ID   RISB_RENSM              Reviewed;         159 AA.
AC   A9WR65;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   08-MAY-2019, entry version 70.
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};
GN   OrderedLocusNames=RSal33209_2344;
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484
OS   / NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S.,
RA   Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J.,
RA   Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum
RT   suggests reductive evolution away from an environmental Arthrobacter
RT   ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
CC   -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-
CC       ribityllumazine by condensation of 5-amino-6-(D-
CC       ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate.
CC       This is the penultimate step in the biosynthesis of riboflavin.
CC       {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 +
CC         H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830;
CC         EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis;
CC       riboflavin 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00178}.
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DR   EMBL; CP000910; ABY24074.1; -; Genomic_DNA.
DR   RefSeq; WP_012245737.1; NC_010168.1.
DR   SMR; A9WR65; -.
DR   STRING; 288705.RSal33209_2344; -.
DR   EnsemblBacteria; ABY24074; ABY24074; RSal33209_2344.
DR   KEGG; rsa:RSal33209_2344; -.
DR   eggNOG; ENOG4108UTT; Bacteria.
DR   eggNOG; COG0054; LUCA.
DR   HOGENOM; HOG000229253; -.
DR   KO; K00794; -.
DR   OMA; HGNKGTE; -.
DR   OrthoDB; 1680292at2; -.
DR   BioCyc; RSAL288705:G1GAP-2085-MONOMER; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000002007; 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   Complete proteome; Reference proteome; Riboflavin biosynthesis;
KW   Transferase.
FT   CHAIN         1    159       6,7-dimethyl-8-ribityllumazine synthase.
FT                                /FTId=PRO_1000077245.
FT   REGION       58     60       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   REGION       80     82       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   REGION       85     86       1-deoxy-L-glycero-tetrulose 4-phosphate
FT                                binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00178}.
FT   ACT_SITE     88     88       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00178}.
FT   BINDING      26     26       5-amino-6-(D-ribitylamino)uracil.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   BINDING     113    113       5-amino-6-(D-ribitylamino)uracil; via
FT                                amide nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   BINDING     127    127       1-deoxy-L-glycero-tetrulose 4-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
SQ   SEQUENCE   159 AA;  16339 MW;  B9AE0B824EAFEDD3 CRC64;
     MSGAGAPVSP QLNAKGLELV IIAASWHEKV MNGLLDGALR AARDAGIEEP RIVRVPGSFE
     LPVAAARLAP DYDAVVALGV VIRGGTPHFE YVCQAATSGL TEVSVRTGVP VGFGLLTCDN
     DQQALDRAGL PAAPGFAGSK EDKGYEATSA ALETALTLR
//