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 16-NOV-2011, entry version 28. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase; DE Short=DMRL synthase; DE Short=Lumazine synthase; DE EC=2.5.1.9; DE AltName: Full=Riboflavin synthase beta chain; GN Name=ribH; OrderedLocusNames=RSal33209_2344; OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 OS / NBRC 15589 / NCIMB 2235). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; 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., 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: Riboflavin synthase is a bifunctional enzyme complex CC catalyzing the formation of riboflavin from 5-amino-6-(1'-D)- CC ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2- CC butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit CC catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino- CC 2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4- CC phosphate yielding 6,7-dimethyl-8-lumazine (By similarity). CC -!- CATALYTIC ACTIVITY: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = CC riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- CC ribitylamino)uracil: step 2/2. CC -!- SIMILARITY: Belongs to the DMRL synthase family. 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; YP_001625488.1; NC_010168.1. DR ProteinModelPortal; A9WR65; -. DR SMR; A9WR65; 13-159. DR STRING; A9WR65; -. DR GeneID; 5824327; -. DR GenomeReviews; CP000910_GR; RSal33209_2344. DR KEGG; rsa:RSal33209_2344; -. DR HOGENOM; HBG311126; -. DR OMA; SSRALMD; -. DR ProtClustDB; PRK00061; -. DR BioCyc; RSAL288705:RSAL33209_2344-MONOMER; -. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:EC. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00178; Lumazine_synth; 1; -. DR InterPro; IPR002180; DMRL_synthase. DR Gene3D; G3DSA:3.40.50.960; DMRL_synthase; 1. DR KO; K00794; -. DR PANTHER; PTHR21058; DMRL_synthase; 1. DR Pfam; PF00885; DMRL_synthase; 1. DR SUPFAM; SSF52121; DMRL_synthase; 1. DR TIGRFAMs; TIGR00114; Lumazine-synth; 1. PE 3: Inferred from homology; KW Complete proteome; Riboflavin biosynthesis; Transferase. FT CHAIN 1 159 6,7-dimethyl-8-ribityllumazine synthase. FT /FTId=PRO_1000077245. SQ SEQUENCE 159 AA; 16339 MW; B9AE0B824EAFEDD3 CRC64; MSGAGAPVSP QLNAKGLELV IIAASWHEKV MNGLLDGALR AARDAGIEEP RIVRVPGSFE LPVAAARLAP DYDAVVALGV VIRGGTPHFE YVCQAATSGL TEVSVRTGVP VGFGLLTCDN DQQALDRAGL PAAPGFAGSK EDKGYEATSA ALETALTLR //