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Protein

GTP cyclohydrolase 1

Gene

FOL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Pathway:i7,8-dihydroneopterin triphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP.
Proteins known to be involved in this subpathway in this organism are:
  1. GTP cyclohydrolase 1 (FOL2)
This subpathway is part of the pathway 7,8-dihydroneopterin triphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP, the pathway 7,8-dihydroneopterin triphosphate biosynthesis and in Cofactor biosynthesis.

Sites

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

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • GTP cyclohydrolase I activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

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_342867. 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 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR267c.
EuPathDBiFungiDB:YGR267C.
SGDiS000003499. FOL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

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.

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.
InParanoidiP51601.
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

        10         20         30         40         50
MHNIQLVQEI ERHETPLNIR PTSPYTLNPP VERDGFSWPS VGTRQRAEET
60 70 80 90 100
EEEEKERIQR ISGAIKTILT ELGEDVNREG LLDTPQRYAK AMLYFTKGYQ
110 120 130 140 150
TNIMDDVIKN AVFEEDHDEM VIVRDIEIYS LCEHHLVPFF GKVHIGYIPN
160 170 180 190 200
KKVIGLSKLA RLAEMYARRL QVQERLTKQI AMALSDILKP LGVAVVMEAS
210 220 230 240
HMCMVSRGIQ KTGSSTVTSC MLGGFRAHKT REEFLTLLGR RSI
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 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP51601.
PaxDbiP51601.
PeptideAtlasiP51601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYGR267c.
EuPathDBiFungiDB:YGR267C.
SGDiS000003499. FOL2.

Phylogenomic databases

eggNOGiCOG0302.
GeneTreeiENSGT00390000013481.
HOGENOMiHOG000221222.
InParanoidiP51601.
KOiK01495.
OMAiVRDIEIY.
OrthoDBiEOG7QRR5W.

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.
BioCyciYEAST:YGR267C-MONOMER.
ReactomeiREACT_342867. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

Miscellaneous databases

NextBioi973323.
PROiP51601.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 134 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

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 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.