ID GCH4_DICTD Reviewed; 257 AA. AC B8DZH0; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 71. 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=Dtur_0615; OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310). OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae; OC Dictyoglomus. OX NCBI_TaxID=515635; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6724 / Z-1310; RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979; RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.; RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM RT 6724 reveals a specialized carbohydrate fermentor."; RL Front. Microbiol. 7:1979-1979(2016). 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; CP001251; ACK41903.1; -; Genomic_DNA. DR RefSeq; YP_002352517.1; NC_011661.1. DR AlphaFoldDB; B8DZH0; -. DR SMR; B8DZH0; -. DR STRING; 515635.Dtur_0615; -. DR EnsemblBacteria; ACK41903; ACK41903; Dtur_0615. DR KEGG; dtu:Dtur_0615; -. DR PATRIC; fig|515635.4.peg.652; -. DR eggNOG; COG1469; Bacteria. DR HOGENOM; CLU_062816_1_1_0; -. DR InParanoid; B8DZH0; -. DR OrthoDB; 9808041at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000007719; Chromosome. DR GO; GO:0003933; F:GTP cyclohydrolase activity; IBA:GO_Central. 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..257 FT /note="GTP cyclohydrolase FolE2" FT /id="PRO_1000215389" FT SITE 143 FT /note="May be catalytically important" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527" SQ SEQUENCE 257 AA; 29786 MW; F662CF9D0E55F2BF CRC64; MKDVQNERDY RGIYLRKVGI KNIHWPIKII TKSGEYQSTV ANIDISVDLR EDLRGTHMSR FVEVLNGIDF LHPENLGKIL QEVREKLKAD SSHIKITFPY FIFKKTPVSQ IASPNMIECV IEAELSKKLY MIIGVKVPIH TLCPCSKEIS EYGAHNQRAI AEIYIKSKKL IWFEDLVEIA ERSASAPIYS LLKRPDEKYI TETAYNNPKF VEDVVRDIVS ELEKEPKISW YRVEVTSFES IHNHNAFACV EKGWIKK //