ID   GCH3_SULTO              Reviewed;         225 AA.
AC   Q975M4; F9VMW6;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=STK_03950;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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; BA000023; BAK54263.1; -; Genomic_DNA.
DR   RefSeq; WP_010978359.1; NC_003106.2.
DR   AlphaFoldDB; Q975M4; -.
DR   SMR; Q975M4; -.
DR   STRING; 273063.STK_03950; -.
DR   EnsemblBacteria; BAK54263; BAK54263; STK_03950.
DR   GeneID; 1458320; -.
DR   KEGG; sto:STK_03950; -.
DR   PATRIC; fig|273063.9.peg.456; -.
DR   eggNOG; arCOG04202; Archaea.
DR   OMA; VQIAHID; -.
DR   OrthoDB; 56576at2157; -.
DR   Proteomes; UP000001015; 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; 3.30.70.270; -; 2.
DR   HAMAP; MF_00608; GTP_cyclohydro_3; 1.
DR   InterPro; IPR007839; GTP_CycHdrlase_3.
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; Reference proteome.
FT   CHAIN           1..225
FT                   /note="GTP cyclohydrolase III"
FT                   /id="PRO_0000145759"
SQ   SEQUENCE   225 AA;  25964 MW;  D531616744AC9723 CRC64;
     MKIMQINLVD YKEWTESLGY DREWKIQNFQ HGFLSRLNEI AAEINSFIIT YRYDSYIMLL
     DGVLIGKNDY ILTKIKELSP VPIDICFGYG KTLLDAERNC SINMDNILLA KDEKVLVAHF
     DLDGFSRKRF LFDAYLEVYK IYNKLFNYAM ELGGLAYYFG GDNIGIFLGV DNINKVIELA
     NSFPNMKVGI GIGNNPREAL KNAAEALHII RIYRDRKIEI VDSKN