ID   MPTA_PYRFU              Reviewed;         267 AA.
AC   Q8TZZ2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=GTP cyclohydrolase MptA {ECO:0000255|HAMAP-Rule:MF_01527};
DE            EC=3.5.4.39 {ECO:0000255|HAMAP-Rule:MF_01527};
DE   AltName: Full=GTP cyclohydrolase IV {ECO:0000255|HAMAP-Rule:MF_01527};
GN   Name=mptA {ECO:0000255|HAMAP-Rule:MF_01527}; OrderedLocusNames=PF1832;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic
CC       phosphate, the first intermediate in the biosynthesis of coenzyme
CC       methanopterin. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = 7,8-dihydroneopterin 2',3'-cyclic phosphate +
CC         diphosphate + formate + H(+); Xref=Rhea:RHEA:25860,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58854; EC=3.5.4.39;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01527};
CC   -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
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DR   EMBL; AE009950; AAL81956.1; -; Genomic_DNA.
DR   RefSeq; WP_011012972.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8TZZ2; -.
DR   SMR; Q8TZZ2; -.
DR   STRING; 186497.PF1832; -.
DR   PRIDE; Q8TZZ2; -.
DR   EnsemblBacteria; AAL81956; AAL81956; PF1832.
DR   GeneID; 41713651; -.
DR   KEGG; pfu:PF1832; -.
DR   PATRIC; fig|186497.12.peg.1903; -.
DR   eggNOG; arCOG04301; Archaea.
DR   HOGENOM; CLU_062816_1_0_2; -.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 109805at2157; -.
DR   PhylomeDB; Q8TZZ2; -.
DR   UniPathway; UPA00065; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0003933; F:GTP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01527_A; GTP_cyclohydrol_A; 1.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   InterPro; IPR022840; GTP_cyclohydrolase_MptA.
DR   PANTHER; PTHR36445; PTHR36445; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Reference proteome.
FT   CHAIN           1..267
FT                   /note="GTP cyclohydrolase MptA"
FT                   /id="PRO_0000147750"
FT   SITE            157
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   267 AA;  30509 MW;  47AA23BCEF2DE7BE CRC64;
     MTIETQEEPP EIKVYLPRVG ITNLKSVAKI EWKGRIYTFI PTFEVAIDLP EEKKGIHMSR
     LVESITETMS EAVEEEVKKV HTSLEDLALC IIRRIEKKHS HKRAEVWIKS TLILERQTPA
     SGKTSYEPYD VEVGVIKNSD GSIKKVLKVK VIGNTACPHA MANNQGKTHI QRAIAELEIE
     THFNEDIALE DMIEVVESSF SSPTYTLLKT PDENAVVRRM YENPKFVEDV AREIVYKARN
     RFKGKIHVKV ISHESIHKHD VIAEVWA