RISA_PICGU
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 03-AUG-2022, entry version 66.
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; Saccharomycetes;
OC Saccharomycetales; 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 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_001487129.1; XM_001487079.1.
DR AlphaFoldDB; A5DB51; -.
DR SMR; A5DB51; -.
DR STRING; 4929.XP_001487129.1; -.
DR EnsemblFungi; EDK36408; EDK36408; PGUG_00506.
DR GeneID; 5129626; -.
DR KEGG; pgu:PGUG_00506; -.
DR eggNOG; KOG3310; Eukaryota.
DR HOGENOM; CLU_034388_1_1_1; -.
DR InParanoid; A5DB51; -.
DR OrthoDB; 1268603at2759; -.
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 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 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
