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InterPro: IPR018234 GTP cyclohydrolase I, conserved site

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1524 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR018234 GTP_CycHdrlase_I_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00859	GTP_CYCLOHYDROL_1_1	1448
PROSITE pattern	PS00860	GTP_CYCLOHYDROL_1_2	1238
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001474 GTP cyclohydrolase I
IPR020602 GTP cyclohydrolase I/Nitrile oxidoreductase

GO Term annotation Help

Process

GO:0046654 tetrahydrofolate biosynthetic process

Function

GO:0003934 GTP cyclohydrolase I activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

GTP cyclohydrolase I (EC:3.5.4.16) catalyses the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. 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 [1].

Structural links Help

PDB - click here

SCOP: d.96.1.1

CATH: 3.30.1130.10

Database links Help

Enzyme: EC:3.5.4.16

CluSTr: ALLvsALL:4745:40.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018234

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P30793 GTP cyclohydrolase 1

P48596 GTP cyclohydrolase 1

P51601 GTP cyclohydrolase 1

Q05915 GTP cyclohydrolase 1

Q19980 GTP cyclohydrolase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001474	GTP cyclohydrolase I
IPR020602	GTP cyclohydrolase I/Nitrile oxidoreductase
IPR018234	GTP cyclohydrolase I, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Maier J, Witter K, Gutlich M, Ziegler I, Werner T, Ninnemann H. Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers. Biochem. Biophys. Res. Commun. 212 705-11 1995 [PubMed: 7542887] http://dx.doi.org/10.1006/bbrc.1995.2026

Additional Reading Open in usermanual
	Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A. Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proc. Natl. Acad. Sci. U.S.A. 97 2000 13567-72 [PubMed: 11087827] http://dx.doi.org/10.1073/pnas.240463497
	Rebelo J, Auerbach G, Bader G, Bracher A, Nar H, Hosl C, Schramek N, Kaiser J, Bacher A, Huber R, Fischer M. Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I. J. Mol. Biol. 326 2003 503-16 [PubMed: 12559918] http://dx.doi.org/10.1016/S0022-2836(02)01303-7
	Nar H, Huber R, Meining W, Schmid C, Weinkauf S, Bacher A. Atomic structure of GTP cyclohydrolase I. Structure 3 1995 459-66 [PubMed: 7663943] http://dx.doi.org/10.1016/S0969-2126(01)00179-4
	Maita N, Hatakeyama K, Okada K, Hakoshima T. Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein. J. Biol. Chem. 279 2004 51534-40 [PubMed: 15448133] http://dx.doi.org/10.1074/jbc.M409440200
	Maita N, Okada K, Hatakeyama K, Hakoshima T. Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP. Proc. Natl. Acad. Sci. U.S.A. 99 2002 1212-7 [PubMed: 11818540] http://dx.doi.org/10.1073/pnas.022646999
	Tanaka Y, Nakagawa N, Kuramitsu S, Yokoyama S, Masui R. Novel reaction mechanism of GTP cyclohydrolase I. High-resolution X-ray crystallography of Thermus thermophilus HB8 enzyme complexed with a transition state analogue, the 8-oxoguanine derivative. J. Biochem. 138 2005 263-75 [PubMed: 16169877] http://dx.doi.org/10.1093/jb/mvi120

InterPro 23.1