ID   GCH4_RUEPO              Reviewed;         367 AA.
AC   Q5LTR1;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=SPO1352;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV94640.1; -; Genomic_DNA.
DR   RefSeq; WP_011047090.1; NC_003911.12.
DR   AlphaFoldDB; Q5LTR1; -.
DR   SMR; Q5LTR1; -.
DR   STRING; 246200.SPO1352; -.
DR   EnsemblBacteria; AAV94640; AAV94640; SPO1352.
DR   KEGG; sil:SPO1352; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_1_5; -.
DR   OMA; AKGIHMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001023; 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..367
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000147723"
FT   SITE            225
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   367 AA;  40860 MW;  02B274509D4DE7B1 CRC64;
     MNLHPRDIDE TPDRDAAAAA LAVLRRWASG ATSTEISELD PSVARLLPDA ALSNYPDLSR
     QYPEDFTVDA TYRAGLPDLQ NGPSSLIRGA KQQIQHVGIS NFRLPIRFHR KEGDDLTLET
     SVTGTVSLEA GKKGINMSRI MRSFYKHAER TFSFEVIEAA LDDYMTDLDS FDARIQMRFS
     YPERIESLRS GLSGYQYYDI ALELVEQGGE RLKIMHLDYV YSSTCPCSLE LSEHARSSRG
     QLATPHSQRS VARLSVVVDG DASCLWFEDL IALCRRAVPT ETQVMVKRED EQAFAELNAA
     NPIFVEDAAR LFCAELLADH RIGDFRVVAS HQESLHSHDA VSVLTEGATF ATASLDPRLF
     ATLFHVG