ID GCH1_MANSM Reviewed; 218 AA. AC Q65TR0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 106. 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}; OrderedLocusNames=MS1043; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Basfia. OX NCBI_TaxID=221988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBEL55E; RX PubMed=15378067; DOI=10.1038/nbt1010; RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., RA Jeong H., Hur C.G., Kim J.J.; RT "The genome sequence of the capnophilic rumen bacterium Mannheimia RT succiniciproducens."; RL Nat. Biotechnol. 22:1275-1281(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}. 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; AE016827; AAU37650.1; -; Genomic_DNA. DR RefSeq; WP_011200219.1; NC_006300.1. DR AlphaFoldDB; Q65TR0; -. DR SMR; Q65TR0; -. DR STRING; 221988.MS1043; -. DR KEGG; msu:MS1043; -. DR eggNOG; COG0302; Bacteria. DR HOGENOM; CLU_049768_3_2_6; -. DR OrthoDB; 9801207at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000000607; 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..218 FT /note="GTP cyclohydrolase 1" FT /id="PRO_1000043706" 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; 25029 MW; B5CDDD0FB03FF1A6 CRC64; MSRISAEAEK VRHALIEKGI ETPMIALTKS KNERRIGIEN RMREVMQLIG LDLTDDSLEE TPVRLAKMFI DEIFSGLDYT NFPKITNIEN RMKVSEMVLV NDVTLTSTCE HHFVTIDGLV SVAYYPKKWV IGLSKINRVV QFFAQRPQVQ ERLTEQILLA FQTILETEDV AVYMKATHFC VKCRGIKDTN SYTVTSAFGG VFLEDRETRK EFLSLINK //