ID   GCH4_GEOSL              Reviewed;         258 AA.
AC   Q74FW8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=GSU0484;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR33816.1; -; Genomic_DNA.
DR   RefSeq; NP_951543.3; NC_002939.5.
DR   RefSeq; WP_010941152.1; NC_002939.5.
DR   AlphaFoldDB; Q74FW8; -.
DR   SMR; Q74FW8; -.
DR   STRING; 243231.GSU0484; -.
DR   EnsemblBacteria; AAR33816; AAR33816; GSU0484.
DR   KEGG; gsu:GSU0484; -.
DR   PATRIC; fig|243231.5.peg.483; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_7; -.
DR   InParanoid; Q74FW8; -.
DR   OMA; PCSQGMS; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0003933; F:GTP cyclohydrolase activity; IBA:GO_Central.
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..258
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000147710"
FT   SITE            144
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   258 AA;  29522 MW;  535E194C25AB1C4A CRC64;
     MPDMQTSRDT RKIPISKVGV KDISYPIVVM DKNRKFQQTV ARVNMYVDLP HHFKGTHMSR
     FIEILNAYRE DIALDKMEPI LQEMKKKLGA SSAHLEIEFP YFIEKRAPVS GARSLMEYTC
     TFTGTLAETF DFVLGVQVPV TSLCPCSKEL SRYGAHNQRS HITVRVRYAG FVWIEELVEL
     IEGCGSSPVW SLLKRADEKF VTERAYENPK FVEDIVREAT LALAAHEAIT WFSVEAENFE
     SIHKHSAYAA IEQDKRKA