ID A0A0A6N339_9THEM Unreviewed; 259 AA. AC A0A0A6N339; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 10-MAY-2017, entry version 14. 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; Thermotogae; Thermotogales; Thermotogaceae; 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, ECO:0000256|SAAS:SAAS00694239}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6- CC (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01527, ECO:0000256|SAAS:SAAS00694234}. CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step CC 1/1. {ECO:0000256|HAMAP-Rule:MF_01527, CC ECO:0000256|SAAS:SAAS00694232}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. CC {ECO:0000256|HAMAP-Rule:MF_01527, ECO:0000256|SAAS:SAAS00694240}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 RefSeq; WP_038052083.1; NZ_JSFH01000005.1. DR RefSeq; WP_038052083.1; NZ_JSFH01000005.1. DR EnsemblBacteria; KHC92879; KHC92879; Mc24_01968. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000030509; Unassembled WGS sequence. DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-HAMAP. DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway. 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:SF2; PTHR36445:SF2; 1. DR Pfam; PF02649; GCHY-1; 1. DR TIGRFAMs; TIGR00294; TIGR00294; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030509}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01527, KW ECO:0000256|SAAS:SAAS00694242, ECO:0000313|EMBL:KHC92879.1}. FT SITE 143 143 May be catalytically important. FT {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 //