Siderius M.,
RA Bakker B.M.;
RT "Metabolic regulation rather than de novo enzyme synthesis dominates the
RT osmo-adaptation of yeast.";
RL Yeast 28:43-53(2011).
RN [22]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-64 AND LYS-144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "The crystal structure of an isoform of DL-glycerol-3-phosphatase, Rhr2p
RT from Saccharomyces cerevisiae.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Major isoform of glycerol-1-phosphate phosphohydrolase
CC involved in glycerol biosynthesis. Plays a role in osmoadaptation and
CC required for adaptation to anaerobic conditions.
CC {ECO:0000269|PubMed:11058591, ECO:0000269|PubMed:15113568,
CC ECO:0000269|PubMed:16358322, ECO:0000269|PubMed:18438874,
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=3.1 mM for (DL)-glycerol 3-phosphate {ECO:0000269|PubMed:8662716};
CC Vmax=49 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: In response to both anaerobic and osmotic stress. Expression
CC seems to be under the control of YIG1. {ECO:0000269|PubMed:11058591,
CC ECO:0000269|PubMed:11113971, ECO:0000269|PubMed:15066826,
CC ECO:0000269|PubMed:16358322, ECO:0000269|PubMed:17425669,
CC ECO:0000269|PubMed:20803479}.
CC -!- DISRUPTION PHENOTYPE: Leads to osmosensitivity.
CC {ECO:0000269|PubMed:10931288}.
CC -!- MISCELLANEOUS: Present with 193000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA86169.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D50471; BAA09060.1; -; mRNA.
DR EMBL; Z38060; CAA86169.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006942; DAA08494.1; -; Genomic_DNA.
DR PIR; S48426; S48426.
DR RefSeq; NP_012211.2; NM_001179403.1.
DR PDB; 2QLT; X-ray; 1.60 A; A=1-250.
DR PDBsum; 2QLT; -.
DR AlphaFoldDB; P41277; -.
DR SMR; P41277; -.
DR BioGRID; 34937; 181.
DR DIP; DIP-4713N; -.
DR IntAct; P41277; 19.
DR MINT; P41277; -.
DR STRING; 4932.YIL053W; -.
DR iPTMnet; P41277; -.
DR MaxQB; P41277; -.
DR PaxDb; P41277; -.
DR PRIDE; P41277; -.
DR TopDownProteomics; P41277; -.
DR EnsemblFungi; YIL053W_mRNA; YIL053W; YIL053W.
DR GeneID; 854758; -.
DR KEGG; sce:YIL053W; -.
DR SGD; S000001315; GPP1.
DR VEuPathDB; FungiDB:YIL053W; -.
DR eggNOG; KOG2914; Eukaryota.
DR GeneTree; ENSGT00940000176698; -.
DR HOGENOM; CLU_045011_13_4_1; -.
DR InParanoid; P41277; -.
DR OMA; VVERSWC; -.
DR BioCyc; MetaCyc:YIL053W-MON; -.
DR BioCyc; YEAST:YIL053W-MON; -.
DR BRENDA; 3.1.3.21; 984.
DR EvolutionaryTrace; P41277; -.
DR PRO; PR:P41277; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P41277; protein.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0006114; P:glycerol biosynthetic process; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IBA:GO_Central.
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 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9038161"
FT CHAIN 2..250
FT /note="Glycerol-1-phosphate phosphohydrolase 1"
FT /id="PRO_0000087560"
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:0007744|PubMed:19779198"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:15166219"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 91
FT /note="I -> IK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..17
FT /evidence="ECO:0007829|PDB:2QLT"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:2QLT"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2QLT"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:2QLT"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2QLT"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:2QLT"
SQ SEQUENCE 250 AA; 27947 MW; 9494B158A937413C CRC64;
MPLTTKPLSL KINAALFDVD GTIIISQPAI AAFWRDFGKD KPYFDAEHVI HISHGWRTYD
AIAKFAPDFA DEEYVNKLEG EIPEKYGEHS IEVPGAVKLC NALNALPKEK WAVATSGTRD
MAKKWFDILK IKRPEYFITA NDVKQGKPHP EPYLKGRNGL GFPINEQDPS KSKVVVFEDA
PAGIAAGKAA GCKIVGIATT FDLDFLKEKG CDIIVKNHES IRVGEYNAET DEVELIFDDY
LYAKDDLLKW
