ID   GCH1_LISMF              Reviewed;         189 AA.
AC   Q71Y82;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=GTP cyclohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I {ECO:0000255|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I {ECO:0000255|HAMAP-Rule:MF_00223};
GN   Name=folE {ECO:0000255|HAMAP-Rule:MF_00223};
GN   OrderedLocusNames=LMOf2365_1962;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00223};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00223}.
CC   -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC       dimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000255|HAMAP-Rule:MF_00223}.
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DR   EMBL; AE017262; AAT04732.1; -; Genomic_DNA.
DR   RefSeq; WP_003727998.1; NC_002973.6.
DR   AlphaFoldDB; Q71Y82; -.
DR   SMR; Q71Y82; -.
DR   KEGG; lmf:LMOf2365_1962; -.
DR   HOGENOM; CLU_049768_3_3_9; -.
DR   OMA; CEHMCMS; -.
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-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   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   PANTHER; PTHR11109; PTHR11109; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   TIGRFAMs; TIGR00063; folE; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Zinc.
FT   CHAIN           1..189
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_0000119420"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
SQ   SEQUENCE   189 AA;  21335 MW;  B79E2F50764A1B91 CRC64;
     MEQIDKQKIA DAVKVILEAV GENPEREGLI DTPMRVARMY EEVFAGLKKD PSVHFDTIFE
     EQHEELVLVK DIRFSSMCEH HLVPFFGVAH VAYLPQNGRV AGLSKLARVV DDVSRRPQLQ
     ERITTTVAEI MMEKLKPLGV MVIMEAEHMC MTIRGVNKPG TKTITSAVRG AFKNDDKLRS
     EVLALIKHN