ID RISB_AQUAE Reviewed; 154 AA. AC O66529; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase; DE Short=DMRL synthase; DE Short=LS; DE Short=Lumazine synthase; DE EC=2.5.1.78; GN Name=ribH; OrderedLocusNames=aq_132; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS. RC STRAIN=VF5; RX PubMed=12603336; DOI=10.1046/j.1432-1033.2003.03478.x; RA Haase I., Mortl S., Kohler P., Bacher A., Fischer M.; RT "Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine RT synthase of Methanococcus jannaschii."; RL Eur. J. Biochem. 270:1025-1032(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC RP ACTIVITY, TEMPERATURE DEPENDENCE, AND SUBUNIT. RC STRAIN=VF5; RX PubMed=11237620; DOI=10.1006/jmbi.2000.4435; RA Zhang X., Meining W., Fischer M., Bacher A., Ladenstein R.; RT "X-ray structure analysis and crystallographic refinement of lumazine RT synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: RT determinants of thermostability revealed from structural comparisons."; RL J. Mol. Biol. 306:1099-1114(2001). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOG RP OR REACTION INTERMEDIATE ANALOG INHIBITORS AND PHOSPHATE, PATHWAY, ACTIVE RP SITE, AND REACTION MECHANISM. RC STRAIN=VF5; RX PubMed=12684006; DOI=10.1016/s0022-2836(03)00186-4; RA Zhang X., Meining W., Cushman M., Haase I., Fischer M., Bacher A., RA Ladenstein R.; RT "A structure-based model of the reaction catalyzed by lumazine synthase RT from Aquifex aeolicus."; RL J. Mol. Biol. 328:167-182(2003). 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:0000269|PubMed:11237620, CC ECO:0000269|PubMed:12603336}. 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:0000269|PubMed:11237620, ECO:0000269|PubMed:12603336}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=10 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius CC and pH 7.0) {ECO:0000269|PubMed:12603336}; CC KM=26 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees CC Celsius and pH 7.0) {ECO:0000269|PubMed:12603336}; CC Vmax=31 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0) CC {ECO:0000269|PubMed:12603336}; CC Vmax=425 nmol/min/mg enzyme (at 70 degrees Celsius and pH 7.0) CC {ECO:0000269|PubMed:12603336}; CC Temperature dependence: CC Extremely thermostable. Has a melting temperature of 119.9 degrees CC Celsius. {ECO:0000269|PubMed:11237620}; 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:0000269|PubMed:12684006}. CC -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, arranged CC as a dodecamer of pentamers. {ECO:0000269|PubMed:11237620}. CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}. 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; AE000657; AAC06489.1; -; Genomic_DNA. DR PIR; F70312; F70312. DR RefSeq; NP_213089.1; NC_000918.1. DR RefSeq; WP_010880027.1; NC_000918.1. DR PDB; 1HQK; X-ray; 1.60 A; A/B/C/D/E=1-154. DR PDB; 1NQU; X-ray; 1.75 A; A/B/C/D/E=1-154. DR PDB; 1NQV; X-ray; 2.05 A; A/B/C/D/E=1-154. DR PDB; 1NQW; X-ray; 2.20 A; A/B/C/D/E=1-154. DR PDB; 1NQX; X-ray; 1.82 A; A/B/C/D/E=1-154. DR PDB; 5MPP; EM; 3.94 A; 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-154. DR PDB; 5MQ3; EM; 5.40 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO=1-154. DR PDB; 5MQ7; EM; 5.20 A; 0A/0B/0C/0D/0E/0X/1A/1B/1C/1D/1E/1X/2A/2B/2C/2D/2E/2X/3A/3B/3C/3D/3E/3X/4A/4B/4C/4D/4E/4X=1-154. DR PDB; 7A4F; EM; 3.50 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/CA/CB/CC/CD/CE/CF/CG/CH/CI/CJ=1-84. DR PDB; 7A4G; EM; 4.20 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO=1-84. DR PDB; 7A4H; EM; 4.50 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO=1-84. DR PDB; 7A4I; EM; 7.04 A; 0A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B=1-84. DR PDB; 7A4J; EM; 3.04 A; 0A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B=1-84. DR PDB; 7X7M; EM; 2.33 A; 0/1/2/3/4/5/6/7/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-154. DR PDB; 8F25; EM; 2.60 A; 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-154. DR PDB; 8PVJ; EM; 3.00 A; A=1-154. DR PDBsum; 1HQK; -. DR PDBsum; 1NQU; -. DR PDBsum; 1NQV; -. DR PDBsum; 1NQW; -. DR PDBsum; 1NQX; -. DR PDBsum; 5MPP; -. DR PDBsum; 5MQ3; -. DR PDBsum; 5MQ7; -. DR PDBsum; 7A4F; -. DR PDBsum; 7A4G; -. DR PDBsum; 7A4H; -. DR PDBsum; 7A4I; -. DR PDBsum; 7A4J; -. DR PDBsum; 7X7M; -. DR PDBsum; 8F25; -. DR PDBsum; 8PVJ; -. DR AlphaFoldDB; O66529; -. DR EMDB; EMD-17968; -. DR EMDB; EMD-33041; -. DR EMDB; EMD-3538; -. DR EMDB; EMD-3543; -. DR EMDB; EMD-3544; -. DR SMR; O66529; -. DR STRING; 224324.aq_132; -. DR DrugBank; DB04262; 3-(7-hydroxy-8-ribityllumazine-6-yl) propionic acid. DR DrugBank; DB04128; 5-Nitroso-6-ribityl-amino-2,4(1H,3H)-pyrimidinedione. DR DrugBank; DB02214; 6,7-dioxo-5H-8-ribitylaminolumazine. DR EnsemblBacteria; AAC06489; AAC06489; aq_132. DR KEGG; aae:aq_132; -. DR PATRIC; fig|224324.8.peg.111; -. DR eggNOG; COG0054; Bacteria. DR HOGENOM; CLU_089358_1_1_0; -. DR InParanoid; O66529; -. DR OrthoDB; 9809709at2; -. DR BRENDA; 2.5.1.78; 396. DR SABIO-RK; O66529; -. DR UniPathway; UPA00275; UER00404. DR EvolutionaryTrace; O66529; -. DR Proteomes; UP000000798; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IBA:GO_Central. DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central. 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 NCBIfam; TIGR00114; lumazine-synth; 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 1: Evidence at protein level; KW 3D-structure; Reference proteome; Riboflavin biosynthesis; Transferase. FT CHAIN 1..154 FT /note="6,7-dimethyl-8-ribityllumazine synthase" FT /id="PRO_0000134708" FT ACT_SITE 88 FT /note="Proton donor" FT /evidence="ECO:0000255" FT BINDING 22..23 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT BINDING 56..58 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT BINDING 80..82 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT BINDING 85..86 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000305" FT BINDING 113 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT BINDING 127 FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" FT /ligand_id="ChEBI:CHEBI:58830" FT /evidence="ECO:0000305" FT BINDING 135 FT /ligand="5-amino-6-(D-ribitylamino)uracil" FT /ligand_id="ChEBI:CHEBI:15934" FT STRAND 2..4 FT /evidence="ECO:0007829|PDB:1HQK" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:1HQK" FT HELIX 24..40 FT /evidence="ECO:0007829|PDB:1HQK" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:1HQK" FT STRAND 48..55 FT /evidence="ECO:0007829|PDB:1HQK" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:1HQK" FT HELIX 59..67 FT /evidence="ECO:0007829|PDB:1HQK" FT STRAND 74..82 FT /evidence="ECO:0007829|PDB:1HQK" FT HELIX 88..107 FT /evidence="ECO:0007829|PDB:1HQK" FT STRAND 111..120 FT /evidence="ECO:0007829|PDB:1HQK" FT HELIX 121..127 FT /evidence="ECO:0007829|PDB:1HQK" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:1HQK" FT HELIX 135..153 FT /evidence="ECO:0007829|PDB:1HQK" SQ SEQUENCE 154 AA; 16705 MW; A189410A16454AB7 CRC64; MQIYEGKLTA EGLRFGIVAS RFNHALVDRL VEGAIDCIVR HGGREEDITL VRVPGSWEIP VAAGELARKE DIDAVIAIGV LIRGATPHFD YIASEVSKGL ANLSLELRKP ITFGVITADT LEQAIERAGT KHGNKGWEAA LSAIEMANLF KSLR //