ID   GCH3_METM5              Reviewed;         266 AA.
AC   A4FZ97;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=MmarC5_1233;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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; CP000609; ABO35531.1; -; Genomic_DNA.
DR   RefSeq; WP_011868984.1; NC_009135.1.
DR   AlphaFoldDB; A4FZ97; -.
DR   SMR; A4FZ97; -.
DR   STRING; 402880.MmarC5_1233; -.
DR   EnsemblBacteria; ABO35531; ABO35531; MmarC5_1233.
DR   GeneID; 4929042; -.
DR   KEGG; mmq:MmarC5_1233; -.
DR   eggNOG; arCOG04202; Archaea.
DR   HOGENOM; CLU_080076_0_0_2; -.
DR   OMA; VQIAHID; -.
DR   OrthoDB; 56576at2157; -.
DR   Proteomes; UP000000253; 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.
FT   CHAIN           1..266
FT                   /note="GTP cyclohydrolase III"
FT                   /id="PRO_1000056691"
SQ   SEQUENCE   266 AA;  29965 MW;  63ABE23A4B107070 CRC64;
     MIQITVVQID NYGPWTVTPN PRRESDLQAL QSRLYCDMNL QFGAHRGLAF YTRFDNIIAI
     TNGIDLETHK RIQNSVKNRY PFTVSMAVAS AETAYGAQKL ATKTIQEYGS AQDDVRKEVL
     DVANEFVSNG YVQLAHVDIN DITGKLTDLE TAYDTYLSVQ KTKLKLMEEL KKYDSLGFFI
     GGDNFMCPCN GMSEKDFLCM FEDIKESCGI ELKAGIGIGK TAEDASDLAD IGLEVIREGK
     TDFQVYTLKQ DVEERKDVTY NYMCPI