P51600 (GCH1_PHYBL) 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
Organism	Phycomyces blakesleeanus
Taxonomic identifier	4837 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Fungi incertae sedis › Early diverging fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Phycomyces

Protein attributes

Sequence length	94 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology

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
Technical term	Allosteric enzyme
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 tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase I activity Inferred from electronic annotation. Source: EC 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 – ›94	›94	GTP cyclohydrolase 1		PRO_0000119487
Sites
	Metal binding	18	1	Zinc By similarity
	Metal binding	21	1	Zinc By similarity
	Metal binding	89	1	Zinc By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	94	1

Sequences

	Sequence		Length	Mass (Da)
	P51600 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4F8C12A0407A65DD	FASTA	94	10,586
	10 20 30 40 50 60 EDHDEMVIVK DVDIFSLCEH HKVPSTGKIS IGYIPNRRVV GLSKLARIAE MFSRRLQVQE 70 80 90 RLTKQVATAL MEILQPQGVA VVVECSHLCM VMRG

References

[1]

"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]. Strain: CBS 283.35.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49760 mRNA. Translation: CAA89830.1.
PIR	S54910.
3D structure databases
ProteinModelPortal	P51600.
SMR	P51600. Positions 1-94.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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]
PROSITE	PS00859. GTP_CYCLOHYDROL_1_1. 1 hit. PS00860. GTP_CYCLOHYDROL_1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCH1_PHYBL

Accession

Primary (citable) accession number: P51600

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program