ID   GCH1_SYNY3              Reviewed;         234 AA.
AC   Q55759;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=GTP cyclohydrolase 1;
DE            EC=3.5.4.16;
DE   AltName: Full=GTP cyclohydrolase I;
DE            Short=GTP-CH-I;
GN   Name=folE; OrderedLocusNames=slr0426;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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: Toroid-shaped homodecamer, composed of two pentamers of five
CC       dimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA10406.1; -; Genomic_DNA.
DR   PIR; S76560; S76560.
DR   AlphaFoldDB; Q55759; -.
DR   SMR; Q55759; -.
DR   IntAct; Q55759; 1.
DR   STRING; 1148.gene:10499907; -.
DR   PaxDb; 1148-1001671; -.
DR   EnsemblBacteria; BAA10406; BAA10406; BAA10406.
DR   KEGG; syn:slr0426; -.
DR   eggNOG; COG0302; Bacteria.
DR   InParanoid; Q55759; -.
DR   PhylomeDB; Q55759; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00642; GTP_cyclohydro1; 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; 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; Hydrolase; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Reference proteome; Zinc.
FT   CHAIN           1..234
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_0000119458"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  26640 MW;  7F007E8B7E4B19C3 CRC64;
     MTIASSHSIN NGMNTGKLVN QLSSLPDRNT HNGQEVKYHP ENVELNKEKM MDAVRVMLES
     VGEDPEREGL LKTPKRVAEA MQFLTQGYDQ SLEKLVNGAI FDEGHNEMVL VRDIDFFSLC
     EHHMLPFMGK AHLAYIPNQK VVGLSKLARI VEMFSRRLQV QERLTRQIAE AVQEILDPQG
     VAVVMEATHM CMVMRGVQKP GSWTVTSAMI GSFQNEQKTR EEFLNLIRHQ PNFY
//