ID   B0JGA3_MICAN            Unreviewed;       218 AA.
AC   B0JGA3;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   04-NOV-2026, entry version 102.
DE   RecName: Full=GTP cyclohydrolase 1 {ECO:0000256|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000256|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I {ECO:0000256|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I {ECO:0000256|HAMAP-Rule:MF_00223};
GN   Name=folE {ECO:0000256|HAMAP-Rule:MF_00223,
GN   ECO:0000313|EMBL:BAG02108.1};
GN   OrderedLocusNames=MAE_22860 {ECO:0000313|EMBL:BAG02108.1};
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG02108.1, ECO:0000313|Proteomes:UP000001510};
RN   [1] {ECO:0000313|EMBL:BAG02108.1, ECO:0000313|Proteomes:UP000001510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247 {ECO:0000313|Proteomes:UP000001510};
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC         H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001052, ECO:0000256|HAMAP-
CC         Rule:MF_00223};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005080, ECO:0000256|HAMAP-Rule:MF_00223}.
CC   -!- SUBUNIT: Homopolymer. {ECO:0000256|HAMAP-Rule:MF_00223}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000256|HAMAP-Rule:MF_00223}.
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DR   EMBL; AP009552; BAG02108.1; -; Genomic_DNA.
DR   RefSeq; WP_002783992.1; NC_010296.1.
DR   AlphaFoldDB; B0JGA3; -.
DR   STRING; 449447.MAE_22860; -.
DR   PaxDb; 449447-MAE_22860; -.
DR   EnsemblBacteria; BAG02108; BAG02108; MAE_22860.
DR   KEGG; mar:MAE_22860; -.
DR   PATRIC; fig|449447.4.peg.2090; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_3_1_3; -.
DR   OMA; AAHMCMA; -.
DR   BioCyc; MAER449447:MAE_RS09965-MONOMER; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001510; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005525; F:GTP binding; IEA:TreeGrafter.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00642; GTP_cyclohydro1; 1.
DR   FunFam; 3.30.1130.10:FF:000001; GTP cyclohydrolase 1; 1.
DR   Gene3D; 1.10.286.10; -; 1.
DR   Gene3D; 3.30.1130.10; -; 1.
DR   HAMAP; MF_00223; FolE; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR043134; GTP-CH-I_N.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR   InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR   NCBIfam; NF006825; folE; 1.
DR   NCBIfam; NF006826; folE; 1.
DR   NCBIfam; TIGR00063; folE; 1.
DR   PANTHER; PTHR11109:SF7; GTP CYCLOHYDROLASE 1; 1.
DR   PANTHER; PTHR11109; GTP CYCLOHYDROLASE I; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00223};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00223}; Reference proteome {ECO:0000313|Proteomes:UP000001510};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00223}.
FT   DOMAIN          35..212
FT                   /note="GTP cyclohydrolase I"
FT                   /evidence="ECO:0000259|Pfam:PF01227"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
SQ   SEQUENCE   218 AA;  24327 MW;  33A9CAFCCB5A26BA CRC64;
     MTLAKSKAIF DNDDYNHFPE VITEPKSPVS EAEMMQAVRT LLLGLGEDPD REGLRDTPKR
     VVKALKFLTS GYQQSLDELL NGAVFHENAN EMVLIRDIDI FSSCEHHILP IIGRAHVAYI
     PNGKVIGLSK IARICEMYAR RLQVQERLTA QIADALQGLL QPQGVAVVIE ATHMCMVMRG
     VEKPGSWTST SAVRGIFADS AKTRQEFMSL IRHSPDFH
//