P51601 (GCH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

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)

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. Ref.8
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	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. 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	1	Zinc By similarity
	Metal binding	135	1	Zinc By similarity
	Metal binding	203	1	Zinc By similarity
Amino acid modifications
	Modified residue	15	1	Phosphothreonine Ref.9 Ref.10 Ref.11
	Modified residue	22	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	23	1	Phosphoserine Ref.9 Ref.10 Ref.11
	Modified residue	25	1	Phosphotyrosine Ref.11
Experimental info
	Sequence conflict	159 – 160	2	LA → QG in CAA89826. Ref.7
	Sequence conflict	206	1	S → M in CAA89826. Ref.7
	Sequence conflict	217	1	V → A in CAA87397. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51601 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: A71AB8750AECD3F6	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

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: 8573145] [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: 9605509] [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: 9169869] [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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [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: 7542887] [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: 14562106] [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: 17330950] [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: 17563356] [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: 18407956] [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. 17 interactions.
MINT	MINT-389985.
STRING	P51601.
Proteomic databases
PeptideAtlas	P51601.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR267C; YGR267C; YGR267C.
GeneID	853183.
KEGG	sce:YGR267C.
NMPDR	fig|4932.3.peg.2912.
Organism-specific databases
CYGD	YGR267c.
SGD	S000003499. FOL2.
Phylogenomic databases
eggNOG	fuNOG07690.
GeneTree	EFGT00050000006867.
HOGENOM	HBG370191.
OMA	LPFMGRA.
OrthoDB	EOG4643MV.
Gene expression databases
ArrayExpress	P51601.
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]
KO	K01495.
PANTHER	PTHR11109. GTP_cyclohydro_I. 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:	December 14, 2011
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program