ID   GCH1_BACPU              Reviewed;          46 AA.
AC   P48063;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
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;
GN   Name=folE; Synonyms=mtrA;
OS   Bacillus pumilus (Bacillus mesentericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7836324; DOI=10.1128/jb.177.3.839-842.1995;
RA   Hoffman R.J., Gollnick P.;
RT   "The mtrB gene of Bacillus pumilus encodes a protein with sequence and
RT   functional homology to the trp RNA-binding attenuation protein (TRAP) of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 177:839-842(1995).
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: Homomer.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR   EMBL; L37879; AAA67543.1; -; Genomic_DNA.
DR   PIR; I39904; I39904.
DR   AlphaFoldDB; P48063; -.
DR   SMR; P48063; -.
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:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1130.10; -; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Zinc.
FT   CHAIN           <1..46
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_0000119385"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   46 AA;  4895 MW;  5C9717AB39019634 CRC64;
     VEAEHMCMTM RGVKKPGAKT VTSAVRGTFA NVAAARAEVL SFIKND