ID   RISA_SCHPO              Reviewed;         208 AA.
AC   Q9Y7P0;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Riboflavin synthase;
DE            Short=RS;
DE            EC=2.5.1.9 {ECO:0000269|PubMed:14690539};
GN   Name=rib5; ORFNames=SPCC1450.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX   PubMed=14690539; DOI=10.1186/1471-2091-4-18;
RA   Fischer M., Schott A.-K., Kemter K., Feicht R., Richter G., Illarionov B.,
RA   Eisenreich W., Gerhardt S., Cushman M., Steinbacher S., Huber R.,
RA   Bacher A.;
RT   "Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics
RT   revealed by 19F NMR protein perturbation experiments.";
RL   BMC Biochem. 4:18-18(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE ANALOG
RP   6-CARBOXYETHYL-7-OXO-8-RIBITYLLUMAZINE.
RX   PubMed=12377123; DOI=10.1016/s0969-2126(02)00864-x;
RA   Gerhardt S., Schott A.-K., Kairies N., Cushman M., Illarionov B.,
RA   Eisenreich W., Bacher A., Huber R., Steinbacher S., Fischer M.;
RT   "Studies on the reaction mechanism of riboflavin synthase: X-ray crystal
RT   structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine.";
RL   Structure 10:1371-1381(2002).
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:14690539}.
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         Evidence={ECO:0000269|PubMed:14690539};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20773;
CC         Evidence={ECO:0000305|PubMed:14690539};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.7 uM for 6,7-dimethyl-8-(1-D-ribityl)lumazine (at pH 7.2 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:14690539};
CC         Vmax=158 nmol/min/mg enzyme for the formation of riboflavin (at pH
CC         7.2 and 37 degrees Celsius) {ECO:0000269|PubMed:14690539};
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:0000305|PubMed:14690539}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:14690539}.
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DR   EMBL; AF505789; AAM28201.1; -; mRNA.
DR   EMBL; CU329672; CAB40180.1; -; Genomic_DNA.
DR   PIR; T40995; T40995.
DR   RefSeq; NP_588312.1; NM_001023302.2.
DR   PDB; 1KZL; X-ray; 2.10 A; A=1-208.
DR   PDBsum; 1KZL; -.
DR   AlphaFoldDB; Q9Y7P0; -.
DR   SMR; Q9Y7P0; -.
DR   BioGRID; 275754; 1.
DR   STRING; 284812.Q9Y7P0; -.
DR   MaxQB; Q9Y7P0; -.
DR   PaxDb; 4896-SPCC1450-13c-1; -.
DR   EnsemblFungi; SPCC1450.13c.1; SPCC1450.13c.1:pep; SPCC1450.13c.
DR   GeneID; 2539183; -.
DR   KEGG; spo:SPCC1450.13c; -.
DR   PomBase; SPCC1450.13c; rib5.
DR   VEuPathDB; FungiDB:SPCC1450.13c; -.
DR   eggNOG; KOG3310; Eukaryota.
DR   HOGENOM; CLU_034388_1_1_1; -.
DR   InParanoid; Q9Y7P0; -.
DR   OMA; IGGHAMS; -.
DR   PhylomeDB; Q9Y7P0; -.
DR   BRENDA; 2.5.1.9; 5613.
DR   UniPathway; UPA00275; UER00405.
DR   EvolutionaryTrace; Q9Y7P0; -.
DR   PRO; PR:Q9Y7P0; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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   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   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Repeat; Riboflavin biosynthesis;
KW   Transferase.
FT   CHAIN           1..208
FT                   /note="Riboflavin synthase"
FT                   /id="PRO_0000068173"
FT   REPEAT          1..97
FT                   /note="Lumazine-binding 1"
FT   REPEAT          98..195
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:0000305|PubMed:12377123"
FT   BINDING         48..50
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:0000305|PubMed:12377123"
FT   BINDING         62..67
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:0000305|PubMed:12377123"
FT   BINDING         101..103
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:0000305|PubMed:12377123"
FT   BINDING         137
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         146..148
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:12377123"
FT   BINDING         160..165
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:12377123"
FT   STRAND          8..18
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          22..28
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   HELIX           65..70
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          105..115
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          118..127
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   HELIX           128..133
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          145..152
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   HELIX           187..198
FT                   /evidence="ECO:0007829|PDB:1KZL"
FT   TURN            199..201
FT                   /evidence="ECO:0007829|PDB:1KZL"
SQ   SEQUENCE   208 AA;  22861 MW;  59C5065DDD4C7B8B CRC64;
     MFTGLVEAIG VVKDVQGTID NGFAMKIEAP QILDDCHTGD SIAVNGTCLT VTDFDRYHFT
     VGIAPESLRL TNLGQCKAGD PVNLERAVLS STRMGGHFVQ GHVDTVAEIV EKKQDGEAID
     FTFRPRDPFV LKYIVYKGYI ALDGTSLTIT HVDDSTFSIM MISYTQSKVI MAKKNVGDLV
     NVEVDQIGKY TEKLVEAHIA DWIKKTQA
//