Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycerol-1-phosphate phosphohydrolase 1

Gene

GPP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major isoform of glycerol-1-phosphate phosphohydrolase involved in glycerol biosynthesis. Plays a role in osmoadaptation and required for adaptation to anaerobic conditions.5 Publications

Catalytic activityi

Glycerol 1-phosphate + H2O = glycerol + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=3.1 mM for (DL)-glycerol 3-phosphate1 Publication
  1. Vmax=49 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei18 – 181NucleophileBy similarity
Metal bindingi18 – 181MagnesiumBy similarity
Active sitei20 – 201Proton donorBy similarity
Metal bindingi20 – 201MagnesiumBy similarity
Metal bindingi179 – 1791MagnesiumBy similarity

GO - Molecular functioni

  • glycerol-1-phosphatase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • dephosphorylation Source: GOC
  • glycerol biosynthetic process Source: SGD
  • response to osmotic stress Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YIL053W-MONOMER.
YEAST:YIL053W-MONOMER.
BRENDAi3.1.3.21. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-1-phosphate phosphohydrolase 1Curated (EC:3.1.3.211 Publication)
Alternative name(s):
(DL)-glycerol-3-phosphatase 11 Publication
Related to HOR2 protein 21 Publication
Gene namesi
Name:GPP11 Publication
Synonyms:RHR21 Publication
Ordered Locus Names:YIL053WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL053W.
SGDiS000001315. GPP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Leads to osmosensitivity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 250249Glycerol-1-phosphate phosphohydrolase 1PRO_0000087560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki64 – 64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei90 – 901PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP41277.
PeptideAtlasiP41277.
TopDownProteomicsiP41277.

PTM databases

iPTMnetiP41277.

Expressioni

Inductioni

In response to both anaerobic and osmotic stress. Expression seems to be under the control of YIG1.6 Publications

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
YIG1Q089563EBI-7829,EBI-30385

Protein-protein interaction databases

BioGridi34937. 93 interactions.
DIPiDIP-4713N.
IntActiP41277. 10 interactions.
MINTiMINT-487007.

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1712Combined sources
Turni21 – 233Combined sources
Helixi27 – 3812Combined sources
Helixi46 – 527Combined sources
Helixi58 – 658Combined sources
Helixi67 – 693Combined sources
Helixi72 – 809Combined sources
Helixi82 – 865Combined sources
Helixi96 – 1049Combined sources
Helixi108 – 1103Combined sources
Beta strandi111 – 1144Combined sources
Helixi119 – 12911Combined sources
Beta strandi135 – 1384Combined sources
Helixi140 – 1423Combined sources
Helixi151 – 1599Combined sources
Helixi169 – 1713Combined sources
Beta strandi174 – 1807Combined sources
Helixi181 – 1899Combined sources
Beta strandi193 – 2019Combined sources
Helixi203 – 2064Combined sources
Beta strandi212 – 2176Combined sources
Helixi218 – 2203Combined sources
Beta strandi221 – 2233Combined sources
Turni228 – 2314Combined sources
Beta strandi232 – 2387Combined sources
Beta strandi241 – 2433Combined sources
Turni245 – 2484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QLTX-ray1.60A1-250[»]
ProteinModelPortaliP41277.
SMRiP41277. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41277.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00530000065392.
HOGENOMiHOG000248341.
InParanoidiP41277.
KOiK06116.
OMAiEFWRDFG.
OrthoDBiEOG72JWT8.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41277-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLTTKPLSL KINAALFDVD GTIIISQPAI AAFWRDFGKD KPYFDAEHVI
60 70 80 90 100
HISHGWRTYD AIAKFAPDFA DEEYVNKLEG EIPEKYGEHS IEVPGAVKLC
110 120 130 140 150
NALNALPKEK WAVATSGTRD MAKKWFDILK IKRPEYFITA NDVKQGKPHP
160 170 180 190 200
EPYLKGRNGL GFPINEQDPS KSKVVVFEDA PAGIAAGKAA GCKIVGIATT
210 220 230 240 250
FDLDFLKEKG CDIIVKNHES IRVGEYNAET DEVELIFDDY LYAKDDLLKW
Length:250
Mass (Da):27,947
Last modified:January 23, 2007 - v3
Checksum:i9494B158A937413C
GO

Sequence cautioni

The sequence CAA86169.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911I → IK AA sequence (PubMed:7895733).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50471 mRNA. Translation: BAA09060.1.
Z38060 Genomic DNA. Translation: CAA86169.1. Different initiation.
BK006942 Genomic DNA. Translation: DAA08494.1.
PIRiS48426.
RefSeqiNP_012211.2. NM_001179403.1.

Genome annotation databases

EnsemblFungiiYIL053W; YIL053W; YIL053W.
GeneIDi854758.
KEGGisce:YIL053W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50471 mRNA. Translation: BAA09060.1.
Z38060 Genomic DNA. Translation: CAA86169.1. Different initiation.
BK006942 Genomic DNA. Translation: DAA08494.1.
PIRiS48426.
RefSeqiNP_012211.2. NM_001179403.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QLTX-ray1.60A1-250[»]
ProteinModelPortaliP41277.
SMRiP41277. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34937. 93 interactions.
DIPiDIP-4713N.
IntActiP41277. 10 interactions.
MINTiMINT-487007.

PTM databases

iPTMnetiP41277.

Proteomic databases

MaxQBiP41277.
PeptideAtlasiP41277.
TopDownProteomicsiP41277.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL053W; YIL053W; YIL053W.
GeneIDi854758.
KEGGisce:YIL053W.

Organism-specific databases

EuPathDBiFungiDB:YIL053W.
SGDiS000001315. GPP1.

Phylogenomic databases

GeneTreeiENSGT00530000065392.
HOGENOMiHOG000248341.
InParanoidiP41277.
KOiK06116.
OMAiEFWRDFG.
OrthoDBiEOG72JWT8.

Enzyme and pathway databases

BioCyciMetaCyc:YIL053W-MONOMER.
YEAST:YIL053W-MONOMER.
BRENDAi3.1.3.21. 984.

Miscellaneous databases

EvolutionaryTraceiP41277.
NextBioi977496.
PROiP41277.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of seven cDNAs for hyperosmolarity-responsive (HOR) genes of Saccharomyces cerevisiae."
    Hirayama T., Maeda T., Saito H., Shinozaki K.
    Mol. Gen. Genet. 249:127-138(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: RS16.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: PROTEIN SEQUENCE OF 86-97 AND 173-188.
    Strain: ATCC 204508 / S288c.
  5. "Purification and characterization of two isoenzymes of DL-glycerol-3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of Gpp2p expression by the osmosensing mitogen-activated protein kinase signal transduction pathway."
    Norbeck J., Paehlman A.-K., Akhtar N., Blomberg A., Adler L.
    J. Biol. Chem. 271:13875-13881(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  6. "Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway."
    Norbeck J., Blomberg A.
    J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8.
    Strain: ATCC 44827 / SKQ2N.
  7. "Identification of two-dimensional gel electrophoresis resolved yeast proteins by matrix-assisted laser desorption ionization mass spectrometry."
    Larsson T., Norbeck J., Karlsson H., Karlsson K.-A., Blomberg A.
    Electrophoresis 18:418-423(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  8. "The control of intracellular glycerol in Saccharomyces cerevisiae influences osmotic stress response and resistance to increased temperature."
    Siderius M., Van Wuytswinkel O., Reijenga K.A., Kelders M., Mager W.H.
    Mol. Microbiol. 36:1381-1390(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Microaerobic glycerol formation in Saccharomyces cerevisiae."
    Costenoble R., Valadi H., Gustafsson L., Niklasson C., Franzen C.J.
    Yeast 16:1483-1495(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "The yeast glycerol 3-phosphatases Gpp1p and Gpp2p are required for glycerol biosynthesis and differentially involved in the cellular responses to osmotic, anaerobic, and oxidative stress."
    Pahlman A.K., Granath K., Ansell R., Hohmann S., Adler L.
    J. Biol. Chem. 276:3555-3563(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Molecular basis for anaerobic growth of Saccharomyces cerevisiae on xylose, investigated by global gene expression and metabolic flux analysis."
    Sonderegger M., Jeppsson M., Hahn-Hagerdal B., Sauer U.
    Appl. Environ. Microbiol. 70:2307-2317(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses."
    Zhou W., Ryan J.J., Zhou H.
    J. Biol. Chem. 279:32262-32268(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64.
  15. "Engineering of Saccharomyces cerevisiae for the production of L-glycerol 3-phosphate."
    Nguyen H.T., Dieterich A., Athenstaedt K., Truong N.H., Stahl U., Nevoigt E.
    Metab. Eng. 6:155-163(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic glycerol metabolism in Saccharomyces cerevisiae."
    Granath K., Modig T., Forsmark A., Adler L., Liden G.
    Yeast 22:1257-1268(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  17. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Fermentative production of L-glycerol 3-phosphate utilizing a Saccharomyces cerevisiae strain with an engineered glycerol biosynthetic pathway."
    Popp A., Nguyen H.T., Boulahya K., Bideaux C., Alfenore S., Guillouet S.E., Nevoigt E.
    Biotechnol. Bioeng. 100:497-505(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Central carbon metabolism of Saccharomyces cerevisiae in anaerobic, oxygen-limited and fully aerobic steady-state conditions and following a shift to anaerobic conditions."
    Wiebe M.G., Rintala E., Tamminen A., Simolin H., Salusjarvi L., Toivari M., Kokkonen J.T., Kiuru J., Ketola R.A., Jouhten P., Huuskonen A., Maaheimo H., Ruohonen L., Penttila M.
    FEMS Yeast Res. 8:140-154(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  20. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Metabolic regulation rather than de novo enzyme synthesis dominates the osmo-adaptation of yeast."
    Bouwman J., Kiewiet J., Lindenbergh A., van Eunen K., Siderius M., Bakker B.M.
    Yeast 28:43-53(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  22. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "The crystal structure of an isoform of DL-glycerol-3-phosphatase, Rhr2p from Saccharomyces cerevisiae."
    Midwest center for structural genomics (MCSG)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiGPP1_YEAST
AccessioniPrimary (citable) accession number: P41277
Secondary accession number(s): D6VVM8, P38012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 193000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.