ID GCH4_EXIS2 Reviewed; 301 AA. AC B1YHT1; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527}; DE EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527}; GN Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527}; GN OrderedLocusNames=Exig_0229; OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 / OS 255-15). OC Bacteria; Bacillota; Bacilli; Bacillales; OC Bacillales Family XII. Incertae Sedis; Exiguobacterium. OX NCBI_TaxID=262543; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01527}. 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_01527}; 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_01527}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. CC {ECO:0000255|HAMAP-Rule:MF_01527}. 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; CP001022; ACB59715.1; -; Genomic_DNA. DR RefSeq; WP_012369140.1; NC_010556.1. DR AlphaFoldDB; B1YHT1; -. DR SMR; B1YHT1; -. DR STRING; 262543.Exig_0229; -. DR KEGG; esi:Exig_0229; -. DR eggNOG; COG1469; Bacteria. DR HOGENOM; CLU_062816_1_1_9; -. DR OrthoDB; 9774824at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000001681; Chromosome. DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule. DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.10.270.10; Urate Oxidase; 1. DR HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1. DR InterPro; IPR022838; GTP_cyclohydrolase_FolE2. DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA. DR PANTHER; PTHR36445; GTP CYCLOHYDROLASE MPTA; 1. DR PANTHER; PTHR36445:SF1; GTP CYCLOHYDROLASE MPTA; 1. DR Pfam; PF02649; GCHY-1; 1. PE 3: Inferred from homology; KW Hydrolase; Reference proteome. FT CHAIN 1..301 FT /note="GTP cyclohydrolase FolE2" FT /id="PRO_0000372028" FT SITE 183 FT /note="May be catalytically important" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527" SQ SEQUENCE 301 AA; 34076 MW; E87B3E9FECA72F7D CRC64; MSTYPVTLPT KEERHKLFGS VPPIKGTKPT EKDKMIDLQN TPKNFLFALD AVGISNVKHP VVIQDGETTQ ATIATFELST SLVQDRKGIN MSRLTEQLDQ YHNEGWVVTN ESLIQFAREL AERMEQSEGQ LTIRYPWFFT RKAPATGLSG LMNAEVWQTV SVNTETNEAT LSVGLTINVT TLCPCSKEIS EYSAHNQRGY VTMEASLRDE ADDFNWKQEL LDAAESNASA PLHPVLKRPD EKRVTEMAYE NPRFVEDMVR LIAADLYEMD PIASFFVECR NEETIHQHDA IARITFDKDA Q //