ID   MPTA_PICTO              Reviewed;         273 AA.
AC   Q6L0A8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=PTO1009;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43594.1; -; Genomic_DNA.
DR   RefSeq; WP_011177810.1; NC_005877.1.
DR   AlphaFoldDB; Q6L0A8; -.
DR   SMR; Q6L0A8; -.
DR   STRING; 263820.PTO1009; -.
DR   EnsemblBacteria; AAT43594; AAT43594; PTO1009.
DR   GeneID; 2844622; -.
DR   KEGG; pto:PTO1009; -.
DR   eggNOG; arCOG04301; Archaea.
DR   HOGENOM; CLU_062816_1_1_2; -.
DR   OMA; ECQEVYD; -.
DR   OrthoDB; 109805at2157; -.
DR   UniPathway; UPA00065; -.
DR   Proteomes; UP000000438; 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..273
FT                   /note="GTP cyclohydrolase MptA"
FT                   /id="PRO_0000147748"
FT   SITE            136
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   273 AA;  31893 MW;  2B16FB934F1E8F9D CRC64;
     MIELKDVQGF RPDYEIPIKR AGIKSFKRRV KLNYNNESFD SYVDVSISVS LNPDRKGLDM
     SRTIESVRSS YNLNDVAYDI YNDLFSRINY SSSGYVNVSF DFYYNNKIYP VSLIAEGDKN
     DVKRYVEVSA EGMTVCPCAM ETIRSIMLYD YNVSYGDIGI SHNQRNKASL KIQYIKDAHL
     ERLIDILESS FSYPVRNMLK RYDEGKMIIE AHKRPKFVED VVREIAYKAA FMEPEMNLYM
     DVRSESFESI HPHNAYAEIE DYTANIRSYL KNR