P51600 · GCH1_PHYBL

Function

function

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

Catalytic activity

Activity regulation

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

Pathway

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

Features

Showing features for binding site.

194102030405060708090
EDHDEMVIVKDVDIFSLCEHHKVPSTGKISIGYIPNRRVVGLSKLARIAEMFSRRLQVQERLTKQVATALMEILQPQGVAVVVECSHLCMVMRG
TypeIDPosition(s)Description
Binding site18Zn2+ (UniProtKB | ChEBI)
Binding site21Zn2+ (UniProtKB | ChEBI)
Binding site89Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionGTP binding
Molecular FunctionGTP cyclohydrolase I activity
Molecular Functionmetal ion binding
Biological Processfolic acid biosynthetic process
Biological Processtetrahydrofolate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    GTP cyclohydrolase 1
  • EC number
  • Alternative names
    • GTP cyclohydrolase I (GTP-CH-I)

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 62921 / CBS 283.35 / IMB 7212
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Mucoromycetes > Mucorales > Phycomycetaceae > Phycomyces

Accessions

  • Primary accession
    P51600

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001194871-94GTP cyclohydrolase 1

Interaction

Subunit

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

Structure

Family & Domains

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    94
  • Mass (Da)
    10,586
  • Last updated
    1996-10-01 v1
  • Checksum
    4F8C12A0407A65DD
EDHDEMVIVKDVDIFSLCEHHKVPSTGKISIGYIPNRRVVGLSKLARIAEMFSRRLQVQERLTKQVATALMEILQPQGVAVVVECSHLCMVMRG

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue94

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z49760
EMBL· GenBank· DDBJ
CAA89830.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp