ID   GCH4_PARP8              Reviewed;         268 AA.
AC   B2JP67;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, 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=Bphy_3947;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(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; CP001044; ACC73070.1; -; Genomic_DNA.
DR   RefSeq; WP_012403243.1; NZ_CADFGH010000005.1.
DR   AlphaFoldDB; B2JP67; -.
DR   SMR; B2JP67; -.
DR   STRING; 391038.Bphy_3947; -.
DR   KEGG; bph:Bphy_3947; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_4; -.
DR   OrthoDB; 9774824at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001192; Chromosome 2.
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; Reference proteome.
FT   CHAIN           1..268
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000372025"
FT   SITE            154
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   268 AA;  30032 MW;  9F0C46D021A72010 CRC64;
     MNQMNPAFVM PDVQSTVDTR QIPIQRVGVK AVRHPLTVRT PDGSAQPTVG TWNLDVHLPA
     EVKGTHMSRF VALLEENKAP LDSSAFRALL TSMLEKLEAP AGRIEVSFPY FVNKTAPVSG
     VQSLLDYEVS LMGDSRDGAT RLFLKVLVPV TSLCPCSKKI SQYGAHNQRS HVTINAELID
     DVPVEDLIRI AEEEASCELW GLLKRPDEKF VTERAYENPK FVEDLVRDVA QRLNDDHRIV
     AYVLEAENFE SIHNHSAYAV IESDKRLR
//