GCH3_METM7
ID GCH3_METM7 Reviewed; 266 AA.
AC A6VJ40;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-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=MmarC7_1403;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR66466.1; -; Genomic_DNA.
DR RefSeq; WP_012067932.1; NC_009637.1.
DR AlphaFoldDB; A6VJ40; -.
DR SMR; A6VJ40; -.
DR STRING; 426368.MmarC7_1403; -.
DR EnsemblBacteria; ABR66466; ABR66466; MmarC7_1403.
DR GeneID; 5329502; -.
DR KEGG; mmz:MmarC7_1403; -.
DR eggNOG; arCOG04202; Archaea.
DR HOGENOM; CLU_080076_0_0_2; -.
DR OMA; VQIAHID; -.
DR OrthoDB; 56576at2157; -.
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_1000056692"
SQ SEQUENCE 266 AA; 30058 MW; 657A6A176BE2278E CRC64;
MIQITVVQID NYGPWTVTPN PRRESDLQAL QSRLYCDMNL QFGAHRGLAF YTRFDNIIAI
TNGIDLETHK RIQNSVKNRY PFTVSMAVAS AETAYEAQKL ATETIQEYGS AQDDVRKEVL
DVANEFVSNG YVQLAHVDIN DITGKLTDLE TAYDTYLSVQ MTKLKLMEEL KKYDSMGFFI
GGDNFMCPCN GMSEKDFLCM FEDIRDSCGI DLKAGIGIGK TAEDASNLAD IGLEVIREGK
TDFQVYTLKQ SIEERKDITY NYMCPI
