ID   Q2NB45_ERYLH            Unreviewed;       203 AA.
AC   Q2NB45;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   02-SEP-2026, entry version 115.
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   OrderedLocusNames=ELI_05020 {ECO:0000313|EMBL:ABC63096.1};
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter group;
OC   Erythrobacter.
OX   NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC63096.1, ECO:0000313|Proteomes:UP000008808};
RN   [1] {ECO:0000313|Proteomes:UP000008808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808};
RX   PubMed=19168610; DOI=10.1128/JB.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(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: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   -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC       dimers. {ECO:0000256|ARBA:ARBA00011857}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000256|ARBA:ARBA00008085, ECO:0000256|HAMAP-Rule:MF_00223}.
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DR   EMBL; CP000157; ABC63096.1; -; Genomic_DNA.
DR   RefSeq; WP_011413932.1; NC_007722.1.
DR   AlphaFoldDB; Q2NB45; -.
DR   STRING; 314225.ELI_05020; -.
DR   KEGG; eli:ELI_05020; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_3_1_5; -.
DR   OrthoDB; 9801207at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000008808; 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   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; NF006825; PRK09347.1-2; 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 {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   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:UP000008808};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00223}.
FT   DOMAIN          23..200
FT                   /note="GTP cyclohydrolase I"
FT                   /evidence="ECO:0000259|Pfam:PF01227"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
SQ   SEQUENCE   203 AA;  22600 MW;  2BC62250F401478C CRC64;
     MACEADYVED PAIKKPDVPE HVQDAIRTLI EWSGDDPARE GLLDTPKRVG RAWLEYCQGY
     KEDPAIHLSR VFEEVGGYDE IVLLKDIPFQ SHCEHHMAPI TGKAAIAYLP RDKVVGISKL
     ARVLHGFARR LQIQERLTAE VANCIWDNLE PEGVAVVIEA QHGCMTGRGV RTPGVSMVTS
     KLCGCFLDDE RSRKEVLSLM GYG
//