RISA_YEAST
ID RISA_YEAST Reviewed; 238 AA.
AC P38145; D6VQQ3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Riboflavin synthase {ECO:0000303|PubMed:7814407};
DE Short=RS {ECO:0000303|PubMed:7814407};
DE EC=2.5.1.9 {ECO:0000269|PubMed:7814407};
GN Name=RIB5 {ECO:0000303|PubMed:7814407}; OrderedLocusNames=YBR256C;
GN ORFNames=YBR1724;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7814407; DOI=10.1074/jbc.270.1.437;
RA Santos M.A., Garcia-Ramirez J.J., Revuelta J.L.;
RT "Riboflavin biosynthesis in Saccharomyces cerevisiae. Cloning,
RT characterization, and expression of the RIB5 gene encoding riboflavin
RT synthase.";
RL J. Biol. Chem. 270:437-444(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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:0000269|PubMed:7814407}.
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; Evidence={ECO:0000269|PubMed:7814407};
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. {ECO:0000269|PubMed:7814407}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q9Y7P0}.
CC -!- MISCELLANEOUS: Present with 7300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z21621; CAA79745.1; -; Genomic_DNA.
DR EMBL; X70529; CAA49920.1; -; Genomic_DNA.
DR EMBL; Z36125; CAA85219.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07373.1; -; Genomic_DNA.
DR PIR; S34072; S34072.
DR RefSeq; NP_009815.1; NM_001178604.1.
DR AlphaFoldDB; P38145; -.
DR SMR; P38145; -.
DR BioGRID; 32952; 140.
DR MINT; P38145; -.
DR STRING; 4932.YBR256C; -.
DR iPTMnet; P38145; -.
DR MaxQB; P38145; -.
DR PaxDb; P38145; -.
DR PRIDE; P38145; -.
DR EnsemblFungi; YBR256C_mRNA; YBR256C; YBR256C.
DR GeneID; 852559; -.
DR KEGG; sce:YBR256C; -.
DR SGD; S000000460; RIB5.
DR VEuPathDB; FungiDB:YBR256C; -.
DR eggNOG; KOG3310; Eukaryota.
DR HOGENOM; CLU_034388_1_1_1; -.
DR InParanoid; P38145; -.
DR OMA; HILSGHV; -.
DR BioCyc; MetaCyc:MON3O-75; -.
DR BioCyc; YEAST:MON3O-75; -.
DR UniPathway; UPA00275; UER00405.
DR PRO; PR:P38145; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38145; protein.
DR GO; GO:0004746; F:riboflavin synthase activity; IDA:SGD.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; Riboflavin biosynthesis;
KW Transferase.
FT CHAIN 1..238
FT /note="Riboflavin synthase"
FT /id="PRO_0000068174"
FT REPEAT 1..103
FT /note="Lumazine-binding 1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT REPEAT 104..205
FT /note="Lumazine-binding 2"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
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 68..73
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 107..109
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 143
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 152..154
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"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 238 AA; 26196 MW; EA57EAD542D46897 CRC64;
MFTGIVECMG TVLENNPYDD SESGGQGVSI TIGNAGSILT DCHVGDSIAV NGVCLTVTEF
NNDSFKVGIS PETIKRSNVA SWIQGTQVNL ERAVSQDVRF GGHYVQGHVD TVANIVSRRP
EGNSIIFGFQ LRDQEYFKYI VEKGFICIDG TSLTIIKVDP LSQGGAFYIS MIKHTQDNVI
MPLKKIGDEV NIEVDLTGKI IEKQILLTLE NQISKKDSTL NTMISNIIEE KVRNYLNK
