AC   MF_00223;
DC   Protein; auto
TR   HAMAP; MF_00223; -; 1; level=0
XX
Names: FolE
XX
ID   GCH1
DE   RecName: Full=GTP cyclohydrolase 1;
DE            EC=3.5.4.16;
DE   AltName: Full=GTP cyclohydrolase I;
DE            Short=GTP-CH-I;
GN   Name=folE;
XX
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   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC   -!- SUBUNIT: Homopolymer.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
XX
DR   Pfam; PF01227; GTP_cyclohydroI; 1; trigger=no
DR   NCBIfam; TIGR00063; FolE; 1; trigger=no
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1; trigger=no
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1; trigger=no
XX
KW   GTP-binding
KW   Nucleotide-binding
KW   One-carbon metabolism
KW   Hydrolase
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
GO   GO:0003934; F:GTP cyclohydrolase I activity
case <FTGroup:1>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0006730; P:one-carbon metabolic process
GO   GO:0046654; P:tetrahydrofolate biosynthetic process
XX
FT   From: GCH1_ECOLI (P0A6T5)
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
XX
Size: 180-235;
Related: None;
Template: P0A6T5; P19465;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: MF_xxxxx (folK)
 Cter: None
Duplicate: in NOSS1, PSEAE, PSEPK, PSESM
Plasmid: None
Comments: The GTP cyclohydrolases of this family share the same function as the bacterial
 GTP cyclohydrolases of the MF_01527 family (GTP cyclohydrolases folE2), without having
 any sequence homology.
XX
# Revision 1.41 2023/06/01
//