ID   GCH4_CITBB              Reviewed;         267 AA.
AC   B5EDQ6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Gbem_3692;
OS   Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS   Bem) (Geobacter bemidjiensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Citrifermentans.
OX   NCBI_TaxID=404380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-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}.
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; CP001124; ACH40684.1; -; Genomic_DNA.
DR   RefSeq; WP_012532122.1; NC_011146.1.
DR   AlphaFoldDB; B5EDQ6; -.
DR   SMR; B5EDQ6; -.
DR   STRING; 404380.Gbem_3692; -.
DR   EnsemblBacteria; ACH40684; ACH40684; Gbem_3692.
DR   KEGG; gbm:Gbem_3692; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_7; -.
DR   OMA; PCSQGMS; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000008825; 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; Reference proteome.
FT   CHAIN           1..267
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_1000185153"
FT   SITE            154
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   267 AA;  30890 MW;  5D17AC8F29B962FE CRC64;
     MIKEYLKKPS LSDVQLTRDT RNIPIGKVGV KDISYPIVVM DKNKSFQNTI ARINMYVDLP
     HHFKGTHMSR FVEILNEYRE EIALDKLELI LSTMKEKLGA SNAHLEMEFP YFVEKTAPVS
     RAKSLMEYTC TFSASLSDRF DFVLGIKVPV TSLCPCSKEL SSYGAHNQRS IMTVQVRYSE
     FIWIEDLIEI IEQCGSSPVY SLLKREDEKF VTERAYENPR FVEDMVREAT VRLLSMQNVT
     WFSVEAENFE SIHKHSAYAA IERSRES