ID F9Y8Y3_KETVW Unreviewed; 144 AA.
AC F9Y8Y3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 28-JAN-2026, entry version 76.
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 ECO:0000313|EMBL:AEM40039.1};
GN OrderedLocusNames=KVU_0200 {ECO:0000313|EMBL:AEM40039.1};
OS Ketogulonicigenium vulgare (strain WSH-001).
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Ketogulonicigenium.
OX NCBI_TaxID=759362 {ECO:0000313|EMBL:AEM40039.1, ECO:0000313|Proteomes:UP000000692};
RN [1] {ECO:0000313|EMBL:AEM40039.1, ECO:0000313|Proteomes:UP000000692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSH-001 {ECO:0000313|EMBL:AEM40039.1,
RC ECO:0000313|Proteomes:UP000000692};
RX PubMed=21994934; DOI=10.1128/JB.06007-11;
RA Liu L., Li Y., Zhang J., Zhou Z., Liu J., Li X., Zhou J., Du G., Wang L.,
RA Chen J.;
RT "Complete genome sequence of the industrial strain Ketogulonicigenium
RT vulgare WSH-001.";
RL J. Bacteriol. 193:6108-6109(2011).
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}.
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DR EMBL; CP002018; AEM40039.1; -; Genomic_DNA.
DR RefSeq; WP_013383461.1; NC_017384.1.
DR AlphaFoldDB; F9Y8Y3; -.
DR KEGG; kvl:KVU_0200; -.
DR PATRIC; fig|759362.5.peg.213; -.
DR eggNOG; COG0054; Bacteria.
DR HOGENOM; CLU_089358_1_1_5; -.
DR OrthoDB; 9797659at2; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000000692; 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 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000692};
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 79
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 15
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 47..49
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 71..73
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 76..77
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 104
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 118
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
SQ SEQUENCE 144 AA; 14813 MW; 20CFED8E3368A1E0 CRC64;
MTATNLRLAI VTSTFSPEIT GGLRKGAEDY LAEAGAPNAA HFSAPGAFEI PLIAQKLAQS
GRYDGVICLG CVIKGDTAHF EYISGAASLG LMNASLATGI PLTFGIITTY SEEQAIARSR
DDAHNKGREA AAACIAALAT LAQV
//
