GCH3_METST
ID GCH3_METST Reviewed; 255 AA.
AC Q2NEH8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Msp_1404;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57775.1; -; Genomic_DNA.
DR RefSeq; WP_011406974.1; NC_007681.1.
DR AlphaFoldDB; Q2NEH8; -.
DR SMR; Q2NEH8; -.
DR STRING; 339860.Msp_1404; -.
DR EnsemblBacteria; ABC57775; ABC57775; Msp_1404.
DR GeneID; 41325977; -.
DR KEGG; mst:Msp_1404; -.
DR eggNOG; arCOG04202; Archaea.
DR HOGENOM; CLU_080076_0_0_2; -.
DR OMA; VQIAHID; -.
DR OrthoDB; 56576at2157; -.
DR Proteomes; UP000001931; 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..255
FT /note="GTP cyclohydrolase III"
FT /id="PRO_1000056694"
SQ SEQUENCE 255 AA; 27879 MW; A1453C810D3358DB CRC64;
MIQVTLIQID NYGPWTVTPG PRAEPDLQTL QSRLYGDLER EFGAHGAIVF FNRFDNLIAI
SNGMDYDDHL LIQQSIRNRY PITISMGVGT ADTAYEAQKI ATKMIQNGGG AQSANRCEVL
NIDSLADDDN SLVQIAHIDI NDITNTLTDI ETAFDTSIKV YEVLLALMDE LAKIGGMCFF
IGGDNYMAPT NGISKDQLRE ALKVVDKKTG VTLKAGIGVA KQAGRAADLA DIGLEDIRAE
LVDDSVLLFN DLDEY
