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P51601

- GCH1_YEAST

UniProt

P51601 - GCH1_YEAST

Protein

GTP cyclohydrolase 1

Gene

FOL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.

    Catalytic activityi

    GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.

    Enzyme regulationi

    GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi132 – 1321ZincBy similarity
    Metal bindingi135 – 1351ZincBy similarity
    Metal bindingi203 – 2031ZincBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. GTP cyclohydrolase I activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. folic acid biosynthetic process Source: UniProtKB-KW
    3. folic acid-containing compound biosynthetic process Source: SGD
    4. tetrahydrofolate biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Folate biosynthesis

    Keywords - Ligandi

    GTP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YGR267C-MONOMER.
    ReactomeiREACT_189008. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    UniPathwayiUPA00848; UER00151.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP cyclohydrolase 1 (EC:3.5.4.16)
    Alternative name(s):
    GTP cyclohydrolase I
    Short name:
    GTP-CH-I
    Gene namesi
    Name:FOL2
    Ordered Locus Names:YGR267C
    ORF Names:G9349
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR267c.
    SGDiS000003499. FOL2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 243243GTP cyclohydrolase 1PRO_0000119489Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphothreonine3 Publications
    Modified residuei23 – 231Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP51601.
    PaxDbiP51601.
    PeptideAtlasiP51601.

    Expressioni

    Gene expression databases

    GenevestigatoriP51601.

    Interactioni

    Subunit structurei

    Toroid-shaped homodecamer, composed of two pentamers of five dimers.By similarity

    Protein-protein interaction databases

    BioGridi33517. 39 interactions.
    DIPiDIP-1318N.
    IntActiP51601. 7 interactions.
    MINTiMINT-389985.
    STRINGi4932.YGR267C.

    Structurei

    3D structure databases

    ProteinModelPortaliP51601.
    SMRiP51601. Positions 50-238.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase I family.Curated

    Phylogenomic databases

    eggNOGiCOG0302.
    GeneTreeiENSGT00390000013481.
    HOGENOMiHOG000221222.
    KOiK01495.
    OMAiVRDIEIY.
    OrthoDBiEOG7QRR5W.

    Family and domain databases

    HAMAPiMF_00223. FolE.
    InterProiIPR001474. GTP_CycHdrlase_I.
    IPR018234. GTP_CycHdrlase_I_CS.
    IPR020602. GTP_CycHdrlase_I_dom.
    [Graphical view]
    PANTHERiPTHR11109. PTHR11109. 1 hit.
    PfamiPF01227. GTP_cyclohydroI. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00063. folE. 1 hit.
    PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P51601-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHNIQLVQEI ERHETPLNIR PTSPYTLNPP VERDGFSWPS VGTRQRAEET    50
    EEEEKERIQR ISGAIKTILT ELGEDVNREG LLDTPQRYAK AMLYFTKGYQ 100
    TNIMDDVIKN AVFEEDHDEM VIVRDIEIYS LCEHHLVPFF GKVHIGYIPN 150
    KKVIGLSKLA RLAEMYARRL QVQERLTKQI AMALSDILKP LGVAVVMEAS 200
    HMCMVSRGIQ KTGSSTVTSC MLGGFRAHKT REEFLTLLGR RSI 243
    Length:243
    Mass (Da):27,769
    Last modified:October 1, 1996 - v1
    Checksum:iA71AB8750AECD3F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1602LA → QG in CAA89826. (PubMed:7542887)Curated
    Sequence conflicti206 – 2061S → M in CAA89826. (PubMed:7542887)Curated
    Sequence conflicti217 – 2171V → A in CAA87397. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z47201 Genomic DNA. Translation: CAA87397.1.
    X94314 Genomic DNA. Translation: CAA63975.1.
    Y07893 Genomic DNA. Translation: CAA69198.1.
    Z73052 Genomic DNA. Translation: CAA97297.1.
    AY692993 Genomic DNA. Translation: AAT93012.1.
    Z49756 mRNA. Translation: CAA89826.1.
    BK006941 Genomic DNA. Translation: DAA08356.1.
    PIRiJC4585.
    RefSeqiNP_011783.1. NM_001181396.1.

    Genome annotation databases

    EnsemblFungiiYGR267C; YGR267C; YGR267C.
    GeneIDi853183.
    KEGGisce:YGR267C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z47201 Genomic DNA. Translation: CAA87397.1 .
    X94314 Genomic DNA. Translation: CAA63975.1 .
    Y07893 Genomic DNA. Translation: CAA69198.1 .
    Z73052 Genomic DNA. Translation: CAA97297.1 .
    AY692993 Genomic DNA. Translation: AAT93012.1 .
    Z49756 mRNA. Translation: CAA89826.1 .
    BK006941 Genomic DNA. Translation: DAA08356.1 .
    PIRi JC4585.
    RefSeqi NP_011783.1. NM_001181396.1.

    3D structure databases

    ProteinModelPortali P51601.
    SMRi P51601. Positions 50-238.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33517. 39 interactions.
    DIPi DIP-1318N.
    IntActi P51601. 7 interactions.
    MINTi MINT-389985.
    STRINGi 4932.YGR267C.

    Proteomic databases

    MaxQBi P51601.
    PaxDbi P51601.
    PeptideAtlasi P51601.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR267C ; YGR267C ; YGR267C .
    GeneIDi 853183.
    KEGGi sce:YGR267C.

    Organism-specific databases

    CYGDi YGR267c.
    SGDi S000003499. FOL2.

    Phylogenomic databases

    eggNOGi COG0302.
    GeneTreei ENSGT00390000013481.
    HOGENOMi HOG000221222.
    KOi K01495.
    OMAi VRDIEIY.
    OrthoDBi EOG7QRR5W.

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .
    BioCyci YEAST:YGR267C-MONOMER.
    Reactomei REACT_189008. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

    Miscellaneous databases

    NextBioi 973323.
    PROi P51601.

    Gene expression databases

    Genevestigatori P51601.

    Family and domain databases

    HAMAPi MF_00223. FolE.
    InterProi IPR001474. GTP_CycHdrlase_I.
    IPR018234. GTP_CycHdrlase_I_CS.
    IPR020602. GTP_CycHdrlase_I_dom.
    [Graphical view ]
    PANTHERi PTHR11109. PTHR11109. 1 hit.
    Pfami PF01227. GTP_cyclohydroI. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00063. folE. 1 hit.
    PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Witter K., Guetlich M., Stucka R., Ziegler I., Bacher A.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: C836.
    2. "Disruption of the GTP-cyclohydrolase I gene in Saccharomyces cerevisiae."
      Nardese V., Gutlich M., Brambilla A., Agostoni Carbone M.L.
      Biochem. Biophys. Res. Commun. 218:273-279(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "A 9359 bp fragment from the right arm of Saccharomyces cerevisiae chromosome VII includes the FOL2 and YTA7 genes and three unknown open reading frames."
      Agostoni Carbone M.L., Lucchini G., Melchioretto P., Nardese V., Vanoni M., Panzeri L.
      Yeast 14:587-591(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers."
      Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.
      Biochem. Biophys. Res. Commun. 212:705-711(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-208.
      Strain: ATCC 204508 / S288c.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 THR-15 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGCH1_YEAST
    AccessioniPrimary (citable) accession number: P51601
    Secondary accession number(s): D6VV45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2840 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3