ID   GCH41_CUPMC             Reviewed;         309 AA.
AC   Q1LPE1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=GTP cyclohydrolase FolE2 1 {ECO:0000255|HAMAP-Rule:MF_01527};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   Name=folE2-1 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   OrderedLocusNames=Rmet_1099;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(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=ABF07985.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000352; ABF07985.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029309978.1; NC_007973.1.
DR   AlphaFoldDB; Q1LPE1; -.
DR   SMR; Q1LPE1; -.
DR   STRING; 266264.Rmet_1099; -.
DR   EnsemblBacteria; ABF07985; ABF07985; Rmet_1099.
DR   KEGG; rme:Rmet_1099; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_0_4; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002429; Chromosome.
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   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   PANTHER; PTHR36445; PTHR36445; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..309
FT                   /note="GTP cyclohydrolase FolE2 1"
FT                   /id="PRO_0000289517"
FT   SITE            156
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   309 AA;  33970 MW;  FFF204BF8A9293C6 CRC64;
     MSAALPDVSL TEASPTFTPL EWVGMQGIDL PIRLVEPGYR RQLHARADIH VDLPAPRVKG
     IHMSRLYALL DALDDGEGLS PIRIRQLLEA MVDSHRDCET GSARLRLRFD LLVRRPALVT
     EGIAGWKSYP VRLDASLVGN VFALTARITA GYSSTCPCSA ALTRQLVEQG FAKAFAHERR
     VDVARVSAWL RQHGTLATPH SQRSEASITV DIAVDLPNLG LLDLVDHIER ALGTPVQTAV
     KRADEQAFAA LNGQNLMFVE DAARRIQVAL DGRFANPRVH VRHLESLHPH DAVAWAAPLQ
     MKHSREVAA