ID   GCH1_CAMJE              Reviewed;         190 AA.
AC   P51594; Q0PBU5; Q9PIT5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 131.
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; OrderedLocusNames=Cj0194;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=7670637; DOI=10.1099/13500872-141-6-1359;
RA   Griffiths P.L., Park R.W.A., Connerton I.F.;
RT   "The gene for Campylobacter trigger factor: evidence for multiple
RT   transcription start sites and protein products.";
RL   Microbiology 141:1359-1367(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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: Toroid-shaped homodecamer, composed of two pentamers of five
CC       dimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA59929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X85954; CAA59929.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL111168; CAL34363.1; -; Genomic_DNA.
DR   PIR; A81438; A81438.
DR   PIR; I40754; I40754.
DR   RefSeq; WP_002851990.1; NC_002163.1.
DR   RefSeq; YP_002343652.1; NC_002163.1.
DR   AlphaFoldDB; P51594; -.
DR   SMR; P51594; -.
DR   IntAct; P51594; 1.
DR   STRING; 192222.Cj0194; -.
DR   PaxDb; 192222-Cj0194; -.
DR   EnsemblBacteria; CAL34363; CAL34363; Cj0194.
DR   GeneID; 904536; -.
DR   KEGG; cje:Cj0194; -.
DR   PATRIC; fig|192222.6.peg.191; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_3_1_7; -.
DR   OrthoDB; 9801207at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00642; GTP_cyclohydro1; 1.
DR   Gene3D; 1.10.286.10; -; 1.
DR   Gene3D; 3.30.1130.10; -; 1.
DR   HAMAP; MF_00223; FolE; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR043134; GTP-CH-I_N.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR   InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR   NCBIfam; TIGR00063; folE; 1.
DR   PANTHER; PTHR11109:SF7; GTP CYCLOHYDROLASE 1; 1.
DR   PANTHER; PTHR11109; GTP CYCLOHYDROLASE I; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Reference proteome; Zinc.
FT   CHAIN           1..190
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_0000119393"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  21800 MW;  24B4CC39BEA49564 CRC64;
     MQKKFEDCVK TMLEIIGENP NREGLIKTPN RVFKAYEFLT SGYTQNVKEI LNDALFESSN
     NEMVLVRDIE FYSLCEHHLL PFFGRAHVAY IPNKKVVGLS KIPRLVEVFA RRLQIQEQLT
     EQIAQALMEN VDAKGVGVVI EARHMCVEMR GVQKANSTTT TSALRGIFLK NEKTREEFFS
     LINSAKQVRF
//