ID   GCH4_BURCM              Reviewed;         269 AA.
AC   Q0BAL7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Bamb_3251;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000441; ABI88806.1; -; Genomic_DNA.
DR   RefSeq; WP_011658296.1; NZ_CP009799.1.
DR   AlphaFoldDB; Q0BAL7; -.
DR   SMR; Q0BAL7; -.
DR   STRING; 339670.Bamb_3251; -.
DR   EnsemblBacteria; ABI88806; ABI88806; Bamb_3251.
DR   GeneID; 44693904; -.
DR   GeneID; 60992425; -.
DR   KEGG; bam:Bamb_3251; -.
DR   PATRIC; fig|339670.21.peg.3456; -.
DR   eggNOG; COG1469; Bacteria.
DR   OMA; PCSQGMS; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000662; Chromosome 2.
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.
FT   CHAIN           1..269
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289479"
FT   SITE            154
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   269 AA;  30245 MW;  FB38350B5CCB9D78 CRC64;
     MNQMNPAFVM PDVQSTVDTR QIPIQRVGVK AVRHPLTVRT ESGDVQPTVG VWNLDVHLPA
     DQKGTHMSRF VALLEDSREP LTVERFRAML ASMLVRLEAE AGRIEVTFPY FVNKTAPVSG
     VQSLLDYEVT LAGESRNGET RLFLKVLVPV TSLCPCSKKI SQYGAHNQRS HVTIDAELAA
     DLPVEALIRI AEEEASCELW GLLKRPDEKF VTERAYENPK FVEDLVRDVA QRLDADERVV
     AYVLEAENFE SIHNHSAYAL IERDKRHAA