O13774 (GCH1_SCHPO) 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

ORF Names:

SPAC17A5.13

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	235 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.
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 sequence orthology. Source: PomBase tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase I activity Inferred from sequence orthology. Source: PomBase 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 – 235	235	GTP cyclohydrolase 1		PRO_0000119488
Sites
	Metal binding	125	1	Zinc By similarity
	Metal binding	128	1	Zinc By similarity
	Metal binding	196	1	Zinc By similarity
Amino acid modifications
	Modified residue	25	1	Phosphothreonine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O13774 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: B0050C358D671E55	FASTA	235	26,493
	10 20 30 40 50 60 MEPGKKDYID SPLRMQPASL SGASTPTIDL DGLSWPCQGT QRRIDTAEEE KVKKISNAIS 70 80 90 100 110 120 TILECLGEDP ERQGLLGTPE RYAKAMLYFT KGYEQNLTEV INEAVFQEDH EEMVIVRDID 130 140 150 160 170 180 VFSLCEHHLV PFIGKIHIGY IPRKRVLGLS KLARIANMFS RRLQVQERLT KQVAQAIQAV 190 200 210 220 230 LKPQGVAVVM EATHMCMVMR GVEKPGSSTV TSSLTGIFQR SHKTREEFFR LIGKF

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB11513.1.
PIR	T37828.
RefSeq	NP_593481.1. NM_001018914.1.
3D structure databases
ProteinModelPortal	O13774.
SMR	O13774. Positions 39-232.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC17A5.13-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC17A5.13.1; SPAC17A5.13.1:pep; SPAC17A5.13.
GeneID	2542406.
KEGG	spo:SPAC17A5.13.
Organism-specific databases
PomBase	SPAC17A5.13.
Phylogenomic databases
eggNOG	COG0302.
HOGENOM	HOG000221222.
KO	K01495.
OMA	LYSVCEH.
OrthoDB	EOG4643MV.
Enzyme and pathway databases
UniPathway	UPA00848; UER00151.
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	20803465.

Entry information

Entry name

GCH1_SCHPO

Accession

Primary (citable) accession number: O13774

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program