ID   GCH1_SERP5              Reviewed;         221 AA.
AC   A8GC24;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   02-SEP-2026, entry version 96.
DE   RecName: Full=GTP cyclohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I {ECO:0000255|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I {ECO:0000255|HAMAP-Rule:MF_00223};
GN   Name=folE {ECO:0000255|HAMAP-Rule:MF_00223};
GN   OrderedLocusNames=Spro_1560;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(2009).
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:0000255|HAMAP-Rule:MF_00223};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00223}.
CC   -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC       dimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000255|HAMAP-Rule:MF_00223}.
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DR   EMBL; CP000826; ABV40664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GC24; -.
DR   SMR; A8GC24; -.
DR   STRING; 399741.Spro_1560; -.
DR   PaxDb; 399741-Spro_1560; -.
DR   KEGG; spe:Spro_1560; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_3_2_6; -.
DR   OrthoDB; 9801207at2; -.
DR   UniPathway; UPA00848; UER00151.
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   FunFam; 1.10.286.10:FF:000002; GTP cyclohydrolase 1; 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; TIGR00063; folE; 1.
DR   NCBIfam; NF006824; PRK09347.1-1; 1.
DR   NCBIfam; NF006826; PRK09347.1-3; 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; Zinc.
FT   CHAIN           1..221
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_1000058677"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
SQ   SEQUENCE   221 AA;  24874 MW;  F712249925D2B04D CRC64;
     MTSLSKEAVL VHAALEERGL ETPLRGEVLD RETRKRRIKE HMTEIMQLLN LDLSDDSLAE
     TPHRIAKMYV DEIFSGLDYA NFPKITVIEN KMKVDEMVTV RDITLTSTCE HHFVTIDGKA
     TVAYIPKDAV IGLSKINRIV QFFSQRPQVQ ERLTQQILVA LQTLLGTNNV AVSIDAVHYC
     VKARGIRDAT SATTTTSLGG LFKSSQNTRQ EFLRAVRHHQ G
//