ID   RIBA_HELPH              Reviewed;         192 AA.
AC   Q1CT68;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=GTP cyclohydrolase-2;
DE            EC=3.5.4.25;
DE   AltName: Full=GTP cyclohydrolase II;
GN   Name=ribA; OrderedLocusNames=HPAG1_0787;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S.,
RA   Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J.,
RA   Mardis E.R., Engstrand L.G., Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis
RT   Helicobacter pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000241; ABF84854.1; -; Genomic_DNA.
DR   RefSeq; YP_627528.1; -.
DR   GeneID; 4099067; -.
DR   GenomeReviews; CP000241_GR; HPAG1_0787.
DR   KEGG; hpa:HPAG1_0787; -.
DR   HOGENOM; Q1CT68; -.
DR   OMA; Q1CT68; YEIVEFI.
DR   BioCyc; HPYL357544:HPAG1_0787-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    192       GTP cyclohydrolase-2.
FT                                /FTId=PRO_1000040568.
FT   NP_BIND      50     54       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        55     55       Zinc; catalytic (By similarity).
FT   METAL        66     66       Zinc; catalytic (By similarity).
FT   METAL        68     68       Zinc; catalytic (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   192 AA;  21642 MW;  D752E2EA021428D9 CRC64;
     MKRLEVSNQA KLPTQFGEFC IQCFREKGSS GSKDHLVVFT PNFSQNPLVR LHSECLTGDA
     LGSQKCDCGG ALQMALERIS KEGGLVIYLR QEGRGIGLFN KVNAYALQDK GYDTIQANEM
     IGFKDDERDY SIAGEILEYY RIKKMRLLTN NPKKIAALEK YAEVTRESLI VCANEHNQGY
     LEVKKLKMGH LL
//