ID   RISA_PICGU              Reviewed;         239 AA.
AC   A5DB51; Q8X181;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   02-SEP-2026, entry version 76.
DE   RecName: Full=Riboflavin synthase;
DE            Short=RS;
DE            EC=2.5.1.9;
GN   Name=RIB5; Synonyms=RIB7; ORFNames=PGUG_00506;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=15925311; DOI=10.1016/j.femsyr.2005.03.007;
RA   Boretsky Y.R., Kapustyak K.Y., Fayura L.R., Stasyk O.V., Stenchuk M.M.,
RA   Bobak Y.P., Drobot L.B., Sibirny A.A.;
RT   "Positive selection of mutants defective in transcriptional repression of
RT   riboflavin synthesis by iron in the flavinogenic yeast Pichia
RT   guilliermondii.";
RL   FEMS Yeast Res. 5:829-837(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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|UniProtKB:Q9Y7P0}.
CC   -!- INDUCTION: Repressed by iron. {ECO:0000269|PubMed:15925311}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDK36408.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF459790; AAL66353.2; -; Genomic_DNA.
DR   EMBL; AY138984; AAN08875.2; -; Genomic_DNA.
DR   EMBL; CH408155; EDK36408.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001487129.2; XM_001487079.1.
DR   AlphaFoldDB; A5DB51; -.
DR   SMR; A5DB51; -.
DR   FunCoup; A5DB51; 173.
DR   STRING; 294746.A5DB51; -.
DR   GeneID; 5129626; -.
DR   KEGG; pgu:PGUG_00506; -.
DR   eggNOG; KOG3310; Eukaryota.
DR   HOGENOM; CLU_034388_1_1_1; -.
DR   InParanoid; A5DB51; -.
DR   OrthoDB; 10258924at2759; -.
DR   UniPathway; UPA00275; UER00405.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00402; Riboflavin_synthase_like; 1.
DR   FunFam; 2.40.30.20:FF:000004; Riboflavin synthase, alpha subunit; 1.
DR   FunFam; 2.40.30.20:FF:000006; Riboflavin synthase, alpha subunit; 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   NCBIfam; NF006767; PRK09289.1; 1.
DR   NCBIfam; TIGR00187; ribE; 1.
DR   PANTHER; PTHR21098:SF0; RIBOFLAVIN SYNTHASE; 1.
DR   PANTHER; PTHR21098; RIBOFLAVIN SYNTHASE ALPHA CHAIN; 1.
DR   Pfam; PF00677; Lum_binding; 2.
DR   PIRSF; PIRSF000498; Riboflavin_syn_A; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 2.
DR   PROSITE; PS51177; LUMAZINE_BIND; 2.
PE   2: Evidence at transcript level;
KW   Reference proteome; Repeat; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..239
FT                   /note="Riboflavin synthase"
FT                   /id="PRO_0000295039"
FT   REPEAT          1..105
FT                   /note="Lumazine-binding 1"
FT   REPEAT          106..205
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         54..56
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         70..75
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         109..111
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         145
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         154..156
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         170..175
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
SQ   SEQUENCE   239 AA;  26044 MW;  64DA06FEFB2D59B2 CRC64;
     MFTGLVEHIG TVLQVTEKDT TASGGDGVSM VIGDCSKILE DVQLGDSICT NGVCLTVTEF
     DMARSQFKVG ISPETLRRSD LGELKPGSKV NLERAVKADV RMGGHVVQGH VDTIATIVNR
     RGDGNAINFT FKLRDSQYGK YIVEKGFIAI DGTSLTVTDV DHEQSEFSIS MVSYTQEKVI
     MPLKNSGDSV NIEVDLTGKL IEKQIELSLL SYIKDETSPL STLIGKLVEK KVDDVLKRN
//