ID Q1AW98_RUBXD Unreviewed; 179 AA. AC Q1AW98; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 18-JUN-2025, entry version 118. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00072606, ECO:0000256|HAMAP-Rule:MF_00178}; DE Short=DMRL synthase {ECO:0000256|HAMAP-Rule:MF_00178}; DE Short=LS {ECO:0000256|HAMAP-Rule:MF_00178}; DE Short=Lumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178}; DE EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664, ECO:0000256|HAMAP-Rule:MF_00178}; GN Name=ribH {ECO:0000256|HAMAP-Rule:MF_00178}; GN OrderedLocusNames=Rxyl_1367 {ECO:0000313|EMBL:ABG04330.1}; OS Rubrobacter xylanophilus (strain DSM 9941 / JCM 11954 / NBRC 16129 / OS PRD-1). OC Bacteria; Bacillati; Actinomycetota; Rubrobacteria; Rubrobacterales; OC Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04330.1, ECO:0000313|Proteomes:UP000006637}; RN [1] {ECO:0000313|EMBL:ABG04330.1, ECO:0000313|Proteomes:UP000006637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1 RC {ECO:0000313|Proteomes:UP000006637}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.; RT "Complete sequence of Rubrobacter xylanophilus DSM 9941."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. 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:0000256|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 + CC phosphate + 2 H2O + H(+); 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:0000256|ARBA:ARBA00048785, ECO:0000256|HAMAP- CC 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:0000256|ARBA:ARBA00004917, CC ECO:0000256|HAMAP-Rule:MF_00178}. CC -!- SIMILARITY: Belongs to the DMRL synthase family. CC {ECO:0000256|ARBA:ARBA00007424, ECO:0000256|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; CP000386; ABG04330.1; -; Genomic_DNA. DR RefSeq; WP_011564347.1; NC_008148.1. DR AlphaFoldDB; Q1AW98; -. DR STRING; 266117.Rxyl_1367; -. DR KEGG; rxy:Rxyl_1367; -. DR eggNOG; COG0054; Bacteria. DR HOGENOM; CLU_089358_1_1_11; -. DR OrthoDB; 9809709at2; -. DR PhylomeDB; Q1AW98; -. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000006637; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:UniProtKB-UniRule. 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 FunFam; 3.40.50.960:FF:000001; 6,7-dimethyl-8-ribityllumazine synthase; 1. DR Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 1. DR HAMAP; MF_00178; Lumazine_synth; 1. DR InterPro; IPR034964; LS. DR InterPro; IPR002180; LS/RS. DR InterPro; IPR036467; LS/RS_sf. DR NCBIfam; TIGR00114; lumazine-synth; 1. DR NCBIfam; NF000812; PRK00061.1-4; 1. DR PANTHER; PTHR21058:SF0; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE; 1. 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. PE 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000006637}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_00178}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00178}. FT ACT_SITE 94 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 28 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 62..64 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 86..88 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 91..92 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 119 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 133 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" SQ SEQUENCE 179 AA; 18663 MW; C84464053C5B7672 CRC64; MERSGRVRHI EGHLSAGGRS FGIVASRFND FVVRRLLEGA LEAIERHGGS LEAVDVAWVP GSYEIPLAAK RMALSGRYDA VICLGAVIRG ATAHFDYVAG GAASGISSAA LESGVPVIFG VITTETIEQA IERAGTKLGN KGFEAAVSAI EMADLMPRLA GEETLRPPRP APAGRPSGP //