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Entry: RISB_SULAC
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ID   RISB_SULAC              Reviewed;         158 AA.
AC   Q4JAJ2;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=Saci_0820;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80187.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4JAJ2; -.
DR   SMR; Q4JAJ2; -.
DR   STRING; 330779.Saci_0820; -.
DR   KEGG; sai:Saci_0820; -.
DR   PATRIC; fig|330779.12.peg.784; -.
DR   eggNOG; arCOG01323; Archaea.
DR   HOGENOM; CLU_089358_3_1_2; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000001018; 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; cd09211; Lumazine_synthase_archaeal; 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; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..158
FT                   /note="6,7-dimethyl-8-ribityllumazine synthase"
FT                   /id="PRO_0000134852"
FT   ACT_SITE        82
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         18
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         50..52
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         74..76
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         79..80
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         107
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         122
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
SQ   SEQUENCE   158 AA;  17608 MW;  6860547B6498BDA7 CRC64;
     MEMQDQSKIN LGIVVSEFNY DITSLMLQRA LSHAEFLGVT VKVVVKVPGS YDMAVIVKEL
     LKRDEIDGVV TLGAVIKGET KHDEIVATQT ARKLMDLSVE YGKPVTLGII GHGVTHEQAV
     ERIEEYSMRA VESAVKLIKR LKKLREIDLT KETNVSIE
//
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