ID   GCH4_PSE14              Reviewed;         301 AA.
AC   Q48HN1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=PSPPH_2920;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ37560.1; -; Genomic_DNA.
DR   RefSeq; WP_011168867.1; NC_005773.3.
DR   AlphaFoldDB; Q48HN1; -.
DR   SMR; Q48HN1; -.
DR   STRING; 264730.PSPPH_2920; -.
DR   EnsemblBacteria; AAZ37560; AAZ37560; PSPPH_2920.
DR   KEGG; psp:PSPPH_2920; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_0_6; -.
DR   OMA; AKGIHMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000551; 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..301
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289511"
FT   SITE            156
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   301 AA;  32977 MW;  CE1ED3975FF7C27E CRC64;
     MNNPLPDVAL TEVSSALVSL DWVGMQGVEV PVRLAEAGVR YPVHAHVDLQ VDLADPSVKG
     IHMSRLYRLL DRYAEHQILS PDTLGALLEA MVESHLDCHS SRARLTLSFN LLCRRPALIT
     EGLSGWKSYP VKLDATWHAG RLCLDVSADI TYSSTCPCSA ALSRQLLEGA FTARFGRQSF
     VDPMQVATWL RENASFATPH SQRSVATVQV RVAEQATELG LMTLIDAVEQ ALGTPVQTAV
     KRADEQAFAR LNGQNLMYVE DAARKVQQAL EGRYAASSVS VRHFESLHPH DAAAQTSNYL
     S