ID   MPTA_KORCO              Reviewed;         279 AA.
AC   B1L550;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Kcr_0832;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB07579.1; -; Genomic_DNA.
DR   RefSeq; WP_012309476.1; NC_010482.1.
DR   AlphaFoldDB; B1L550; -.
DR   SMR; B1L550; -.
DR   STRING; 374847.Kcr_0832; -.
DR   EnsemblBacteria; ACB07579; ACB07579; Kcr_0832.
DR   GeneID; 6094110; -.
DR   KEGG; kcr:Kcr_0832; -.
DR   eggNOG; arCOG04301; Archaea.
DR   HOGENOM; CLU_062816_1_0_2; -.
DR   InParanoid; B1L550; -.
DR   OMA; PCSQGMS; -.
DR   PhylomeDB; B1L550; -.
DR   UniPathway; UPA00065; -.
DR   Proteomes; UP000001686; Chromosome.
DR   GO; GO:0003933; F:GTP cyclohydrolase activity; IBA:GO_Central.
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..279
FT                   /note="GTP cyclohydrolase MptA"
FT                   /id="PRO_0000372041"
FT   SITE            146
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   279 AA;  31263 MW;  7B781300155D1E06 CRC64;
     MRLPEELLER ARDIHSEAPS HRIKLDRVGS FGLKVPVEFK GFLLLAEADV WVSLPEGRRG
     VDLSRQVEAI YELSNPPKDP FSLCREAAIS LLEKLNYADS SGVSIRFDAP LQDGESLKYY
     GVEISSIASD EIINKIRVEI LGMTACPCTA ELIRAYKSSE IAATHTQRSL GILEVSTKAE
     HPDPDKLASI IERAMSSPLR TYTKRPDEGG LVIRSLSNAR LAEDVVREMI HLFLEEFGHL
     PEDTHILAAV RSMESVHMHD IYAERSFSLD EIRKEISSH