ID   GCH12_PSEPK             Reviewed;         186 AA.
AC   Q88JY1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=GTP cyclohydrolase 1 2 {ECO:0000255|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I 2 {ECO:0000255|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I 2 {ECO:0000255|HAMAP-Rule:MF_00223};
GN   Name=folE2 {ECO:0000255|HAMAP-Rule:MF_00223};
GN   OrderedLocusNames=PP_2512;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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_00223};
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_00223}.
CC   -!- SUBUNIT: Homomer. {ECO:0000255|HAMAP-Rule:MF_00223}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000255|HAMAP-Rule:MF_00223}.
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; AE015451; AAN68124.1; -; Genomic_DNA.
DR   RefSeq; NP_744660.1; NC_002947.4.
DR   RefSeq; WP_010953446.1; NC_002947.4.
DR   AlphaFoldDB; Q88JY1; -.
DR   SMR; Q88JY1; -.
DR   STRING; 160488.PP_2512; -.
DR   PaxDb; 160488-PP_2512; -.
DR   GeneID; 83680902; -.
DR   KEGG; ppu:PP_2512; -.
DR   PATRIC; fig|160488.4.peg.2667; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_3_1_6; -.
DR   OrthoDB; 9801207at2; -.
DR   PhylomeDB; Q88JY1; -.
DR   BioCyc; PPUT160488:G1G01-2695-MONOMER; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.286.10; -; 1.
DR   Gene3D; 3.30.1130.10; -; 1.
DR   HAMAP; MF_00223; FolE; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR043134; GTP-CH-I_N.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR   InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR   NCBIfam; TIGR00063; folE; 1.
DR   PANTHER; PTHR11109:SF7; GTP CYCLOHYDROLASE 1; 1.
DR   PANTHER; PTHR11109; GTP CYCLOHYDROLASE I; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Nucleotide-binding; One-carbon metabolism;
KW   Reference proteome.
FT   CHAIN           1..186
FT                   /note="GTP cyclohydrolase 1 2"
FT                   /id="PRO_0000119431"
SQ   SEQUENCE   186 AA;  20886 MW;  D4F2562CC214F0F7 CRC64;
     MSHSLAEHYH EILVGIGENP QREGLLDTPR RAAKAMQYLC NGYAQDLHEV VNGALFESEN
     DEMIVVRDIE LYSLCEHHML PFIGKAHVAY LPTGRVLGLS KVARVVDMFA RRLQIQENLT
     RQIAYAVQEV TDAAGVGVVI EAKHMCMMMR GVEKQNSVMI SSVMLGAFRD APSTRHEFLN
     LIGRHN
//