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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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Folate biosynthesis

Keywords - Ligandi

GTP-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 lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesPhycomycetaceaePhycomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase I family.Curated

Family and domain databases

InterProiIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP51600.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.

Family and domain databases

InterProiIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGCH1_PHYBL
AccessioniPrimary (citable) accession number: P51600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 5, 2016
This is version 69 of the entry and version 1 of the sequence. [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

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.