ID   RIBB_ECOUT              Reviewed;         217 AA.
AC   Q1R6T4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=UTI89_C3483;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE08930.1; -; Genomic_DNA.
DR   RefSeq; YP_542461.1; -.
DR   SMR; Q1R6T4; 4-217.
DR   GeneID; 3993889; -.
DR   GenomeReviews; CP000243_GR; UTI89_C3483.
DR   KEGG; eci:UTI89_C3483; -.
DR   HOGENOM; Q1R6T4; -.
DR   OMA; Q1R6T4; YGSGIVC.
DR   BioCyc; ECOL364106:UTI89_C3483-MON; -.
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    217       3,4-dihydroxy-2-butanone 4-phosphate
FT                                synthase.
FT                                /FTId=PRO_1000040607.
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   217 AA;  23339 MW;  C8220A407A342609 CRC64;
     MNQTLLSSFG TPFERVENAL AALREGRGVM VLDDEDRENE GDMIFPAETM TVEQMALTIR
     HGSGIVCLCI TDDRRKQLDL PMMVENNTSA YGTGFTVTIE AAEGVTTGVS AADRITTVRA
     AIADGAKPSD LNRPGHVFPL RAQAGGVLTR GGHTEATIDL MTLAGFKPAG VLCELTNDDG
     TMARAPECIE FANKHNMALV TIEDLVAYRQ AHERKAS
//