GCH1_PHYBL
ID GCH1_PHYBL Reviewed; 94 AA.
AC P51600;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=GTP cyclohydrolase 1;
DE EC=3.5.4.16;
DE AltName: Full=GTP cyclohydrolase I;
DE Short=GTP-CH-I;
DE Flags: Fragment;
OS Phycomyces blakesleeanus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=4837;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DSM 62921 / CBS 283.35 / IMB 7212;
RX PubMed=7542887; DOI=10.1006/bbrc.1995.2026;
RA Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.;
RT "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes
RT by reverse-transcription polymerase chain reaction using a general set of
RT degenerate primers.";
RL Biochem. Biophys. Res. Commun. 212:705-711(1995).
CC -!- FUNCTION: GTP cyclohydrolase 1 is the first enzyme in the biosynthetic
CC pathway leading to folic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC -!- ACTIVITY REGULATION: GTP shows a positive allosteric effect, and
CC tetrahydrobiopterin inhibits the enzyme activity. {ECO:0000250}.
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC dimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; Z49760; CAA89830.1; -; mRNA.
DR PIR; S54910; S54910.
DR AlphaFoldDB; P51600; -.
DR SMR; P51600; -.
DR VEuPathDB; FungiDB:PHYBL_112460; -.
DR UniPathway; UPA00848; UER00151.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1130.10; -; 1.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR001474; GTP_CycHdrlase_I.
DR InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR PANTHER; PTHR11109; PTHR11109; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 1.
DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Folate biosynthesis; GTP-binding; Hydrolase;
KW Metal-binding; Nucleotide-binding; Zinc.
FT CHAIN <1..>94
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119487"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 94
SQ SEQUENCE 94 AA; 10586 MW; 4F8C12A0407A65DD CRC64;
EDHDEMVIVK DVDIFSLCEH HKVPSTGKIS IGYIPNRRVV GLSKLARIAE MFSRRLQVQE
RLTKQVATAL MEILQPQGVA VVVECSHLCM VMRG
