ID   MPTA_HALWD              Reviewed;         309 AA.
AC   Q18F47;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=HQ_3317A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53414.1; -; Genomic_DNA.
DR   RefSeq; WP_011572516.1; NC_008212.1.
DR   AlphaFoldDB; Q18F47; -.
DR   SMR; Q18F47; -.
DR   STRING; 362976.HQ_3317A; -.
DR   EnsemblBacteria; CAJ53414; CAJ53414; HQ_3317A.
DR   GeneID; 4193410; -.
DR   KEGG; hwa:HQ_3317A; -.
DR   eggNOG; arCOG04301; Archaea.
DR   HOGENOM; CLU_062816_1_0_2; -.
DR   OMA; PCSQGMS; -.
DR   UniPathway; UPA00065; -.
DR   Proteomes; UP000001975; 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.
DR   TIGRFAMs; TIGR00294; TIGR00294; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Reference proteome.
FT   CHAIN           1..309
FT                   /note="GTP cyclohydrolase MptA"
FT                   /id="PRO_0000289534"
FT   SITE            157
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   309 AA;  33922 MW;  1556BE07B2A160D3 CRC64;
     MSHQLPDIQA SRPDVTVGLS QVGVTDVDKL VKIERDGETP LVLMAEFEVF VDLPSGRKGI
     DMSRNMQVID ETLEAAVSGS VSRVEDMCGD VAERLLEKHE YTTTATVEMT ADLVMHEDTP
     ASELPTQNTI SILASATATD EGTREEIGAE VIGMTVCPCS QGMSASRARD VMHDLDIEDE
     TIETFLEQVP QPGHSQRGHA TLTVTADGSP DVDLIELADI ARDAMSARIY NLAKRPDEDY
     MTYHAHADAK FVEDCVRSMA EQVVNSFEHL DDDAVVRMKQ SNDESIHQHN AHAEREVTLE
     QLRAEVSAS