ID   GCH4_NEIMF              Reviewed;         298 AA.
AC   A1KT61;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   25-MAY-2022, entry version 66.
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}; OrderedLocusNames=NMC0755;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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=CAM10043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM421808; CAM10043.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A1KT61; -.
DR   SMR; A1KT61; -.
DR   EnsemblBacteria; CAM10043; CAM10043; NMC0755.
DR   KEGG; nmc:NMC0755; -.
DR   HOGENOM; CLU_062816_1_1_4; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002286; 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   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..298
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289499"
FT   SITE            188
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   298 AA;  33280 MW;  023BFD2A015B7CB4 CRC64;
     MQLLKASDII SHLQIDGIFP GGNAIPCTHL NNYMNIKEKQ LMNTIADVQS SRDLRNLPIN
     QVGIKDLRFP ITLQTAEGIQ STIARLTMTV YLPAEQKGTH MSRFVALMEQ HAEALDFAQL
     RKLTTEMVAL LDSRAGKISV SFPFFRKKTA PVSGIRSLLD YDVCLTGEIK DGAYGHSMKV
     MIPVTSLCPC SKEISQYGAH NQRSHVTVSL TADAEVGIEE VIDYVEAQAS CQLYGLLKRP
     DEKYVTEKAY ENPKFVEDMV RDVATSLIAD KRIKSFVVES ENFESIHNHS AYAYIAYP