ID   GCH41_BURL3             Reviewed;         316 AA.
AC   Q39AS8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Bcep18194_B0317;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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; CP000152; ABB10433.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q39AS8; -.
DR   SMR; Q39AS8; -.
DR   EnsemblBacteria; ABB10433; ABB10433; Bcep18194_B0317.
DR   KEGG; bur:Bcep18194_B0317; -.
DR   PATRIC; fig|482957.22.peg.3901; -.
DR   HOGENOM; CLU_062816_0_0_4; -.
DR   OMA; AKGIHMS; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002705; 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..316
FT                   /note="GTP cyclohydrolase FolE2 1"
FT                   /id="PRO_0000289482"
FT   SITE            166
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   316 AA;  33976 MW;  4610995773F63D32 CRC64;
     MEKALHRISS MNAPLPDISL TDAAPGGRPL EWVGMQGIDL PVAVAEPGCR RDVHARADVQ
     VDLPAPHVKG IHMSRLYRLL DGLGDGTALS PAGLQHVLHA MVDSHRDCDT RSARLRLRFD
     LLARRAALVT DGLAGWKAYP VRIDATLSGA RFELRAQVTV VYSSTCPCSA ALSRHWVEQA
     FLAAFGHDDR VEPAAVAAWL KRHATAATPH SQRSEAVVSV ALPADGATLG LIDLIDRIEH
     ALGTPVQTAV KRADEQAFAV LNGGNLMFVE DAARRVQAAL DGHHANPRVH VRHLESLHPH
     DAVAWAAPVR EGADAC