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P50141 (GCH1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase 1

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I
Gene names
Name:GCH1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence 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. HAMAP-Rule MF_00223

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_00223

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. HAMAP-Rule MF_00223

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_00223

Subunit structure

Toroid-shaped homodecamer, composed of two pentamers of five dimers By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_00223.

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119477

Sites

Metal binding1271Zinc By similarity
Metal binding1301Zinc By similarity
Metal binding1981Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
P50141 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F235D56B991D8C24

FASTA23626,115
        10         20         30         40         50         60 
MAAARSCNGY ARREGPPSPK LGTEKPRVSA GSGGSGDGWR GERPRSEEDN ELSLPSLAAA 

        70         80         90        100        110        120 
YTTILRALGE DPERQGLLKT PWRAATAMQF FTKGYQETIA DVLNDAIFDE DHDEMVIVKN 

       130        140        150        160        170        180 
IDMFSLCEHH LVPFVGKVHI GYLPNKQVLG LSKLARIVEI YSRRLQVQER LTKQIAIAIT 

       190        200        210        220        230 
EALQPAGVGV VIEATHMCMV MRGVQKMNSK TATSTMLGVF REDPKTREEF LTLIRS 

« Hide

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].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49267 mRNA. Translation: CAA89261.1.
PIRI50646.
RefSeqNP_990554.1. NM_205223.1.
UniGeneGga.674.

3D structure databases

ProteinModelPortalP50141.
SMRP50141. Positions 43-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000019895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396146.
KEGGgga:396146.

Organism-specific databases

CTD2643.

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
HOVERGENHBG003136.
InParanoidP50141.
KOK01495.
PhylomeDBP50141.

Enzyme and pathway databases

UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_00223. FolE.
InterProIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERPTHR11109. PTHR11109. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsTIGR00063. folE. 1 hit.
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816203.
PROP50141.

Entry information

Entry nameGCH1_CHICK
AccessionPrimary (citable) accession number: P50141
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways