ID   RISB_FLAJ1              Reviewed;         190 AA.
AC   A5FNH3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE            Short=DMRL synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE            Short=LS {ECO:0000255|HAMAP-Rule:MF_00178};
DE            Short=Lumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE            EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178};
GN   Name=ribH {ECO:0000255|HAMAP-Rule:MF_00178}; OrderedLocusNames=Fjoh_0212;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
CC   -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by
CC       condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-
CC       butanone 4-phosphate. This is the penultimate step in the biosynthesis
CC       of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
CC         ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2
CC         H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00178};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC       from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC       ribitylamino)uracil: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00178}.
CC   -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00178}.
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DR   EMBL; CP000685; ABQ03249.1; -; Genomic_DNA.
DR   RefSeq; WP_012022320.1; NZ_MUGZ01000005.1.
DR   AlphaFoldDB; A5FNH3; -.
DR   SMR; A5FNH3; -.
DR   STRING; 376686.Fjoh_0212; -.
DR   EnsemblBacteria; ABQ03249; ABQ03249; Fjoh_0212.
DR   KEGG; fjo:Fjoh_0212; -.
DR   eggNOG; COG0054; Bacteria.
DR   HOGENOM; CLU_089358_1_2_10; -.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 1680292at2; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR   GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd09209; Lumazine_synthase-I; 1.
DR   Gene3D; 3.40.50.960; -; 1.
DR   HAMAP; MF_00178; Lumazine_synth; 1.
DR   InterPro; IPR034964; LS.
DR   InterPro; IPR002180; LS/RS.
DR   InterPro; IPR036467; LS/RS_sf.
DR   PANTHER; PTHR21058; PTHR21058; 1.
DR   Pfam; PF00885; DMRL_synthase; 1.
DR   SUPFAM; SSF52121; SSF52121; 1.
DR   TIGRFAMs; TIGR00114; lumazine-synth; 1.
PE   3: Inferred from homology;
KW   Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..190
FT                   /note="6,7-dimethyl-8-ribityllumazine synthase"
FT                   /id="PRO_1000077234"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         31
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         65..67
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         89..91
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         94..95
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         122
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         136
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
SQ   SEQUENCE   190 AA;  20961 MW;  8B8E41D9E2D7E03F CRC64;
     MATENKNLSE YDKNTIPNAK DFRFGIVVSE WNDVITEGLY NGAFEALIDC DVPAQQIIRW
     NVPGSFELIY GAKKMLQTQN VDAVIVIGCV IQGETKHFDF VCEGVTQGIK DLNVQTDIPV
     IFCVLTDNNM QQSIDRSGGV HGNKGTEAAI AAIKMAYIRQ QASISHPFNQ PLLSSGALQI
     EETPIKIEKE