ID   GCH4_CERS5              Reviewed;         359 AA.
AC   A4WQ81;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Rsph17025_0639;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-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; CP000661; ABP69545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WQ81; -.
DR   SMR; A4WQ81; -.
DR   STRING; 349102.Rsph17025_0639; -.
DR   EnsemblBacteria; ABP69545; ABP69545; Rsph17025_0639.
DR   KEGG; rsq:Rsph17025_0639; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_1_5; -.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 757842at2; -.
DR   BioCyc; RSPH349102:G1G8M-660-MON; -.
DR   UniPathway; UPA00848; UER00151.
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.
FT   CHAIN           1..359
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_1000068669"
FT   SITE            218
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   359 AA;  40159 MW;  8B3657134040B156 CRC64;
     MNILTPVADR LPSREEAEEA LAVLRRWAKH TPVSDVAGLA PDVPALVYPE FSRSYPRNFT
     VDEAYKASLP DLQNGPASLI VGAKAVIQHV GISNFRLPIR YHTRDNGDLT LETSVTGTVS
     LEAEKKGINM SRIMRSFYAH AEQGFSFEVI ERALEDYKRD LESFDARIQM RFSFPVKVPS
     LRSGLVGWQY YDIALELVDR GGVRKKIMHL DFVYSSTCPC SLELSEHARR ERGQLATPHS
     QRSVARISVE VRPGKCLWFE DLIELARAAV PTETQVMVKR EDEQAFAELN AANPIFVEDA
     ARSFCQALQA DPRIGDFRVV ASHQESLHSH DAVSVLTEGP TFAAESLDPR LFASLYHTG