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 10-MAY-2017, entry version 61. 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; OC 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., RA Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., RA Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.; RT "Genome sequence of the fish pathogen Renibacterium salmoninarum RT suggests reductive evolution away from an environmental Arthrobacter RT ancestor."; RL J. Bacteriol. 190:6970-6982(2008). CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8- CC ribityllumazine by condensation of 5-amino-6-(D- CC ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. CC This is the penultimate step in the biosynthesis of riboflavin. CC {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- CATALYTIC ACTIVITY: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5- CC amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D- CC ribityl)lumazine + 2 H(2)O + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00178}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin 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. CC {ECO:0000255|HAMAP-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 ProteinModelPortal; A9WR65; -. DR SMR; A9WR65; -. DR STRING; 288705.RSal33209_2344; -. DR EnsemblBacteria; ABY24074; ABY24074; RSal33209_2344. DR KEGG; rsa:RSal33209_2344; -. DR PATRIC; 23078055; VBIRenSal21953_2441. DR eggNOG; ENOG4108UTT; Bacteria. DR eggNOG; COG0054; LUCA. DR HOGENOM; HOG000229253; -. DR KO; K00794; -. DR OMA; MFGADKG; -. DR OrthoDB; POG091H021R; -. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000002007; Chromosome. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.960; -; 1. DR HAMAP; MF_00178; Lumazine_synth; 1. DR InterPro; IPR002180; LS/RS. DR Pfam; PF00885; DMRL_synthase; 1. DR SUPFAM; SSF52121; SSF52121; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Riboflavin biosynthesis; KW Transferase. FT CHAIN 1 159 6,7-dimethyl-8-ribityllumazine synthase. FT /FTId=PRO_1000077245. FT REGION 58 60 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 80 82 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 85 86 1-deoxy-L-glycero-tetrulose 4-phosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT ACT_SITE 88 88 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT BINDING 26 26 5-amino-6-(D-ribitylamino)uracil. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 113 113 5-amino-6-(D-ribitylamino)uracil; via FT amide nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 127 127 1-deoxy-L-glycero-tetrulose 4-phosphate. FT {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 //