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GCH3_SACS2
ID   GCH3_SACS2              Reviewed;         231 AA.
AC   Q980B6;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=SSO0399;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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; AE006641; AAK40728.1; -; Genomic_DNA.
DR   PIR; A99184; A99184.
DR   RefSeq; WP_009988791.1; NC_002754.1.
DR   AlphaFoldDB; Q980B6; -.
DR   SMR; Q980B6; -.
DR   STRING; 273057.SSO0399; -.
DR   EnsemblBacteria; AAK40728; AAK40728; SSO0399.
DR   GeneID; 44129380; -.
DR   KEGG; sso:SSO0399; -.
DR   PATRIC; fig|273057.12.peg.395; -.
DR   eggNOG; arCOG04202; Archaea.
DR   HOGENOM; CLU_080076_0_0_2; -.
DR   InParanoid; Q980B6; -.
DR   OMA; VQIAHID; -.
DR   PhylomeDB; Q980B6; -.
DR   Proteomes; UP000001974; 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; 1.
DR   PIRSF; PIRSF009265; GTP_cyclohydro_3; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..231
FT                   /note="GTP cyclohydrolase III"
FT                   /id="PRO_0000145758"
SQ   SEQUENCE   231 AA;  27013 MW;  5119B366CD40AB18 CRC64;
     MKILAIKLLD YREWTERLGY DREWLIQKIQ NKFMMKIHEI ASQYNTFPLQ LRFDNFLMIA
     DGITTTQLAY MINDMQENLP VRIKSCLGYG KTPLEAQWNA SICLNNQDDN EIKEYTDEKI
     AALHFDINFN TETLKYTSVY DSFIEITNIY VNLSRFLYKI GGILQYLGGD NYLGFISTES
     VNKVIEEFSD DNKIKVGIGI GKNARTAIRL ATTSLEKIRN NREKTWHMEE E
 
 
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