ID GCH1_LISMC Reviewed; 189 AA. AC C1KWN3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 67. 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=Lm4b_01950; OS Listeria monocytogenes serotype 4b (strain CLIP80459). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=568819; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIP80459; RX PubMed=22530965; DOI=10.1186/1471-2164-13-144; RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., RA Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P., RA Rusniok C., Buchrieser C., Goebel W., Chakraborty T.; RT "Comparative genomics and transcriptomics of lineages I, II, and III RT strains of Listeria monocytogenes."; RL BMC Genomics 13:144-144(2012). 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; FM242711; CAS05708.1; -; Genomic_DNA. DR RefSeq; WP_003727998.1; NC_012488.1. DR AlphaFoldDB; C1KWN3; -. DR SMR; C1KWN3; -. DR KEGG; lmc:Lm4b_01950; -. DR HOGENOM; CLU_049768_3_3_9; -. 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 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..189 FT /note="GTP cyclohydrolase 1" FT /id="PRO_1000204290" 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 //