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Protein

GTP cyclohydrolase 1

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

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi4 – 41ZincBy similarity
Metal bindingi7 – 71ZincBy similarity
Metal bindingi75 – 751ZincBy similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTP cyclohydrolase I activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. tetrahydrobiopterin biosynthetic process Source: UniProtKB-KW
  3. tetrahydrofolate biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Tetrahydrobiopterin 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
OrganismiEuglena gracilis
Taxonomic identifieri3039 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaEuglenidaEuglenalesEuglenaceaeEuglena

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›80›80GTP cyclohydrolase 1PRO_0000119484Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP51597.
SMRiP51597. Positions 1-80.
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]
PROSITEiPS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P51597-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
FSMCEHHMLP FWGKVHIAYI PKGKVLGLSK LARVAEMYAR RLQVQERLTR
60 70 80
QIASAIERSI QPLGVAVVVD CCHMCMVMRG
Length:80
Mass (Da):9,097
Last modified:October 1, 1996 - v1
Checksum:i8C46A15D01A7B8C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei80 – 801

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49757 mRNA. Translation: CAA89827.1.
PIRiS54909.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49757 mRNA. Translation: CAA89827.1.
PIRiS54909.

3D structure databases

ProteinModelPortaliP51597.
SMRiP51597. Positions 1-80.
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]
PROSITEiPS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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: Z / ATCC 12894.

Entry informationi

Entry nameiGCH1_EUGGR
AccessioniPrimary (citable) accession number: P51597
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

External Data

Dasty 3

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 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.