ID   GCH11_NOSS1             Reviewed;         235 AA.
AC   Q8YLL1;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=GTP cyclohydrolase 1 1;
DE            EC=3.5.4.16;
DE   AltName: Full=GTP cyclohydrolase I 1;
DE            Short=GTP-CH-I 1;
GN   Name=folE1; OrderedLocusNames=alr5287;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC   -!- SUBUNIT: Homomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR   EMBL; BA000019; BAB76986.1; -; Genomic_DNA.
DR   PIR; AG2466; AG2466.
DR   RefSeq; WP_010999411.1; NZ_RSCN01000005.1.
DR   AlphaFoldDB; Q8YLL1; -.
DR   SMR; Q8YLL1; -.
DR   STRING; 103690.17134426; -.
DR   EnsemblBacteria; BAB76986; BAB76986; BAB76986.
DR   KEGG; ana:alr5287; -.
DR   eggNOG; COG0302; Bacteria.
DR   OMA; YHETIYD; -.
DR   OrthoDB; 1632367at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR11109; PTHR11109; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   TIGRFAMs; TIGR00063; folE; 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; Hydrolase; Nucleotide-binding; One-carbon metabolism;
KW   Reference proteome.
FT   CHAIN           1..235
FT                   /note="GTP cyclohydrolase 1 1"
FT                   /id="PRO_0000119379"
FT   REGION          26..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   235 AA;  26524 MW;  64044971731BE2AD CRC64;
     MTIASSNGSN RAQSPLITDL AEAINTRPDR NTHNGREPEL HQPSEEDMES MMGAVRSILV
     GVGEDPEREG LLKTPKRVAE AMRFLTSGYN QSLEELLNGA VFDEGHNEMV LVRDINFFSL
     CEHHMLPFMG RAHVAYIPNQ KVVGLSKLAR IVEMYSRRLQ VQERLTRQIA EAVQTILEPQ
     GVAVVMEASH MCMVMRGVQK PGSWTVTSAM LGVFQEEQKT REEFFNLIRH QPAFF