ID   MPTA_PYRHO              Reviewed;         269 AA.
AC   O59447;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=PH1783;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA30902.1; -; Genomic_DNA.
DR   PIR; G71188; G71188.
DR   AlphaFoldDB; O59447; -.
DR   SMR; O59447; -.
DR   STRING; 70601.3258219; -.
DR   EnsemblBacteria; BAA30902; BAA30902; BAA30902.
DR   KEGG; pho:PH1783; -.
DR   eggNOG; arCOG04301; Archaea.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 109805at2157; -.
DR   UniPathway; UPA00065; -.
DR   Proteomes; UP000000752; 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.
FT   CHAIN           1..269
FT                   /note="GTP cyclohydrolase MptA"
FT                   /id="PRO_0000147751"
FT   SITE            159
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   269 AA;  30911 MW;  EBF296C18828FE56 CRC64;
     MRELFIETQE KEPEIKIPLP RVGITNLRTI AKINWKGRVY TFIPTFEITI DLPREKKGIH
     MSRLVESITD AMSEAIEEEV KKIHTSLEEL ALAVIQRLEE KHRHKRAEVW IRTTLILEKM
     TPASNKLSYE PYDVEVGVIK EGDKIKKTLK VKVIGNTACP HAMANNEGKT HIQRAIGELE
     VTTDFNEYVT LEDMIEVVES SFSSPTYTLL KTPDENSVVR RMYENPKFVE DVAREILIKA
     KKKFPGKIHV KVVSNESIHK HDVIAEAWA