ID GCH4_IDILO Reviewed; 308 AA. AC Q5R041; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 29-MAY-2024, entry version 97. 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}; OrderedLocusNames=IL0489; OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=283942; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR; RX PubMed=15596722; DOI=10.1073/pnas.0407638102; RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.; RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina RT loihiensis reveals amino acid fermentation as a source of carbon and RT energy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004). 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; AE017340; AAV81332.1; -; Genomic_DNA. DR RefSeq; WP_011233750.1; NC_006512.1. DR AlphaFoldDB; Q5R041; -. DR SMR; Q5R041; -. DR STRING; 283942.IL0489; -. DR KEGG; ilo:IL0489; -. DR eggNOG; COG1469; Bacteria. DR HOGENOM; CLU_062816_0_0_6; -. DR OrthoDB; 239637at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000001171; Chromosome. DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule. 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..308 FT /note="GTP cyclohydrolase FolE2" FT /id="PRO_0000147711" FT SITE 155 FT /note="May be catalytically important" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527" SQ SEQUENCE 308 AA; 34233 MW; D4CDA07CC2E8FE89 CRC64; MPTVMPDVAN QTQAQTEGAL DWVGMSNIEV PLMVAAAGVP ERPVAAKVEA FVNLKNPKTK GIHMSRLYLL LDKMSTEGEL SHDTLKQLLN DFIESHKDIS DQAFIKFDFD YHLRRKSLIS KKQGWKAYPV SLTGRYDAGQ LKLELSVDVP YSSTCPCSAA LARQLIQDAF SEKFAGQEQV DASIMHEWLG STEGIVATPH SQRSVAEVKV ALSDSVNDFP IVELIDAIEG ALKTPVQAAV KREDEQEFAR LNGQNLMFCE DASRRLQHQL NQMSNFRDFW LRVNHYESLH AHDAVSVTTK GVPGGYSA //