ID   GCH4_RUTMC              Reviewed;         264 AA.
AC   A1AVX5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=Rmag_0304;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthturnera.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
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; CP000488; ABL02082.1; -; Genomic_DNA.
DR   RefSeq; WP_011737707.1; NC_008610.1.
DR   AlphaFoldDB; A1AVX5; -.
DR   SMR; A1AVX5; -.
DR   STRING; 413404.Rmag_0304; -.
DR   KEGG; rma:Rmag_0304; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_6; -.
DR   OrthoDB; 9774824at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002587; 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..264
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289520"
FT   SITE            150
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   264 AA;  29971 MW;  B6245A9B22438F98 CRC64;
     MSAIHLPDTQ NSADTRQIII DKVGIKDITH PITYIDCDGN KIPTIGIFTM TVSLSERVKG
     THMSRFIEIL NEGPCEFSAH NFDKIIDKVR KRLESDIAHI TLNFTFFRRK KAPSSGVESM
     MDYQVTLYGT LNKDEVQVMM KVVVPVTSLC PCSKSISKYG AHNQRSHITI KAKAAKDKTL
     HIEDLIDLAE RKASCELYAI LKRDDEKVVT ERAYDNPAFV EDLVRDIAVD LNADDKISYY
     RLESENFESI HNHSAYALIE NQKC
//