ID   GCH4_EXISA              Reviewed;         303 AA.
AC   C4KZ55;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=EAT1b_1441;
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=360911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b;
RX   PubMed=21460088; DOI=10.1128/jb.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ70368.1; -; Genomic_DNA.
DR   RefSeq; WP_012727487.1; NC_012673.1.
DR   AlphaFoldDB; C4KZ55; -.
DR   SMR; C4KZ55; -.
DR   STRING; 360911.EAT1b_1441; -.
DR   KEGG; eat:EAT1b_1441; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_9; -.
DR   OrthoDB; 9774824at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000716; 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   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..303
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_1000215390"
FT   SITE            183
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   303 AA;  33959 MW;  4DC671B653EB9A38 CRC64;
     MSTSHVALPT KAERHKLFGS VPPIKGTKPT EKEQMVDLQN TPKNFLFALD SVGISNVKHP
     VNVETPEGVQ STVATFELTT SLVQDRKGIN MSRLTEQLDA YHQQGWTVSN RSLIEFAQEL
     AERMEQTEGQ LTIRYPWFFT RKAPATGLSG LMNADVMHRV TYNLETGVAN VTVGLVINVT
     TLCPCSKEIS EYSAHNQRGY ITIEAGLDET SMDGFDWRAA LLDAAESNAS APLHPVLKRP
     DEKRATEIAY ENPRFVEDMV RLIAADLYEM KQVVNFFVEC RNEESIHQHD AIASITFDKR
     QDA
//