ID   RIBA_NEIMF              Reviewed;         197 AA.
AC   A1KU62;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=GTP cyclohydrolase-2;
DE            EC=3.5.4.25;
DE   AltName: Full=GTP cyclohydrolase II;
GN   Name=ribA; OrderedLocusNames=NMC1155;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 /
OS   FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C.,
RA   Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E.,
RA   Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S.,
RA   Unwin L., Whitehead S., Quail M.A., Achtman M., Barrell B.G.,
RA   Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM10403.1; -; Genomic_DNA.
DR   RefSeq; YP_975191.1; -.
DR   GeneID; 4676360; -.
DR   GenomeReviews; AM421808_GR; NMC1155.
DR   KEGG; nmc:NMC1155; -.
DR   OMA; A1KU62; QGFILYL.
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    197       GTP cyclohydrolase-2.
FT                                /FTId=PRO_1000040571.
FT   NP_BIND      50     54       GTP (By similarity).
FT   NP_BIND      93     95       GTP (By similarity).
FT   ACT_SITE    127    127       Proton acceptor (Potential).
FT   ACT_SITE    129    129       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      71     71       GTP (By similarity).
FT   BINDING     115    115       GTP (By similarity).
FT   BINDING     150    150       GTP (By similarity).
FT   BINDING     155    155       GTP (By similarity).
SQ   SEQUENCE   197 AA;  21930 MW;  FDC2DA4AF94C61EF CRC64;
     MSEMLNHVAS CRLPTEWGVF TMHGFEEANG QEHVALTVGN FSDGNPVLTR IHSECLTGDA
     LFSRKCDCGP QLEAAMRAVQ TEGRGIIVYL RQEGRGIGLI NKIRAYHLQD QGMDTVEANL
     ALGLPVDARD FRLAQSIYEY LGIRSVKLLT NNPEKIQTLK DAGINVVERI PLHVGENLEN
     KRYLQTKADK LGHLMSE
//