SMART: Pfam domain GTP

The domain within your query sequence starts at position 62 and ends at position 240; the E-value for the GTP_cyclohydroI domain shown below is 4e-78.

LAAAYSSILLSLGEDPQRQGLLKTPWRAATAMQYFTKGYQETISDVLNDAIFDEDHDEMV
IVKDIDMFSMCEHHLVPFVGRVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIA
VAITEALQPAGVGVVIEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIR

GTP_cyclohydroI

PFAM accession number:	PF01227
Interpro abstract (IPR020602):	GTP cyclohydrolase I ( EC 3.5.4.16 ) catalyses the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP [ (PUBMED:12559918) ]. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. The comparison of the sequence of the enzyme from bacterial and eukaryotic sources shows that the structure of this enzyme has been extremely well conserved throughout evolution [ (PUBMED:7542887) ]. This entry represents a common fold found in GTP cyclohydrolase I [ (PUBMED:15767583) ].

PFAM accession number:

PF01227

Interpro abstract (IPR020602):

GTP cyclohydrolase I ( EC 3.5.4.16 ) catalyses the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP [ (PUBMED:12559918) ]. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. The comparison of the sequence of the enzyme from bacterial and eukaryotic sources shows that the structure of this enzyme has been extremely well conserved throughout evolution [ (PUBMED:7542887) ].

This entry represents a common fold found in GTP cyclohydrolase I [ (PUBMED:15767583) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GTP_cyclohydroI