ID   RIBB_BAUCH              Reviewed;         211 AA.
AC   Q1LSL6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
DE            Short=DHBP synthase;
DE            EC=4.1.99.12;
GN   Name=ribB; OrderedLocusNames=BCI_0623;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
CC       formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC       dihydroxybutan-2-one 4-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 3,4-
CC       dihydroxy-2-butanone 4-phosphate from D-ribulose 5-phosphate: step
CC       1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the DHBP synthase family.
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DR   EMBL; CP000238; ABF14246.1; -; Genomic_DNA.
DR   RefSeq; YP_589048.1; -.
DR   SMR; Q1LSL6; 5-209.
DR   GeneID; 4056350; -.
DR   GenomeReviews; CP000238_GR; BCI_0623.
DR   KEGG; bci:BCI_0623; -.
DR   HOGENOM; Q1LSL6; -.
DR   OMA; Q1LSL6; YGSGIVC.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate syntha...; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00180; -; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   Gene3D; G3DSA:3.90.870.10; DHBP_synth_RibB-like_a/b_dom; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   ProDom; PD003034; DHBP_synthase; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lyase; Magnesium; Manganese; Metal-binding;
KW   Riboflavin biosynthesis.
FT   CHAIN         1    211       3,4-dihydroxy-2-butanone 4-phosphate
FT                                synthase.
FT                                /FTId=PRO_1000040596.
FT   REGION       37     38       Substrate binding (By similarity).
FT   REGION      150    154       Substrate binding (By similarity).
FT   METAL        38     38       Magnesium or manganese 1 (By similarity).
FT   METAL        38     38       Magnesium or manganese 2 (By similarity).
FT   METAL       153    153       Magnesium or manganese 2 (By similarity).
FT   BINDING      42     42       Substrate (By similarity).
FT   BINDING     174    174       Substrate (By similarity).
FT   SITE        136    136       Essential for catalytic activity (By
FT                                similarity).
FT   SITE        174    174       Essential for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   211 AA;  23094 MW;  55D255123CB83D18 CRC64;
     MNQIIFSQFG TPIERVEIAL QALRHGRGVL VLDNEDRENE GDMIFAAEKM TIEQMALAIR
     YGSGIICLCL TEERRQQLEL PMMVEHNTSH YQTAFTVTIE AAEGVTTGVS AADRITTIRT
     AIKNDAIPED LNRPGHVFPL LAQPGGVLNR GGHTEAAIDL TLLAGLKPAG VLCEVTNEDG
     SMARALEIIA FSNQHNMPVL TINDLVAYRS R
//