ID   RIBA_PASMU              Reviewed;         219 AA.
AC   P57863;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=GTP cyclohydrolase-2;
DE            EC=3.5.4.25;
DE   AltName: Full=GTP cyclohydrolase II;
GN   Name=ribA; OrderedLocusNames=PM0677;
OS   Pasteurella multocida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   MEDLINE=21145866; PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02761.1; -; Genomic_DNA.
DR   RefSeq; NP_245614.1; -.
DR   GeneID; 1244024; -.
DR   GenomeReviews; AE004439_GR; PM0677.
DR   KEGG; pmu:PM0677; -.
DR   NMPDR; fig|272843.1.peg.677; -.
DR   HOGENOM; P57863; -.
DR   OMA; P57863; QGFILYL.
DR   BRENDA; 3.5.4.25; 258935.
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    219       GTP cyclohydrolase-2.
FT                                /FTId=PRO_0000151766.
FT   NP_BIND      51     55       GTP (By similarity).
FT   NP_BIND      94     96       GTP (By similarity).
FT   ACT_SITE    128    128       Proton acceptor (Potential).
FT   ACT_SITE    130    130       Nucleophile (By similarity).
FT   METAL        56     56       Zinc; catalytic (By similarity).
FT   METAL        67     67       Zinc; catalytic (By similarity).
FT   METAL        69     69       Zinc; catalytic (By similarity).
FT   BINDING      72     72       GTP (By similarity).
FT   BINDING     116    116       GTP (By similarity).
FT   BINDING     151    151       GTP (By similarity).
FT   BINDING     156    156       GTP (By similarity).
SQ   SEQUENCE   219 AA;  24634 MW;  EA76FC6FF716BF55 CRC64;
     MAKIQRVTEA NLPTEFGMFR IVGFEFPDTK KEHVALVLGE VENTDEPILA RIHSECLTGD
     ALYSLKCDCG FQLAAALRQI SQEGRGVLIY HREEGRGIGL INKIRAYSLQ DKGMDTIEAN
     LALGFAADER NFEVCADIFA LLGINKVRLL TNNPNKIDTM KKAGINIVER VALNVGENRY
     NTEYLDTKAK KMGHFIIHNQ QKYPLECPYC SEEVPVQEK
//