ID   GCH4_LAWIP              Reviewed;         258 AA.
AC   Q1MPD2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   18-JUN-2025, entry version 86.
DE   RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   OrderedLocusNames=LI1091;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00;
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
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_01527};
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_01527}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
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DR   EMBL; AM180252; CAJ55145.1; -; Genomic_DNA.
DR   RefSeq; WP_011527174.1; NC_008011.1.
DR   AlphaFoldDB; Q1MPD2; -.
DR   SMR; Q1MPD2; -.
DR   STRING; 363253.LI1091; -.
DR   KEGG; lip:LI1091; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_7; -.
DR   OrthoDB; 9774824at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002430; Chromosome.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.270.10; Urate Oxidase; 1.
DR   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   NCBIfam; NF010200; PRK13674.1-1; 1.
DR   PANTHER; PTHR36445; GTP CYCLOHYDROLASE MPTA; 1.
DR   PANTHER; PTHR36445:SF1; GTP CYCLOHYDROLASE MPTA; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..258
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289495"
FT   SITE            145
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   258 AA;  29492 MW;  41008B81354FF064 CRC64;
     MKDIQSTPAQ IAFPIDRVGV KGLKFPIQIQ TRDIGMQHTV AIVDMGVDLS VSSRGTHMSR
     FVEVLQDWNE PLCCESLERL VKQTQKKLQS QHAYIAFFFP YFLHKRAPST NMLSLFSYDC
     KLSAKSINYN IEFILELTVP VMTVCPCSKA ISHEGAHSQR SEIYIQLRLE QFRFIEDFIV
     LAESSASSPL YSLLKRADEK YVTEDAFAHP KFVEDVVRNI SSKLITVTDV LGFRVEVESF
     ESIHAHNAFA YIEHEFIC
//