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   02-DEC-2020, entry version 76.
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; 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., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
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; 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; COG0054; Bacteria.
DR   HOGENOM; CLU_089358_1_1_11; -.
DR   OMA; CQGVTQG; -.
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   Reference proteome; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..159
FT                   /note="6,7-dimethyl-8-ribityllumazine synthase"
FT                   /id="PRO_1000077245"
FT   REGION          58..60
FT                   /note="5-amino-6-(D-ribitylamino)uracil binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   REGION          80..82
FT                   /note="5-amino-6-(D-ribitylamino)uracil binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   REGION          85..86
FT                   /note="1-deoxy-L-glycero-tetrulose 4-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   ACT_SITE        88
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         26
FT                   /note="5-amino-6-(D-ribitylamino)uracil"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         113
FT                   /note="5-amino-6-(D-ribitylamino)uracil; via amide nitrogen
FT                   and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         127
FT                   /note="1-deoxy-L-glycero-tetrulose 4-phosphate"
FT                   /evidence="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
//