RISA_SCHPO
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 03-AUG-2022, entry version 136.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 4896.SPCC1450.13c.1; -.
DR MaxQB; Q9Y7P0; -.
DR PaxDb; Q9Y7P0; -.
DR PRIDE; Q9Y7P0; -.
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; HILSGHV; -.
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; IDA:PomBase.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IDA:PomBase.
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 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
