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Protein

GTP cyclohydrolase 1

Gene
N/A
Organism
Phycomyces blakesleeanus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.

Catalytic activityi

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

Enzyme regulationi

GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity.By similarity

Pathwayi: 7,8-dihydroneopterin triphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP.
Proteins known to be involved in this subpathway in this organism are:
  1. GTP cyclohydrolase 1
This subpathway is part of the pathway 7,8-dihydroneopterin triphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydroneopterin triphosphate from GTP, the pathway 7,8-dihydroneopterin triphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi18ZincBy similarity1
Metal bindingi21ZincBy similarity1
Metal bindingi89ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processFolate biosynthesis
LigandGTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase 1 (EC:3.5.4.16)
Alternative name(s):
GTP cyclohydrolase I
Short name:
GTP-CH-I
OrganismiPhycomyces blakesleeanus
Taxonomic identifieri4837 [NCBI]
Taxonomic lineageiEukaryotaFungiMucoromycotaMucoromycotinaMucoralesPhycomycetaceaePhycomyces

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000119487‹1 – ›94GTP cyclohydrolase 1Add BLAST›94

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP51600.
SMRiP51600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase I family.Curated

Family and domain databases

InterProiView protein in InterPro
IPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiView protein in Pfam
PF01227. GTP_cyclohydroI. 1 hit.
PROSITEiView protein in PROSITE
PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.

Sequencei

Sequence statusi: Fragment.

P51600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EDHDEMVIVK DVDIFSLCEH HKVPSTGKIS IGYIPNRRVV GLSKLARIAE
60 70 80 90
MFSRRLQVQE RLTKQVATAL MEILQPQGVA VVVECSHLCM VMRG
Length:94
Mass (Da):10,586
Last modified:October 1, 1996 - v1
Checksum:i4F8C12A0407A65DD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei941

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49760 mRNA. Translation: CAA89830.1.
PIRiS54910.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiGCH1_PHYBL
AccessioniPrimary (citable) accession number: P51600
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 15, 2017
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families