ID   GCH1_SYNE7              Reviewed;         213 AA.
AC   Q54769; Q31MU2; Q8KPT2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 131.
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=Synpcc7942_1597; ORFNames=sec0031;
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Phung L.T., Haselkorn R.;
RT   "Genes encoding the alpha subunit of carboxyltransferase of the acetyl-CoA
RT   carboxylase complex and GTP cyclohydrolase I from cyanobacterium
RT   Synechococcus sp. PCC 7942.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., Gonzalez A.,
RA   Salinas I., McMurtry S., Golden S.S., Youderian P.;
RT   "Synechococcus elongatus PCC7942 cosmid 6C3.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB82043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAM82644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U59236; AAB82043.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY120852; AAM82644.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000100; ABB57627.1; -; Genomic_DNA.
DR   RefSeq; WP_011242367.1; NZ_JACJTX010000004.1.
DR   AlphaFoldDB; Q54769; -.
DR   SMR; Q54769; -.
DR   STRING; 1140.Synpcc7942_1597; -.
DR   PaxDb; 1140-Synpcc7942_1597; -.
DR   GeneID; 76400335; -.
DR   KEGG; syf:Synpcc7942_1597; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_2_2_3; -.
DR   OrthoDB; 9801207at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1597-MONOMER; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000889800; 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   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..213
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_0000119457"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23715 MW;  4DA8E3F94B84BE45 CRC64;
     MTSPSLNGSN SLVDAIRPET EAVSQAEMEA AVRTLLLGVG EDPEREGLLK TPKRVAEAYR
     FLTSGYSQSL DDLVNGAIFD EGHNEMVLVR DITAFSLCEH HMLPFMGKVH VAYIPNQKVV
     GLSKLARIVE MYSRRLQVQE RLTRQIAESV QEILDPQGVA VVMEATHMCM VMRGVQKPGS
     WTVTSAMVGV FQEDQRTREE FLSLIRHQPA AFA
//