ID   RISC_METTH              Reviewed;         153 AA.
AC   O26237;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Riboflavin synthase;
DE            EC=2.5.1.9;
GN   Name=ribC; OrderedLocusNames=MTH_134;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-
CC         ribitylamino)uracil + riboflavin; Xref=Rhea:RHEA:20772,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:57986,
CC         ChEBI:CHEBI:58201; EC=2.5.1.9;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC       from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC       ribitylamino)uracil: step 2/2.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
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DR   EMBL; AE000666; AAB84640.1; -; Genomic_DNA.
DR   PIR; B69045; B69045.
DR   AlphaFoldDB; O26237; -.
DR   SMR; O26237; -.
DR   STRING; 187420.MTH_134; -.
DR   EnsemblBacteria; AAB84640; AAB84640; MTH_134.
DR   KEGG; mth:MTH_134; -.
DR   PATRIC; fig|187420.15.peg.107; -.
DR   HOGENOM; CLU_1682776_0_0_2; -.
DR   OMA; QLMTNTH; -.
DR   UniPathway; UPA00275; UER00405.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR   GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd09210; Riboflavin_synthase_archaeal; 1.
DR   Gene3D; 3.40.50.960; -; 1.
DR   InterPro; IPR002180; LS/RS.
DR   InterPro; IPR036467; LS/RS_sf.
DR   InterPro; IPR006399; Ribfl_synth_arc.
DR   Pfam; PF00885; DMRL_synthase; 1.
DR   PIRSF; PIRSF015750; Ribfl_synth_arc; 1.
DR   SUPFAM; SSF52121; SSF52121; 1.
DR   TIGRFAMs; TIGR01506; ribC_arch; 1.
PE   3: Inferred from homology;
KW   Magnesium; Reference proteome; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..153
FT                   /note="Riboflavin synthase"
FT                   /id="PRO_0000134861"
SQ   SEQUENCE   153 AA;  16909 MW;  79DD08CCBABBB785 CRC64;
     MIKVGICDTT FARYDMGGAA IDELKKHTAG IKIIRRTVPG IKDLPVACKK LIEEEGCEMV
     MALGMPGPEE KDKVCAHEAS TGLIQAQLMT NTHILEVFVH EDEEDDPEEL KVLADNRARE
     HAQNLIMMLF KPDRLTREAG MGLREGKPDA GPL