ID A0A7C3C2E5_9BACT Unreviewed; 157 AA. AC A0A7C3C2E5; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 03-MAY-2023, entry version 10. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00012664, 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 ORFNames=ENJ72_01110 {ECO:0000313|EMBL:HFB83365.1}; OS Thermodesulfatator sp. OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Thermodesulfatator. OX NCBI_TaxID=1874629 {ECO:0000313|EMBL:HFB83365.1}; RN [1] {ECO:0000313|EMBL:HFB83365.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HyVt-511 {ECO:0000313|EMBL:HFB83365.1}; RX PubMed=31911466; RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.; RT "Genome- and Community-Level Interaction Insights into Carbon Utilization RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal RT Sediment."; RL mSystems 5:e00795-e00719(2020). 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 + 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:0000256|ARBA:ARBA00001697, 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HFB83365.1}. 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; DRNM01000075; HFB83365.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7C3C2E5; -. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000885938; Unassembled WGS sequence. 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; 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 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. DR TIGRFAMs; TIGR00114; lumazine-synth; 1. PE 3: Inferred from homology; 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 90 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 24 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00178" FT BINDING 82..84 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 87..88 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 115 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" FT BINDING 129 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178" SQ SEQUENCE 157 AA; 16926 MW; 4D86638AB7270D6C CRC64; MSYQRFEGDF QARGLRLAII VGRFNEFISG KLLAGALDAL KRHGAREEDI DVFWVPGSFE IPLVAKRLAT SGRYQALVCL GAIIRGATPH FEYVAAEASK GIAQVMLETG VPIAFGVLTT DTIEQAIERA GTKAGNKGFE AAMVAIEMAN LLQKIPS //