ID   GCH4_POLAQ              Reviewed;         272 AA.
AC   A4SZK2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
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=Pnuc_1703;
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA   Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA   Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34916.1; -; Genomic_DNA.
DR   RefSeq; WP_011903539.1; NC_009379.1.
DR   AlphaFoldDB; A4SZK2; -.
DR   SMR; A4SZK2; -.
DR   GeneID; 31482092; -.
DR   KEGG; pnu:Pnuc_1703; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_4; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000231; 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; Reference proteome.
FT   CHAIN           1..272
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000372033"
FT   SITE            159
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   272 AA;  30294 MW;  05B8FBEFE86CD2A0 CRC64;
     MNPAFLKASA MPDVQSSRDE RALPIEQVGI RGVRHPLMIR SNTGNFPSVG NFEMDVALPA
     HVKGTHMSRF MALLQKQDEA IDSTTVVALV RDMLPLLDAK EGHVQFTYTH FVKKAAPVSG
     VESLMDYEVT WMATAKQNDA GSVEVELGLR AQVPVMSLCP CSKEISEFGA HNQRSHVTMT
     VVLDTQTKMT VEDLVSAAER EASSELWGLL KRPDEKWVTE RSYSNPKFVE DLVRDVAGRL
     KADTRIQSFV VDAENFESIH NHSAFARISH KK
//