ID A0A0A6N339_9THEM Unreviewed; 259 AA. AC A0A0A6N339; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 08-NOV-2023, entry version 29. DE RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000256|HAMAP-Rule:MF_01527}; DE EC=3.5.4.16 {ECO:0000256|HAMAP-Rule:MF_01527}; GN Name=folE2 {ECO:0000256|HAMAP-Rule:MF_01527}; GN ORFNames=Mc24_01968 {ECO:0000313|EMBL:KHC92879.1}; OS Thermotoga sp. Mc24. OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=1231241 {ECO:0000313|EMBL:KHC92879.1, ECO:0000313|Proteomes:UP000030509}; RN [1] {ECO:0000313|EMBL:KHC92879.1, ECO:0000313|Proteomes:UP000030509} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mc24 {ECO:0000313|EMBL:KHC92879.1, RC ECO:0000313|Proteomes:UP000030509}; RA Nesbo C.L., Dlutek M., Marquis P., Bonch-Osmolovskaya E., Ilya K., RA Doolittle F.W.; RT "Genomes of Thermotoga isolates."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. CC {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01527}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. CC {ECO:0000256|HAMAP-Rule:MF_01527}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KHC92879.1}. 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; JSFH01000005; KHC92879.1; -; Genomic_DNA. DR RefSeq; WP_038052083.1; NZ_JSFH01000005.1. DR AlphaFoldDB; A0A0A6N339; -. DR STRING; 1231241.Mc24_01968; -. DR EnsemblBacteria; KHC92879; KHC92879; Mc24_01968. DR PATRIC; fig|1231241.4.peg.395; -. DR eggNOG; COG1469; Bacteria. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000030509; Unassembled WGS sequence. 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:SF1; GTP CYCLOHYDROLASE FOLE2; 1. DR PANTHER; PTHR36445; GTP CYCLOHYDROLASE MPTA; 1. DR Pfam; PF02649; GCHY-1; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01527}. FT SITE 143 FT /note="May be catalytically important" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01527" SQ SEQUENCE 259 AA; 30342 MW; 90684CF86DD40B19 CRC64; MKDVQNEKDP RMVPLKKVGI KDLHWPLKVI LKEDGYQSTV AQISCSVDLH REKRGIHMSR FIEVLNKLEV ITPQIFEEIL DDLIEIMEAK RAHLEIRFPY FIWKESPVSR KKSPLKVDCF VEAEKEKNFS FKIGVRTPVH TLCPCSKEIS DYGAHNQRAF VEITVKTKKF IWFEDLVEIA ERNASSPLYT LLKRPDEKFV TEKAYENPRF VEDVARDVAL ELEKEPRITW YRVYVESMES IHNHNAFACV EKGDFVLEG //