ID   RIBA_SHESA              Reviewed;         203 AA.
AC   A0KYF8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, 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=Shewana3_2600;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-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; CP000469; ABK48827.1; -; Genomic_DNA.
DR   RefSeq; YP_870233.1; -.
DR   GeneID; 4478468; -.
DR   GenomeReviews; CP000469_GR; Shewana3_2600.
DR   KEGG; shn:Shewana3_2600; -.
DR   NMPDR; fig|94122.5.peg.2644; -.
DR   OMA; A0KYF8; 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    203       GTP cyclohydrolase-2.
FT                                /FTId=PRO_1000040585.
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   203 AA;  22838 MW;  64A796ECC4C79BBC CRC64;
     MSIKYVATSK LPTPWGVFAM HGFEDTETSK EHVALTFGTL SSDAPVLGRI HSECLTGDAL
     FSLRCDCGFQ LQTAMQNIAE TGSGFILYLR QEGRGIGLLN KIRAYELQDK GANTVEANEQ
     LGFPADMRKY DMIQPMLEQI GVKHVRLMTN NPRKVKAMKE IGIEVVERVP LQVGKNRYNE
     AYLKTKSTEL GHMMSEYHFT DEE
//