ID   GCH4_KLEPN              Reviewed;         299 AA.
AC   Q6U5S4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 59.
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}; ORFNames=LV189;
OS   Klebsiella pneumoniae.
OG   Plasmid pLVPK.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CG43;
RX   PubMed=15276215; DOI=10.1016/j.gene.2004.05.008;
RA   Chen Y.-T., Chang H.-Y., Lai Y.-C., Pan C.-C., Tsai S.-F., Peng H.-L.;
RT   "Sequencing and analysis of the large virulence plasmid pLVPK of Klebsiella
RT   pneumoniae CG43.";
RL   Gene 337:189-198(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR07797.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY378100; AAR07797.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q6U5S4; -.
DR   SMR; Q6U5S4; -.
DR   UniPathway; UPA00848; UER00151.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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   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; Plasmid.
FT   CHAIN           1..299
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000147712"
FT   SITE            147
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   299 AA;  32801 MW;  5396818BE23DCCB4 CRC64;
     MLPDIQSTKG DGEGESLSWV GMEQIDLPID IAGRPVSAKV NAGINLLSSP EAEKGIHMSR
     LYLLLDELTQ GEITPALLQH VLKAFLVSHQ GRSDEASIEI SGDLLLSRKS LNSNHSGWKA
     YPLTLSAELR QSFTVTLKVG IPYSSTCPAS AALSRHVAGL QFSKDFGNRI DRLPAAEIAD
     WLVEKGMPAT PHSQRSWAWV DIRLNPEAKS LPVLELIDYA EVALGTAVQT VVKRSDEQAF
     AVANGQNLMF CEDAARRLNN VFRCASFCEA FDIRVEHQES LHPHNAVARI HWKGSKNVT
//