ID GCH1_PECCP Reviewed; 220 AA. AC C6DEM6; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 04-NOV-2026, entry version 80. 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=PC1_1670; OS Pectobacterium carotovorum subsp. carotovorum (strain PC1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=561230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PC1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."; RL Submitted (JUL-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; CP001657; ACT12711.1; -; Genomic_DNA. DR RefSeq; WP_005967317.1; NC_012917.1. DR AlphaFoldDB; C6DEM6; -. DR SMR; C6DEM6; -. DR STRING; 561230.PC1_1670; -. DR PaxDb; 561230-PC1_1670; -. DR GeneID; 90763075; -. DR KEGG; pct:PC1_1670; -. DR eggNOG; COG0302; Bacteria. DR HOGENOM; CLU_049768_3_2_6; -. DR OMA; AAHRKHE; -. DR OrthoDB; 9801207at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000002736; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005525; F:GTP binding; IEA:TreeGrafter. 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:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:TreeGrafter. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 1.10.286.10:FF:000002; GTP cyclohydrolase 1; 1. DR FunFam; 3.30.1130.10:FF:000001; GTP cyclohydrolase 1; 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; NF006824; folE; 1. DR NCBIfam; NF006826; folE; 1. 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; Reference proteome; Zinc. FT CHAIN 1..220 FT /note="GTP cyclohydrolase 1" FT /id="PRO_1000204291" 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; 24570 MW; 5F322C69FB19FE5B CRC64; MSSLSKEAVM VHEALLARGL ETPLRGALLD RDTRKQRIAE HMTEIMNLLS LDLSDDSLAE TPTRIAKMYV DEIFSGLDYA NFPKITIIEN KMKVDEMVTV RDITLTSTCE HHFVTIDGKA TVAYIPKDGV IGLSKLNRIV QFFSQRPQVQ ERLTQQILVA LQTLLGTNNV AVSIDAVHYC VKARGIRDAT SATTTTSLGG LFKSSQNTRQ EFLRAVRHHN //