ID A0A517QJT0_9PLAN Unreviewed; 156 AA.
AC A0A517QJT0;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
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 ECO:0000313|EMBL:QDT31902.1};
GN ORFNames=Mal48_11390 {ECO:0000313|EMBL:QDT31902.1};
OS Thalassoglobus polymorphus.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
OC Planctomycetales; Planctomycetaceae; Thalassoglobus.
OX NCBI_TaxID=2527994 {ECO:0000313|EMBL:QDT31902.1, ECO:0000313|Proteomes:UP000315724};
RN [1] {ECO:0000313|EMBL:QDT31902.1, ECO:0000313|Proteomes:UP000315724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mal48 {ECO:0000313|EMBL:QDT31902.1,
RC ECO:0000313|Proteomes:UP000315724};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) 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|ARBA:ARBA00058151, ECO:0000256|HAMAP-
CC 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; CP036267; QDT31902.1; -; Genomic_DNA.
DR RefSeq; WP_145196826.1; NZ_CP036267.1.
DR AlphaFoldDB; A0A517QJT0; -.
DR KEGG; tpol:Mal48_11390; -.
DR OrthoDB; 9809709at2; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000315724; Chromosome.
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 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:UP000315724};
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 156 AA; 16520 MW; BD36773AD9BFF1E0 CRC64;
MTQKISGNMI ADSNDQYAIV VSRFNELVTK RLLDGAVDTL KRHGASADSI VECWVPGAYE
LPIIAERLAA SGKYAAVITL GAVIQGDTDH HDYINHAVAQ GIMDASQKNG IPVLFGVLTC
RTMEQALDRA GGKAGNKGVE AALAAIETVN VLKQLS
//
