ID   GCH4_NEIG1              Reviewed;         257 AA.
AC   Q5F9K6;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=GTP cyclohydrolase FolE2;
DE            EC=3.5.4.16;
DE   AltName: Full=GTP cyclohydrolase 1B;
GN   Name=folE2; OrderedLocusNames=NGO0387;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17032654; DOI=10.1074/jbc.m607114200;
RA   El Yacoubi B., Bonnett S., Anderson J.N., Swairjo M.A., Iwata-Reuyl D.,
RA   de Crecy-Lagard V.;
RT   "Discovery of a new prokaryotic type I GTP cyclohydrolase family.";
RL   J. Biol. Chem. 281:37586-37593(2006).
CC   -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC       {ECO:0000269|PubMed:17032654}.
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:0000269|PubMed:17032654};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004969; AAW89131.1; -; Genomic_DNA.
DR   RefSeq; YP_207543.1; NC_002946.2.
DR   PDB; 3D2O; X-ray; 2.04 A; A/B=1-257.
DR   PDB; 5K95; X-ray; 2.77 A; A/B=1-257.
DR   PDB; 5K9G; X-ray; 1.90 A; A/B=1-257.
DR   PDBsum; 3D2O; -.
DR   PDBsum; 5K95; -.
DR   PDBsum; 5K9G; -.
DR   AlphaFoldDB; Q5F9K6; -.
DR   SMR; Q5F9K6; -.
DR   STRING; 242231.NGO_0387; -.
DR   EnsemblBacteria; AAW89131; AAW89131; NGO_0387.
DR   KEGG; ngo:NGO_0387; -.
DR   PATRIC; fig|242231.10.peg.468; -.
DR   HOGENOM; CLU_062816_1_1_4; -.
DR   OMA; PCSQGMS; -.
DR   BRENDA; 3.5.4.16; 3590.
DR   UniPathway; UPA00848; UER00151.
DR   EvolutionaryTrace; Q5F9K6; -.
DR   Proteomes; UP000000535; Chromosome.
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   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   PANTHER; PTHR36445; PTHR36445; 1.
DR   Pfam; PF02649; GCHY-1; 1.
DR   TIGRFAMs; TIGR00294; TIGR00294; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..257
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000147714"
FT   SITE            147
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000250"
FT   STRAND          18..34
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          37..51
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   HELIX           61..69
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   HELIX           76..90
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          93..108
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          115..129
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          132..146
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   HELIX           148..153
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          160..173
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   HELIX           177..185
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   HELIX           198..210
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   HELIX           215..228
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          232..241
FT                   /evidence="ECO:0007829|PDB:5K9G"
FT   STRAND          246..256
FT                   /evidence="ECO:0007829|PDB:5K9G"
SQ   SEQUENCE   257 AA;  28747 MW;  A0235399C3EDF2A9 CRC64;
     MNAIADVQSS RDLRNLPINQ VGIKDLRFPI TLKTAEGTQS TVARLTMTVY LPAEQKGTHM
     SRFVALMEQH TEVLDFAQLH RLTAEMVALL DSRAGKISVS FPFFRKKTAP VSGIRSLLDY
     DVSLTGEMKD GAYGHSMKVM IPVTSLCPCS KEISQYGAHN QRSHVTVSLT SDAEVGIEEV
     IDYVETQASC QLYGLLKRPD EKYVTEKAYE NPKFVEDMVR DVATSLIADK RIKSFVVESE
     NFESIHNHSA YAYIAYP