ID   GCH4_PSEE4              Reviewed;         293 AA.
AC   Q1I2L2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, 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}; OrderedLocusNames=PSEEN5515;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK18124.1; -; Genomic_DNA.
DR   RefSeq; WP_011536476.1; NC_008027.1.
DR   AlphaFoldDB; Q1I2L2; -.
DR   SMR; Q1I2L2; -.
DR   STRING; 384676.PSEEN5515; -.
DR   EnsemblBacteria; CAK18124; CAK18124; PSEEN5515.
DR   KEGG; pen:PSEEN5515; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_0_6; -.
DR   OMA; AKGIHMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000658; 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.
FT   CHAIN           1..293
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289508"
FT   SITE            149
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   293 AA;  32104 MW;  4F15FC121C52FA4D CRC64;
     MTSLTLPDIA AQSAQQPLPL DWVGMCGIAM PVQFEGRQLS ALADAGVSLD DGASRGIHMS
     RLYLALEALE RDTLTPRLIH QVLEQFLFSH EGLSASAHLR LQFDHLLKRP ALVSPLAGWK
     HYPVAIDARL KAEMFHVELS VEIPYSSTCP CSAALARQLI QERFDQDFTG QAVDRQGVRA
     WLGSSSGIVA TPHSQRSMAK LQVRLVGDEL PVTVLIDKAE AALGTAVQTA VKRADEQAFA
     LANGQNLMFC EDAARRLNLA LRQLDWVAGF TVRVEHAESL HAHDAVAVSR FQR