GCH3_METVS
ID GCH3_METVS Reviewed; 266 AA.
AC A6US18;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Mevan_1393;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-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; CP000742; ABR55290.1; -; Genomic_DNA.
DR RefSeq; WP_012066204.1; NC_009634.1.
DR AlphaFoldDB; A6US18; -.
DR SMR; A6US18; -.
DR STRING; 406327.Mevan_1393; -.
DR EnsemblBacteria; ABR55290; ABR55290; Mevan_1393.
DR GeneID; 5324816; -.
DR KEGG; mvn:Mevan_1393; -.
DR eggNOG; arCOG04202; Archaea.
DR HOGENOM; CLU_080076_0_0_2; -.
DR OMA; VQIAHID; -.
DR OrthoDB; 56576at2157; -.
DR Proteomes; UP000001107; 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_1000056695"
SQ SEQUENCE 266 AA; 29948 MW; E7A3A7E2D3F25A1F CRC64;
MIQITVVQID NYGPWTVTPN PRRESDLQAL QSRLYCDMNL QFGAHKGLAF YTRFDNIIAI
TNGIDLETHR RIQNSIKNRY PFTVSMAIAS AETPYDAQKL ATEKLQEYGS AQDEVRKEVL
DIANEFVSNG YVQLAHVDIN DITGTLTDLE TAYDTYLSVQ MTKLKLMEEL KKYNSMGFFI
GGDNFMCPCN GMNEKDFQCM FEDIMESSGI ELKAGIGIGK TAEDASNLAD IGLEIIREGK
TDLQVYKLKQ ATGETKSSPY NYMCPI
