ID   GCH4_CERS1              Reviewed;         359 AA.
AC   A3PH01;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=Rsph17029_0501;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
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   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-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; CP000577; ABN75617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3PH01; -.
DR   SMR; A3PH01; -.
DR   KEGG; rsh:Rsph17029_0501; -.
DR   HOGENOM; CLU_062816_0_1_5; -.
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   Gene3D; 3.10.270.10; Urate Oxidase; 1.
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; GTP CYCLOHYDROLASE MPTA; 1.
DR   PANTHER; PTHR36445:SF1; GTP CYCLOHYDROLASE MPTA; 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_0000292756"
FT   SITE            218
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   359 AA;  40175 MW;  FFD98B7D831BBBE2 CRC64;
     MNILTPVAER LPSREEAEEA LAVLRRWATH TPASDVAALA PEAPALVYPD LSRAYPRTFT
     VDEAYKASLP DLQNGPASLI VGAKAVIQHV GISNFRLPIR YHTRDNGDLQ LETSVTGTVS
     LEAEKKGINM SRIMRSFYAH AEQAFSFEVI ERALEDYKRD LESFDARIQM RFSFPVKVPS
     LRSGLTGWQY YDIALELVDR GGVRKEIMHL DFVYSSTCPC SLELSEHARR ERGQLATPHS
     QRSVARISVE VRQGKCLWFE DLLDLVRSAV PTETQVMVKR EDEQAFAELN AANPIFVEDA
     ARSFCQALQS DPRIGDFRVV ASHQESLHSH DAVSVLTEGP TFAAESLDPR LFSSLYHVG
//