ID RISB_RENSM Reviewed; 159 AA. AC A9WR65; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 14-DEC-2022, entry version 80. 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}; GN OrderedLocusNames=RSal33209_2344; OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / OS NBRC 15589 / NCIMB 2235). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium. OX NCBI_TaxID=288705; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235; RX PubMed=18723615; DOI=10.1128/jb.00721-08; RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.; RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests RT reductive evolution away from an environmental Arthrobacter ancestor."; RL J. Bacteriol. 190:6970-6982(2008). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000910; ABY24074.1; -; Genomic_DNA. DR RefSeq; WP_012245737.1; NC_010168.1. DR AlphaFoldDB; A9WR65; -. DR SMR; A9WR65; -. DR STRING; 288705.RSal33209_2344; -. DR EnsemblBacteria; ABY24074; ABY24074; RSal33209_2344. DR KEGG; rsa:RSal33209_2344; -. DR eggNOG; COG0054; Bacteria. DR HOGENOM; CLU_089358_1_1_11; -. DR OMA; CQGVTQG; -. DR OrthoDB; 1680292at2; -. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000002007; 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; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE; 1. DR Pfam; PF00885; DMRL_synthase; 1. DR SUPFAM; SSF52121; Lumazine synthase; 1. DR TIGRFAMs; TIGR00114; lumazine-synth; 1. PE 3: Inferred from homology; KW Reference proteome; Riboflavin biosynthesis; Transferase. FT CHAIN 1..159 FT /note="6,7-dimethyl-8-ribityllumazine synthase" FT /id="PRO_1000077245" FT ACT_SITE 88 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178" FT BINDING 26 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178" FT BINDING 58..60 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178" FT BINDING 80..82 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178" FT BINDING 85..86 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178" FT BINDING 113 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178" FT BINDING 127 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178" SQ SEQUENCE 159 AA; 16339 MW; B9AE0B824EAFEDD3 CRC64; MSGAGAPVSP QLNAKGLELV IIAASWHEKV MNGLLDGALR AARDAGIEEP RIVRVPGSFE LPVAAARLAP DYDAVVALGV VIRGGTPHFE YVCQAATSGL TEVSVRTGVP VGFGLLTCDN DQQALDRAGL PAAPGFAGSK EDKGYEATSA ALETALTLR //