ID A0A1V3DBG4_STEMA Unreviewed; 208 AA. AC A0A1V3DBG4; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 02-OCT-2024, entry version 23. DE RecName: Full=Riboflavin synthase {ECO:0000256|ARBA:ARBA00013950, ECO:0000256|NCBIfam:TIGR00187}; DE EC=2.5.1.9 {ECO:0000256|ARBA:ARBA00012827, ECO:0000256|NCBIfam:TIGR00187}; GN ORFNames=EKL94_01735 {ECO:0000313|EMBL:RTQ92014.1}; OS Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas OS maltophilia). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Lysobacterales; OC Lysobacteraceae; Stenotrophomonas; Stenotrophomonas maltophilia group. OX NCBI_TaxID=40324 {ECO:0000313|EMBL:RTQ92014.1, ECO:0000313|Proteomes:UP000271705}; RN [1] {ECO:0000313|EMBL:RTQ92014.1, ECO:0000313|Proteomes:UP000271705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDMC339 {ECO:0000313|EMBL:RTQ92014.1, RC ECO:0000313|Proteomes:UP000271705}; RA Kartti S., Manni A., Chemao El Fihri M.W., Laamarti M., Temsamani L., RA El Jamali J.E., Ouadghiri M., Ibrahimi A., Filati-Maltouf A.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00002803}. 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:0000256|ARBA:ARBA00000968}; 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:0000256|ARBA:ARBA00004887}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RTQ92014.1}. 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; RXLZ01000003; RTQ92014.1; -; Genomic_DNA. DR RefSeq; WP_024957263.1; NZ_VLGL01000007.1. DR AlphaFoldDB; A0A1V3DBG4; -. DR OrthoDB; 9788537at2; -. DR Proteomes; UP000271705; Unassembled WGS sequence. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW. 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 4: Predicted; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RTQ92014.1}. SQ SEQUENCE 208 AA; 21905 MW; 40C82A5834C761B7 CRC64; MFTGIIEGVG RLAARESIGG DVRFTFNVGN LPFDNVQMGE SIAINGVCLT VIAFDASSFQ ADASTETLGL TTLGQLGEGS VINLERAMRP TDRLGGHLVS GHVDGLGQVL SIHEDARAQR WRFAAPASLR RYIAKKGSIC VDGVSLTVNE VDDEGFDVAL IPHTVANTAF SAAGVGSAVN LEIDLVARYV ERLISVPTNG QHPQGDVA //