ID   GCH42_CUPMC             Reviewed;         267 AA.
AC   Q1LK35;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=GTP cyclohydrolase FolE2 2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   Name=folE2-2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   OrderedLocusNames=Rmet_2614;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; 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}.
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DR   EMBL; CP000352; ABF09491.1; -; Genomic_DNA.
DR   RefSeq; WP_008649847.1; NC_007973.1.
DR   AlphaFoldDB; Q1LK35; -.
DR   SMR; Q1LK35; -.
DR   STRING; 266264.Rmet_2614; -.
DR   GeneID; 60820950; -.
DR   KEGG; rme:Rmet_2614; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_4; -.
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   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..267
FT                   /note="GTP cyclohydrolase FolE2 2"
FT                   /id="PRO_0000289516"
FT   SITE            153
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   267 AA;  29908 MW;  09A8A32B70A92D9B CRC64;
     MNDINPAFVM PDVQSSVDTR QIVIQRVGVK GVRYPLTLKT PAGAVGTVGT FNMDVRLPAD
     QKGTHMSRFV ALLEENRAPL DLAAFRALVD DMLVRLEADA GRIEVSFPYF ITKTAPVSGV
     QSLLDYEVTL VAEARDGQTR MFMTALVPVT SLCPCSKKIS QYGAHNQRSH ITMRVELAGD
     LDVEALVRMA EEEASCELWG LLKRPDEKFV TERAYENPKF VEDLVRDIAM RLNADDRIVA
     YTLEAENFES IHNHSAYAVI EHDKRHQ
//