ID RISA_SHIFL Reviewed; 213 AA. AC P0AFU9; P29015; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Riboflavin synthase; DE Short=RS; DE EC=2.5.1.9; GN Name=ribE; Synonyms=ribC; OrderedLocusNames=SF1690, S1822; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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}. 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; AE005674; AAN43269.1; -; Genomic_DNA. DR EMBL; AE014073; AAP17158.1; -; Genomic_DNA. DR RefSeq; NP_707562.1; NC_004337.2. DR RefSeq; WP_000493947.1; NZ_WPGW01000025.1. DR AlphaFoldDB; P0AFU9; -. DR BMRB; P0AFU9; -. DR SMR; P0AFU9; -. DR STRING; 198214.SF1690; -. DR PaxDb; 198214-SF1690; -. DR GeneID; 1024885; -. DR GeneID; 75204508; -. DR KEGG; sfl:SF1690; -. DR KEGG; sfx:S1822; -. DR PATRIC; fig|198214.7.peg.1999; -. DR HOGENOM; CLU_034388_0_1_6; -. DR UniPathway; UPA00275; UER00405. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; Chromosome. 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 NCBIfam; TIGR00187; ribE; 1. DR PANTHER; PTHR21098:SF13; 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 3: Inferred from homology; KW Reference proteome; Repeat; Riboflavin biosynthesis; Transferase. FT CHAIN 1..213 FT /note="Riboflavin synthase" FT /id="PRO_0000068172" 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:0000250|UniProtKB:Q2YN92" 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:0000250|UniProtKB:Q2YN92" 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:0000250|UniProtKB:P0AFU8" 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:0000250|UniProtKB:Q2YN92" 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:0000250|UniProtKB:Q2YN92" FT BINDING 160..165 FT /ligand="2,4-dihydroxypteridine" FT /ligand_id="ChEBI:CHEBI:16489" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q2YN92" SQ SEQUENCE 213 AA; 23445 MW; CD1C7E40E4AC88B6 CRC64; MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT VTEINGNHVS FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS GHIMTTAEVA KILTSENNRQ IWFKVQDSQL MKYILYKGFI GIDGISLTVG EVTPTRFCVH LIPETLERTT LGKKKLGARV NIEIDPQTQA VVDTVERVLA ARENAMNQPG TEA //