ID GCH41_DECAR Reviewed; 266 AA. AC Q47IT5; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=GTP cyclohydrolase FolE2 1 {ECO:0000255|HAMAP-Rule:MF_01527}; DE EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527}; GN Name=folE2-1 {ECO:0000255|HAMAP-Rule:MF_01527}; GN OrderedLocusNames=Daro_0489; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae; OC Dechloromonas. OX NCBI_TaxID=159087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCB; RX PubMed=19650930; DOI=10.1186/1471-2164-10-351; RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., RA Lapidus A.; RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: RT indications of a surprisingly complex life-style and cryptic anaerobic RT pathways for aromatic degradation."; RL BMC Genomics 10:351-351(2009). 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; CP000089; AAZ45246.1; -; Genomic_DNA. DR AlphaFoldDB; Q47IT5; -. DR SMR; Q47IT5; -. DR STRING; 159087.Daro_0489; -. DR KEGG; dar:Daro_0489; -. DR eggNOG; COG1469; Bacteria. DR HOGENOM; CLU_062816_1_1_4; -. DR OrthoDB; 9774824at2; -. DR UniPathway; UPA00848; UER00151. 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. FT CHAIN 1..266 FT /note="GTP cyclohydrolase FolE2 1" FT /id="PRO_0000289488" FT SITE 154 FT /note="May be catalytically important" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527" SQ SEQUENCE 266 AA; 29695 MW; 33614D3D050A5D12 CRC64; MNAPENIFLP DVQAAADTRR LAIQSVGVKG LRYPLQLENA AGELTSTVAT FAMSVGLPPE VKGTHMSRFV ELLEARTGPL TQVGLLRMMA DMLLRLDASS GRIELAFPYF IRKMAPVSGV ESLLDYDATL IVDQRAWESA TLTLRVVAPV TSLCPCSKKI SDYGAHNQRS HITLEARLRS PMSIEDLVRI AEEEASCEVF GLLKRPDEKW VTERAYDNPK FVEDLVRDIA LRLMNEPRIA EWKVASENFE SIHNHSAYAE LYGCNE //