GCH3_METTH
ID GCH3_METTH Reviewed; 249 AA.
AC O27096;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=MTH_1017;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85513.1; -; Genomic_DNA.
DR PIR; F69002; F69002.
DR RefSeq; WP_010876648.1; NC_000916.1.
DR AlphaFoldDB; O27096; -.
DR SMR; O27096; -.
DR STRING; 187420.MTH_1017; -.
DR PRIDE; O27096; -.
DR EnsemblBacteria; AAB85513; AAB85513; MTH_1017.
DR GeneID; 24854149; -.
DR KEGG; mth:MTH_1017; -.
DR PATRIC; fig|187420.15.peg.1000; -.
DR HOGENOM; CLU_080076_0_0_2; -.
DR OMA; VQIAHID; -.
DR Proteomes; UP000005223; 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..249
FT /note="GTP cyclohydrolase III"
FT /id="PRO_0000145756"
SQ SEQUENCE 249 AA; 27645 MW; 0B6DD6F1CEEB2BAF CRC64;
MIQMTLIQID NYGPWTVTPT PRNEADLQIM QAELYADLQR QFAARQGLVF FTRFDNMLAV
TNGMDLEDHR RIQKSIGNRY PITVSMGVGA AETPYDAQRN ASRALQSHGG AQSEERKEVL
AIDGLVDEGY VQIAHIDING ITETMTDIVP AYDTSFIVNR VQHFLMKKLI KEGALLFFIG
GDNFMSPCNG LEPQGLLRII NEIDDEINVA LKAGIGKAPT AEKAANLADL ALEEIRGGFT
YDLVHVMKE
