ID   RIBA_CAMFF              Reviewed;         195 AA.
AC   A0RR75;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=GTP cyclohydrolase-2;
DE            EC=3.5.4.25;
DE   AltName: Full=GTP cyclohydrolase II;
GN   Name=ribA; OrderedLocusNames=CFF8240_1575;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000487; ABK81791.1; -; Genomic_DNA.
DR   RefSeq; YP_892708.1; -.
DR   GeneID; 4538031; -.
DR   GenomeReviews; CP000487_GR; CFF8240_1575.
DR   KEGG; cff:CFF8240_1575; -.
DR   NMPDR; fig|360106.5.peg.1507; -.
DR   TIGR; CFF8240_1575; -.
DR   OMA; A0RR75; YEIVEFI.
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    195       GTP cyclohydrolase-2.
FT                                /FTId=PRO_1000040557.
FT   NP_BIND      48     52       GTP (By similarity).
FT   NP_BIND      90     92       GTP (By similarity).
FT   ACT_SITE    124    124       Proton acceptor (Potential).
FT   ACT_SITE    126    126       Nucleophile (By similarity).
FT   METAL        53     53       Zinc; catalytic (By similarity).
FT   METAL        64     64       Zinc; catalytic (By similarity).
FT   METAL        66     66       Zinc; catalytic (By similarity).
FT   BINDING      69     69       GTP (By similarity).
FT   BINDING     112    112       GTP (By similarity).
FT   BINDING     147    147       GTP (By similarity).
FT   BINDING     152    152       GTP (By similarity).
SQ   SEQUENCE   195 AA;  22228 MW;  57B11CC0AB21A647 CRC64;
     MEIIKSNIAN LPSRFGKFQI KSYKEGCCKE HLTIFSPNLD VTKTVNVRIH SECLTGDAIG
     SLKCDCRDQL EASLKYINKH GGMVIYLRQE GRNIGLLNKV NAYALQDNGL DTIEANHQLG
     FKADERTYEI VDFILKDFGI KSINLLTNNP LKLASLTCVN IEKRIPIEIE SNEFNKDYLK
     VKKEQMGHML DEFTR
//