ID GCH4_BURM7 Reviewed; 269 AA. AC A3MBD3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 2. DT 27-MAR-2024, entry version 80. 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=BMA10247_A0366; OS Burkholderia mallei (strain NCTC 10247). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10247; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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 -!- SEQUENCE CAUTION: CC Sequence=ABO02353.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000547; ABO02353.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_004195713.1; NZ_CP007801.1. DR AlphaFoldDB; A3MBD3; -. DR SMR; A3MBD3; -. DR GeneID; 56598187; -. DR KEGG; bmaz:BM44_3366; -. DR KEGG; bmn:BMA10247_A0366; -. DR PATRIC; fig|320389.8.peg.3780; -. 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..269 FT /note="GTP cyclohydrolase FolE2" FT /id="PRO_0000316527" FT SITE 154 FT /note="May be catalytically important" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527" SQ SEQUENCE 269 AA; 30188 MW; 832F04704D584F29 CRC64; MNLMNPEFAM PDVQSTVDTR QMPIQRVGVR AVRHPLTVRT AEGETQATVG TWNLDVHLPA DQKGTHMSRF VALLEERGGP LTADAFRTML ATMLEKLEAR AGRIEVSFPY FVNKTAPVSG VRSLLDYEVT LTGDVRDGLT RVFAKVLVPV TSLCPCSKKI SQYGAHNQRS HVTIDAELAA DVPVEDLIRI AEEEASCELW GLLKRPDEKF VTERAYENPK FVEDLVRDVA RRLDADERIV AYVLEAENFE SIHNHSAYAL IERDKRRGA //