ID   GCH3_PYRCJ              Reviewed;         221 AA.
AC   A3MV81;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=GTP cyclohydrolase III {ECO:0000255|HAMAP-Rule:MF_00608};
DE            EC=3.5.4.29 {ECO:0000255|HAMAP-Rule:MF_00608};
GN   Name=gch3 {ECO:0000255|HAMAP-Rule:MF_00608}; OrderedLocusNames=Pcal_1123;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 2-amino-5-formylamino-6-
CC       ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and
CC       inorganic phosphate from GTP. Also has an independent pyrophosphate
CC       phosphohydrolase activity. {ECO:0000255|HAMAP-Rule:MF_00608}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + 3 H2O = 2-amino-5-formylamino-6-(5-phospho-D-
CC         ribosylamino)pyrimidin-4(3H)-one + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:22468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57258; EC=3.5.4.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00608};
CC   -!- SIMILARITY: Belongs to the archaeal-type GTP cyclohydrolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00608}.
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DR   EMBL; CP000561; ABO08548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MV81; -.
DR   SMR; A3MV81; -.
DR   STRING; 410359.Pcal_1123; -.
DR   EnsemblBacteria; ABO08548; ABO08548; Pcal_1123.
DR   KEGG; pcl:Pcal_1123; -.
DR   eggNOG; arCOG04202; Archaea.
DR   HOGENOM; CLU_080076_0_0_2; -.
DR   OMA; THVTRAN; -.
DR   Proteomes; UP000001431; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043740; F:GTP cyclohydrolase IIa activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   HAMAP; MF_00608; GTP_cyclohydro_3; 1.
DR   InterPro; IPR007839; GTP_CycHdrlase_3.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   PANTHER; PTHR42202; PTHR42202; 1.
DR   Pfam; PF05165; GCH_III; 2.
DR   PIRSF; PIRSF009265; GTP_cyclohydro_3; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..221
FT                   /note="GTP cyclohydrolase III"
FT                   /id="PRO_1000147163"
SQ   SEQUENCE   221 AA;  24196 MW;  1955ED8EF54120F9 CRC64;
     MHRVAVVTLR GYREWTESLG PRREHIIQRV QAGLHMALWR HFTSIGAFPH HTRYDAAVAL
     VNNIPTTLIE KAVDKLKKAS PVPVEYCIGT GPTPYEAYLS CGEAAGDGDN YAVLAHMDMV
     DSTHVTRANG PLHVYLQILH IISDLGDLCK RLGCIALYLG GDNVAVLLPE PKAAYEIAER
     VPVPVRVGVG VAKRPYTAFV KATKALDYLR SHGVVGVKVL K