ID   GCH4_DELAS              Reviewed;         296 AA.
AC   A9C020;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Daci_3650;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) 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; CP000884; ABX36282.1; -; Genomic_DNA.
DR   RefSeq; WP_012205478.1; NC_010002.1.
DR   AlphaFoldDB; A9C020; -.
DR   SMR; A9C020; -.
DR   STRING; 398578.Daci_3650; -.
DR   PRIDE; A9C020; -.
DR   EnsemblBacteria; ABX36282; ABX36282; Daci_3650.
DR   KEGG; dac:Daci_3650; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_0_4; -.
DR   OMA; AKGIHMS; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000784; 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..296
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000372026"
FT   SITE            156
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   296 AA;  32306 MW;  978F17C3BFB5352F CRC64;
     MLAPLPDVSL TDPAPSLSPL QWVGMQGIDL PVTVAEPGYW RELHARADVQ VDLPAAHVKG
     IHMSRLYRQL DSLAEESALS ALALRHALQA MIDSHLDCQS RSARMRLSLD LLAQRPALVT
     HDLSGWKSYP VRLDATLAQG VFQLRLQVGV GYSSTCPCSA ALSRQLLEQG FLQAFAGEPL
     VEPDQVASWL RRHGTLATAH SQRSEAQVSV DLACDAPDLG ILPLIARVEQ ALGTPVQTAV
     KRADEQAFAA LNGRNLMFVE DAARRIQAAL EGIYARPRVH VRHMESLHPH DAVAWA