RISB_THENN
ID RISB_THENN Reviewed; 166 AA.
AC B9K7K0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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}; OrderedLocusNames=CTN_0757;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) 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:0000255|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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00178}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00178}.
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DR EMBL; CP000916; ACM22933.1; -; Genomic_DNA.
DR RefSeq; WP_015919250.1; NC_011978.1.
DR AlphaFoldDB; B9K7K0; -.
DR SMR; B9K7K0; -.
DR STRING; 309803.CTN_0757; -.
DR EnsemblBacteria; ACM22933; ACM22933; CTN_0757.
DR KEGG; tna:CTN_0757; -.
DR eggNOG; COG0054; Bacteria.
DR HOGENOM; CLU_089358_1_1_0; -.
DR OMA; CQGVTQG; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000000445; Chromosome.
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; -; 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; PTHR21058; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR SUPFAM; SSF52121; SSF52121; 1.
DR TIGRFAMs; TIGR00114; lumazine-synth; 1.
PE 3: Inferred from homology;
KW Riboflavin biosynthesis; Transferase.
FT CHAIN 1..166
FT /note="6,7-dimethyl-8-ribityllumazine synthase"
FT /id="PRO_1000195516"
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 22
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 56..58
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 80..82
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 85..86
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 113
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 127
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
SQ SEQUENCE 166 AA; 18142 MW; 7F9A9C97F338248E CRC64;
MKVVQGDYRG EGLKIAVVVP RFNDLVTSKL LEGALDGLKR HGVSDENITV VRIPGSMEAI
YTLKRLLDLG VHDAIIVLGA VIRGETYHFN VVANEIGKAV AQFNMNSDVP IVFGVLTTDT
LEQALNRAGA KSGNKGFEAA MVAIEMANLR KKLRRDFLEP HSNSRQ
