ID   RISA_AQUAE              Reviewed;         207 AA.
AC   O67604;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Riboflavin synthase;
DE            Short=RS;
DE            EC=2.5.1.9;
GN   Name=ribE; Synonyms=ribC; OrderedLocusNames=aq_1707;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-
CC       ribityllumazine, resulting in the formation of riboflavin and 5-amino-
CC       6-(D-ribitylamino)uracil. {ECO:0000250}.
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   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
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DR   EMBL; AE000657; AAC07572.1; -; Genomic_DNA.
DR   PIR; B70447; B70447.
DR   RefSeq; NP_214170.1; NC_000918.1.
DR   RefSeq; WP_010881107.1; NC_000918.1.
DR   AlphaFoldDB; O67604; -.
DR   SMR; O67604; -.
DR   STRING; 224324.aq_1707; -.
DR   EnsemblBacteria; AAC07572; AAC07572; aq_1707.
DR   KEGG; aae:aq_1707; -.
DR   PATRIC; fig|224324.8.peg.1311; -.
DR   eggNOG; COG0307; Bacteria.
DR   HOGENOM; CLU_034388_2_0_0; -.
DR   InParanoid; O67604; -.
DR   OMA; HFVTGHV; -.
DR   OrthoDB; 1276859at2; -.
DR   UniPathway; UPA00275; UER00405.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0004746; F:riboflavin synthase activity; IBA:GO_Central.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
DR   CDD; cd00402; Riboflavin_synthase_like; 1.
DR   Gene3D; 2.40.30.20; -; 2.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR001783; Lumazine-bd.
DR   InterPro; IPR026017; Lumazine-bd_dom.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR21098; PTHR21098; 1.
DR   Pfam; PF00677; Lum_binding; 2.
DR   PIRSF; PIRSF000498; Riboflavin_syn_A; 1.
DR   SUPFAM; SSF63380; SSF63380; 2.
DR   TIGRFAMs; TIGR00187; ribE; 1.
DR   PROSITE; PS51177; LUMAZINE_BIND; 2.
PE   3: Inferred from homology;
KW   Reference proteome; Repeat; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..207
FT                   /note="Riboflavin synthase"
FT                   /id="PRO_0000068157"
FT   REPEAT          1..94
FT                   /note="Lumazine-binding 1"
FT   REPEAT          95..191
FT                   /note="Lumazine-binding 2"
FT   BINDING         4..6
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         45..47
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between two trimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         59..64
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between two trimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFU8"
FT   BINDING         98..100
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between two trimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         133
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between two trimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         142..144
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         156..161
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
SQ   SEQUENCE   207 AA;  23196 MW;  322A09FF7B15E432 CRC64;
     MFTGLVEDLG KVKNLTLSSK GAKLSVETKL EDVKLGDSVS VNGACLTVVD IKSSTLTFDV
     SPETLKRTNL GKLKTGDYVN LERALRVGER LGGHIVQGHV DFTAPVKSFN FLGEHYELVI
     EIPEEWSIYV VEKGSIALDG ISLTVNYVKE NKVFINIIPH TYKSTNLQFK KVGDLLNVET
     DILGKYVINY LNKLKKKEDI FKEFLKW