ID   GCH4_CALBD              Reviewed;         256 AA.
AC   B9MNP4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Athe_0441;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL   Submitted (JAN-2009) 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; CP001393; ACM59573.1; -; Genomic_DNA.
DR   RefSeq; WP_015907036.1; NC_012034.1.
DR   AlphaFoldDB; B9MNP4; -.
DR   SMR; B9MNP4; -.
DR   STRING; 521460.Athe_0441; -.
DR   EnsemblBacteria; ACM59573; ACM59573; Athe_0441.
DR   GeneID; 31771799; -.
DR   KEGG; ate:Athe_0441; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_9; -.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000007723; 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..256
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_1000185150"
FT   SITE            143
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   256 AA;  29756 MW;  2027B4E8614761B0 CRC64;
     MIDVQSQKDQ RGISIQKVGI KDLNWPIVVM DRENKTQTTI AKIIAAAELK GDIRGTHMSR
     FIEAIDELKV VGPKEIEKLL DRIKEKLNSE KAYIRFDFPY FINKRTPVTA TLSPLKVDCY
     FEAEKDQKFD LKVGVIVPVH TLCPCSKEIS EYGAHNQRAY VTIEVRMKKF MWIEELVEIA
     EASASCPLYS ILKRPDEKWV TERAYQNPRF VEDLLREVVL KMKEDGRIKW YKVFVESIES
     IHNHNAFAYI EGEITK