ID   RISC_ARCFU              Reviewed;         153 AA.
AC   O28856;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Riboflavin synthase;
DE            EC=2.5.1.9;
GN   Name=ribC; OrderedLocusNames=AF_1416;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(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   -!- 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   -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89831.1; -; Genomic_DNA.
DR   PIR; G69426; G69426.
DR   RefSeq; WP_010878913.1; NC_000917.1.
DR   AlphaFoldDB; O28856; -.
DR   SMR; O28856; -.
DR   STRING; 224325.AF_1416; -.
DR   DNASU; 1484640; -.
DR   EnsemblBacteria; AAB89831; AAB89831; AF_1416.
DR   GeneID; 24795028; -.
DR   KEGG; afu:AF_1416; -.
DR   eggNOG; arCOG01322; Archaea.
DR   HOGENOM; CLU_1682776_0_0_2; -.
DR   OMA; QLMTNTH; -.
DR   OrthoDB; 104564at2157; -.
DR   PhylomeDB; O28856; -.
DR   UniPathway; UPA00275; UER00405.
DR   Proteomes; UP000002199; 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   Reference proteome; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..153
FT                   /note="Riboflavin synthase"
FT                   /id="PRO_0000134859"
SQ   SEQUENCE   153 AA;  17083 MW;  C64E3D55752A9F37 CRC64;
     MKIGIADTTF SRINMGKIAI DELRKISSIP YERYTVPGIK DLPIAAKKLL EEKGCDIVIT
     LGWVGGTQKD MLSYIVLSMG LVIVQLMTNK HVIDVTIHED EAEDEKTLMM VAENRVREHV
     RNAVDLLVNP KRLQKLAGTG QRQGYPDVGP ILK