P51596 (GCH1_ONCMY) 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:

gch1

Organism

Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)

Taxonomic identifier

8022 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Actinopterygii › Actinopteri › Neopterygii › Teleostei › Elopocephala › Clupeocephala › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonoidei › Salmonidae › Salmoninae › Oncorhynchus

Protein attributes

Sequence length	225 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May positively regulate nitric oxide synthesis in endothelial cells. May be involved in dopamine synthesis. May modify pain sensitivity and persistence By similarity.
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. Zinc is required for catalytic activity. Inhibited by Mg2+ 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.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the GTP cyclohydrolase I family.

Ontologies

Keywords
Biological process	Tetrahydrobiopterin biosynthesis
Cellular component	Cytoplasm Nucleus
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 tetrahydrobiopterin 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: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – ›225	›225	GTP cyclohydrolase 1		PRO_0000119479
Sites
	Metal binding	149	1	Zinc By similarity
	Metal binding	152	1	Zinc By similarity
	Metal binding	220	1	Zinc By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	225	1

Sequences

	Sequence		Length	Mass (Da)
	P51596 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 57DA39D5664887D8	FASTA	225	25,168
	10 20 30 40 50 60 MERSKQSHDN QADSRPTTNE SSLNGHFDGL VKKTPGMWDV KGRGTAGESS SHTGSSVVEN 70 80 90 100 110 120 WKHERTRSIE DNEMSLPSLA AAYTTIIRGL GKDPQRQGLL KTPWRAATAM QFFTKGYQEK 130 140 150 160 170 180 IIDVLNDAIL DEDHDEMVIV KDIDMFSMCE HHLVPIFGRV HIGYLPNKRV LGLSKLARIV 190 200 210 220 EIYSRRLQVQ ERLTKQIAVA ITEALQPAGV GVVIEATHMC MVMRG

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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49707 mRNA. Translation: CAA89809.1.
UniGene	Omy.11719.
3D structure databases
ProteinModelPortal	P51596.
SMR	P51596. Positions 65-225.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG003136.
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...

Entry information

Entry name

GCH1_ONCMY

Accession

Primary (citable) accession number: P51596

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program