ID   RIBA_PSEE4              Reviewed;         205 AA.
AC   Q1IFL5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=GTP cyclohydrolase-2;
DE            EC=3.5.4.25;
DE   AltName: Full=GTP cyclohydrolase II;
GN   Name=ribA; OrderedLocusNames=PSEEN0596;
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].
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.,
RA   Wincker P., 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: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC       ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC       pyrophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
CC       hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 6,7-
CC       dimethyl-8-(1-D-ribityl)lumazine from GTP: step 1/4.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
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DR   EMBL; CT573326; CAK13539.1; -; Genomic_DNA.
DR   RefSeq; YP_606354.1; -.
DR   GeneID; 4090213; -.
DR   GenomeReviews; CT573326_GR; PSEEN0596.
DR   KEGG; pen:PSEEN0596; -.
DR   NMPDR; fig|384676.6.peg.519; -.
DR   HOGENOM; Q1IFL5; -.
DR   OMA; Q1IFL5; QGFILYL.
DR   BioCyc; PENT384676:PSEEN0596-MON; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00179; -; 1.
DR   InterPro; IPR000926; GTP_CycHdrlase_II.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   TIGRFAMs; TIGR00505; ribA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; GTP-binding; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Riboflavin biosynthesis; Zinc.
FT   CHAIN         1    205       GTP cyclohydrolase-2.
FT                                /FTId=PRO_1000040574.
FT   NP_BIND      49     53       GTP (By similarity).
FT   NP_BIND      92     94       GTP (By similarity).
FT   ACT_SITE    126    126       Proton acceptor (Potential).
FT   ACT_SITE    128    128       Nucleophile (By similarity).
FT   METAL        54     54       Zinc; catalytic (By similarity).
FT   METAL        65     65       Zinc; catalytic (By similarity).
FT   METAL        67     67       Zinc; catalytic (By similarity).
FT   BINDING      70     70       GTP (By similarity).
FT   BINDING     114    114       GTP (By similarity).
FT   BINDING     149    149       GTP (By similarity).
FT   BINDING     154    154       GTP (By similarity).
SQ   SEQUENCE   205 AA;  22409 MW;  81C12C12EB8AA688 CRC64;
     MPVVFVAASK LPTPFAIFTM HGFLDEATGR EHVVLSLGDI ADGEPVLGRL HSECLTGDAL
     FSQRCDCGSQ LEAALQAIAR EGRGVLLYLR QEGRGIGLLN KIRAYELQDG GADTVEANER
     LGFAADQRDY AMCLPMLEHL GVKSLRLMTN NPRKVKALTD MSIKVAERVP LHTGHNPHNR
     LYLATKADKL GHMMGNKHQG EVPQA
//