ID   GCH11_PSEAE             Reviewed;         186 AA.
AC   Q9HYG8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=GTP cyclohydrolase 1 1;
DE            EC=3.5.4.16;
DE   AltName: Full=GTP cyclohydrolase I 1;
DE            Short=GTP-CH-I 1;
GN   Name=folE1; OrderedLocusNames=PA3438;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC   -!- SUBUNIT: Homomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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; AE004091; AAG06826.1; -; Genomic_DNA.
DR   PIR; D83217; D83217.
DR   RefSeq; NP_252128.1; NC_002516.2.
DR   RefSeq; WP_003091896.1; NZ_QZGE01000037.1.
DR   AlphaFoldDB; Q9HYG8; -.
DR   SMR; Q9HYG8; -.
DR   STRING; 287.DR97_4484; -.
DR   PaxDb; Q9HYG8; -.
DR   PRIDE; Q9HYG8; -.
DR   EnsemblBacteria; AAG06826; AAG06826; PA3438.
DR   GeneID; 878765; -.
DR   KEGG; pae:PA3438; -.
DR   PATRIC; fig|208964.12.peg.3599; -.
DR   PseudoCAP; PA3438; -.
DR   HOGENOM; CLU_049768_3_1_6; -.
DR   InParanoid; Q9HYG8; -.
DR   OMA; VACVIDA; -.
DR   PhylomeDB; Q9HYG8; -.
DR   BioCyc; PAER208964:G1FZ6-3505-MON; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
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   PANTHER; PTHR11109; PTHR11109; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   TIGRFAMs; TIGR00063; folE; 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 1"
FT                   /id="PRO_0000119428"
SQ   SEQUENCE   186 AA;  20833 MW;  1F53E719217C519F CRC64;
     MNPALSQHYR EILVGLGEDP QREGLLDTPK RAAKAMQYLC HGYGQTLEEI VNGALFASDN
     DEMVIVRDIE LYSLCEHHLL PFIGKAHVAY IPTGKVLGLS KVARIVDMFA RRLQIQENLT
     RQIAEAVRQV TSAAGVAVVI EAQHMCMMMR GVEKQNSQMF TSVMLGAFRD SNTTRQEFLQ
     LIGRSK