GCH3_METS3
ID GCH3_METS3 Reviewed; 254 AA.
AC A5ULV0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-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=Msm_0973;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87178.1; -; Genomic_DNA.
DR RefSeq; WP_004032962.1; NC_009515.1.
DR AlphaFoldDB; A5ULV0; -.
DR SMR; A5ULV0; -.
DR STRING; 420247.Msm_0973; -.
DR EnsemblBacteria; ABQ87178; ABQ87178; Msm_0973.
DR GeneID; 5216943; -.
DR KEGG; msi:Msm_0973; -.
DR PATRIC; fig|420247.28.peg.970; -.
DR eggNOG; arCOG04202; Archaea.
DR HOGENOM; CLU_080076_0_0_2; -.
DR OMA; VQIAHID; -.
DR Proteomes; UP000001992; 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..254
FT /note="GTP cyclohydrolase III"
FT /id="PRO_1000056693"
SQ SEQUENCE 254 AA; 28458 MW; A2ED2D0DA09F5CC3 CRC64;
MIQMTLIQID NYGPWTVTPR PRNESDLQIL QAELYADLER QFANKKGLVF FTRFDNLLAV
TNGIDEEDHL RIQRSIRNRY PITISMGVGA AETPHEAQKL ATIALQKEGG AQSSKRKEIL
AIDSLAPADE NNLVQAAHID INSVTETLTD IESAFDTNFM VNKAQHYLMT KLIKKGALLF
FIGGDNFMAP CNGLSEKEIE DILVEINDEI GIGLKAGIGV GRNMEDAAYM ADLGLEEIRD
HDNGMWTWVI EKEY
