ID GCH1_EDWI9 Reviewed; 220 AA. AC C5BCL9; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 83. 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=NT01EI_1277; OS Edwardsiella ictaluri (strain 93-146). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Hafniaceae; Edwardsiella. OX NCBI_TaxID=634503; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=93-146; RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.; RT "Complete genome sequence of Edwardsiella ictaluri 93-146."; RL Submitted (MAR-2009) 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: Homomer. {ECO:0000255|HAMAP-Rule:MF_00223}. 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; CP001600; ACR68474.1; -; Genomic_DNA. DR RefSeq; WP_015870641.1; NC_012779.2. DR AlphaFoldDB; C5BCL9; -. DR SMR; C5BCL9; -. DR STRING; 67780.B6E78_16640; -. DR GeneID; 69538292; -. DR KEGG; eic:NT01EI_1277; -. DR PATRIC; fig|634503.3.peg.1152; -. DR HOGENOM; CLU_049768_3_2_6; -. DR OrthoDB; 9801207at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000001485; 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 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. 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..220 FT /note="GTP cyclohydrolase 1" FT /id="PRO_1000204287" 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 220 AA; 24617 MW; C994B85ED68E8F57 CRC64; MSSLSKEAAL VHEALLARGL ETPLRGEPLA RDTRKAQIEA HMTEVMRLLN LDLSDDSLVE TPSRIAKMYV DEIFSGLDYA NFPKITIIEN KMDVDEMVTV RDITLTSTCE HHFVTIDGKA TVAYIPKERV IGLSKINRIV RFFAQRPQVQ ERLTQQILVA LQTLLGTKNV AVSIDAVHYC VKARGVRDAT SATTTTSLGG LFKTSQNTRQ EFLRAVRHHV //