ID   GCH4_COPPD              Reviewed;         271 AA.
AC   B5Y6R9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
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};
GN   OrderedLocusNames=COPRO5265_0095;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS   BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC   Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus strain
RT   ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) 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; CP001145; ACI18177.1; -; Genomic_DNA.
DR   RefSeq; WP_012544827.1; NC_011295.1.
DR   AlphaFoldDB; B5Y6R9; -.
DR   SMR; B5Y6R9; -.
DR   STRING; 309798.COPRO5265_0095; -.
DR   EnsemblBacteria; ACI18177; ACI18177; COPRO5265_0095.
DR   KEGG; cpo:COPRO5265_0095; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_9; -.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001732; 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.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..271
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_1000215386"
FT   SITE            146
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   271 AA;  30811 MW;  A6F6425ADEA7D22F CRC64;
     MRDVQSERDP RNVPLDYVGI ENVRLPITVR TKEGGKQPTV GTFSIGVDFP HSFRGTHMSR
     FMEVLYQHLE EISQTRLRVT LEDIKERLKA TKAMIEVAFP FAIKKSTPVT KLETVMYVDA
     SFKAELNSTR GYVVTSTVTV PVHSLCPCSR DISEFGAHNQ RVDVTVSWQG DLWIEDVIAL
     VESSASQPLY PLLKRPDEKY VTEKAYLNPK FVEDIAKDLF LKLDPLSPCF RIKVVSYESI
     HPHNAVAIKE KRAEVSESSV RSNDQEHRDC T