GTP cyclohydrolase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P51601 (GCH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GTP cyclohydrolase 1
EC=3.5.4.16

Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I

Gene names

Name:	FOL2
Ordered Locus Names:	YGR267C
ORF Names:	G9349

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.
Catalytic activity	GTP + H₂O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
Enzyme regulation	GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity By similarity.
Pathway	Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
Subunit structure	Toroid-shaped homodecamer, composed of two pentamers of five dimers By similarity.
Miscellaneous	Present with 2840 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the GTP cyclohydrolase I family.

Ontologies

Keywords
Biological process	Folate biosynthesis
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7,8-dihydroneopterin 3'-triphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW folic acid-containing compound biosynthetic process Inferred from mutant phenotype Ref.2. Source: SGD tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276 PubMed 14562095. Source: SGD nucleus Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase I activity Inferred from mutant phenotype Ref.2. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 243

243

GTP cyclohydrolase 1

PRO_0000119489

Sites

Metal binding

132

Zinc By similarity

Metal binding

135

Zinc By similarity

Metal binding

203

Zinc By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.9 Ref.10 Ref.11

Modified residue

Phosphothreonine Ref.10 Ref.11

Modified residue

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

Phosphotyrosine Ref.11

Experimental info

Sequence conflict

159 – 160

LA → QG in CAA89826. Ref.7

Sequence conflict

206

S → M in CAA89826. Ref.7

Sequence conflict

217

V → A in CAA87397. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P51601 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A71AB8750AECD3F6
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FASTA

243

27,769

        10         20         30         40         50         60 
MHNIQLVQEI ERHETPLNIR PTSPYTLNPP VERDGFSWPS VGTRQRAEET EEEEKERIQR 

        70         80         90        100        110        120 
ISGAIKTILT ELGEDVNREG LLDTPQRYAK AMLYFTKGYQ TNIMDDVIKN AVFEEDHDEM 

       130        140        150        160        170        180 
VIVRDIEIYS LCEHHLVPFF GKVHIGYIPN KKVIGLSKLA RLAEMYARRL QVQERLTKQI 

       190        200        210        220        230        240 
AMALSDILKP LGVAVVMEAS HMCMVSRGIQ KTGSSTVTSC MLGGFRAHKT REEFLTLLGR 


RSI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] 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]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Strain: ADR376.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; THR-22 AND SER-23, MASS SPECTROMETRY.
[11]	"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; THR-22; SER-23 AND TYR-25, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	JC4585.
RefSeq	NP_011783.1. NM_001181396.1.
3D structure databases
ProteinModelPortal	P51601.
SMR	P51601. Positions 50-238.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1318N.
IntAct	P51601. 15 interactions.
MINT	MINT-389985.
STRING	4932.YGR267C.
Proteomic databases
PaxDb	P51601.
PeptideAtlas	P51601.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR267C; YGR267C; YGR267C.
GeneID	853183.
KEGG	sce:YGR267C.
Organism-specific databases
CYGD	YGR267c.
SGD	S000003499. FOL2.
Phylogenomic databases
eggNOG	COG0302.
GeneTree	ENSGT00390000013481.
HOGENOM	HOG000221222.
KO	K01495.
OMA	LIRHQPA.
OrthoDB	EOG4643MV.
Enzyme and pathway databases
UniPathway	UPA00848; UER00151.
Gene expression databases
Genevestigator	P51601.
GermOnline	YGR267C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view]
PANTHER	PTHR11109. PTHR11109. 1 hit.
Pfam	PF01227. GTP_cyclohydroI. 1 hit. [Graphical view]
TIGRFAMs	TIGR00063. folE. 1 hit.
PROSITE	PS00859. GTP_CYCLOHYDROL_1_1. 1 hit. PS00860. GTP_CYCLOHYDROL_1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973323.

Entry information

Entry name

GCH1_YEAST

Accession

Primary (citable) accession number: P51601
Secondary accession number(s): D6VV45

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents