ID   RIBB_HAEI8              Reviewed;         215 AA.
AC   Q4QMD5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=NTHI0925;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87812.1; -; Genomic_DNA.
DR   RefSeq; YP_248472.1; -.
DR   GeneID; 3430234; -.
DR   GenomeReviews; CP000057_GR; NTHI0925.
DR   KEGG; hit:NTHI0925; -.
DR   HOGENOM; Q4QMD5; -.
DR   OMA; Q4QMD5; YGSGIVC.
DR   BioCyc; HINF281310:NTHI0925-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    215       3,4-dihydroxy-2-butanone 4-phosphate
FT                                synthase.
FT                                /FTId=PRO_1000040610.
FT   REGION       38     39       Substrate binding (By similarity).
FT   REGION      151    155       Substrate binding (By similarity).
FT   METAL        39     39       Magnesium or manganese 1 (By similarity).
FT   METAL        39     39       Magnesium or manganese 2 (By similarity).
FT   METAL       154    154       Magnesium or manganese 2 (By similarity).
FT   BINDING      43     43       Substrate (By similarity).
FT   BINDING     175    175       Substrate (By similarity).
FT   SITE        137    137       Essential for catalytic activity (By
FT                                similarity).
FT   SITE        175    175       Essential for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   215 AA;  23281 MW;  D64A5C8BD9FBAF2A CRC64;
     MNQSILSPFG NTAEERVLNA INAFKHGTGV LVLDDEDREN EGDLIFPAET ITSEQMAKLI
     RYGSGIVCLC ITDERCQQLD LPPMVEHNNS VNKTAFTVTI EAAKGVSTGV SAADRVTTIQ
     TAIADNAVPT DLHRPGHVFP LRAANGGVLT RRGHTEASVD LARLAGFKEA GVICEITNDD
     GTMARTPEIV EFAKKFGYSV LTIEDLVEYR LAHNI
//