ID GCH1_HAEDU Reviewed; 218 AA. AC Q7VM90; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 116. 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=HD_1103; OS Haemophilus ducreyi (strain 35000HP / ATCC 700724). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=233412; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35000HP / ATCC 700724; RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., RA Nguyen D., Wang J., Forst C., Hood L.; RT "The complete genome sequence of Haemophilus ducreyi."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017143; AAP95969.1; -; Genomic_DNA. DR RefSeq; WP_010945018.1; NC_002940.2. DR AlphaFoldDB; Q7VM90; -. DR SMR; Q7VM90; -. DR STRING; 233412.HD_1103; -. DR KEGG; hdu:HD_1103; -. DR eggNOG; COG0302; Bacteria. DR HOGENOM; CLU_049768_3_2_6; -. DR OrthoDB; 9801207at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000001022; 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..218 FT /note="GTP cyclohydrolase 1" FT /id="PRO_0000119410" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223" SQ SEQUENCE 218 AA; 25050 MW; C21BBE869CB5A9B6 CRC64; MSIISSEAQK VRQALIKKGI ETPTIELTQD KDSRRAEIQQ HMRSVLELLG LDLRDDSLEE TPHRLAKMYV DEIFSGLDYA TFPKITTIEN RMKVSEMVLV DDITLTSTCE HHFVTIDGKV AVAYYPKKWV IGLSKINRVV QFFAQRPQVQ ERFTEQILTA FQTILETEDV AIYVKATHFC VKCRGIKDSN SYTVTSAFGG VFLDDRETRK EFLNLIHK //