GCH3_METJA
ID GCH3_METJA Reviewed; 268 AA.
AC Q57609;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=GTP cyclohydrolase III;
DE EC=3.5.4.29;
DE AltName: Full=MjGC;
GN Name=gch3; OrderedLocusNames=MJ0145;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP CHARACTERIZATION, MUTAGENESIS OF HIS-136, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=12475257; DOI=10.1021/bi0268798;
RA Graham D.E., Xu H., White R.H.;
RT "A member of a new class of GTP cyclohydrolases produces
RT formylaminopyrimidine nucleotide monophosphates.";
RL Biochemistry 41:15074-15084(2002).
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.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Homotrimer.
CC -!- MASS SPECTROMETRY: Mass=30359; Mass_error=114; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12475257};
CC -!- MISCELLANEOUS: This enzyme couples pyrophosphate hydrolysis to the
CC guanine ring-opening reaction. GTP cyclohydrolase and pyrophosphate
CC phosphoydrolase activities probably occur at independent sites.
CC -!- SIMILARITY: Belongs to the archaeal-type GTP cyclohydrolase family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98128.1; -; Genomic_DNA.
DR PIR; B64318; B64318.
DR RefSeq; WP_010869640.1; NC_000909.1.
DR PDB; 2QV6; X-ray; 2.00 A; A/B/C/D=1-268.
DR PDBsum; 2QV6; -.
DR AlphaFoldDB; Q57609; -.
DR SMR; Q57609; -.
DR STRING; 243232.MJ_0145; -.
DR EnsemblBacteria; AAB98128; AAB98128; MJ_0145.
DR GeneID; 1450989; -.
DR KEGG; mja:MJ_0145; -.
DR eggNOG; arCOG04202; Archaea.
DR HOGENOM; CLU_080076_0_0_2; -.
DR InParanoid; Q57609; -.
DR OMA; VQIAHID; -.
DR OrthoDB; 56576at2157; -.
DR PhylomeDB; Q57609; -.
DR BioCyc; MetaCyc:MON-14598; -.
DR BRENDA; 3.5.4.29; 3260.
DR EvolutionaryTrace; Q57609; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Magnesium; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..268
FT /note="GTP cyclohydrolase III"
FT /id="PRO_0000145754"
FT MUTAGEN 136
FT /note="H->Q: Decrease in GTP cyclohydrolase and
FT pyrophosphate phosphohydrolase activities."
FT /evidence="ECO:0000269|PubMed:12475257"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 24..43
FT /evidence="ECO:0007829|PDB:2QV6"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2QV6"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:2QV6"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:2QV6"
FT HELIX 222..237
FT /evidence="ECO:0007829|PDB:2QV6"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:2QV6"
SQ SEQUENCE 268 AA; 30286 MW; 627BBD523868B05B CRC64;
MIQITVIQID NYGPWTVTPN PRRESDLQAL QSRLYADLNL MFGAHKGLVF YTRFDNLIAI
TNGIDLITHK RIQESIRNRY PFTVSMVIAS AETPYEAQKL ATETLQEYGS AQDENRKEVL
DVANELVVDG YVQIAHIDIN NITGTLTDIV SAYDTYLNVN KVKLALMEEL LKYNALLFFI
GGDNFMAPSN GMSEEDFLDI FNRINKKYKI ELKAGIGIGR TAEDASNLAD IGLEKIRGKL
VDKNVCTLKQ DDFLESKMGM GKIYHPQF
