ID A0A1B1NLS9_9VIBR Unreviewed; 217 AA. AC A0A1B1NLS9; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 27-MAR-2024, entry version 24. DE RecName: Full=Riboflavin synthase {ECO:0000256|ARBA:ARBA00013950}; DE EC=2.5.1.9 {ECO:0000256|ARBA:ARBA00012827}; GN Name=ribE {ECO:0000313|EMBL:ANS84642.1}; GN ORFNames=VSF3289_02484 {ECO:0000313|EMBL:ODS12196.1}, VSVS05_02146 GN {ECO:0000313|EMBL:ANU37250.1}, VSVS12_00854 GN {ECO:0000313|EMBL:ANS84642.1}; OS Vibrio scophthalmi. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=45658 {ECO:0000313|EMBL:ANS84642.1, ECO:0000313|Proteomes:UP000092656}; RN [1] {ECO:0000313|EMBL:ANS84642.1, ECO:0000313|Proteomes:UP000092656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VS-12 {ECO:0000313|EMBL:ANS84642.1, RC ECO:0000313|Proteomes:UP000092656}; RA Han H.-J.; RT "Genome sequencing of Vibrio scophthalmi strain VS-12, an isolated from RT Paralichthys olivaceus."; RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ANU37250.1, ECO:0000313|Proteomes:UP000092528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VS-05 {ECO:0000313|EMBL:ANU37250.1, RC ECO:0000313|Proteomes:UP000092528}; RA Han H.-J.; RT "Genome sequencing of Vibrio scophthalmi strain VS-05, an isolated from RT Paralichthys olivaceus."; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ODS12196.1, ECO:0000313|Proteomes:UP000095131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FP3289 {ECO:0000313|EMBL:ODS12196.1, RC ECO:0000313|Proteomes:UP000095131}; RA Han H.-J.; RT "Genome sequencing of Vibrio scophthalmi strain FP3289, an isolated from RT Paralichthys olivaceus."; RL Submitted (AUG-2016) 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 --------------------------------------------------------------------------- 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; CP016307; ANS84642.1; -; Genomic_DNA. DR EMBL; CP016414; ANU37250.1; -; Genomic_DNA. DR EMBL; MDCJ01000002; ODS12196.1; -; Genomic_DNA. DR RefSeq; WP_005592771.1; NZ_MDCJ01000002.1. DR AlphaFoldDB; A0A1B1NLS9; -. DR STRING; 45658.VSVS12_00854; -. DR KEGG; vsc:VSVS12_00854; -. DR PATRIC; fig|45658.6.peg.811; -. DR OrthoDB; 9788537at2; -. DR Proteomes; UP000092528; Chromosome 1. DR Proteomes; UP000092656; Chromosome 1. DR Proteomes; UP000095131; Unassembled WGS sequence. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC. 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:ANS84642.1}. FT REPEAT 1..97 FT /note="Lumazine-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524" FT DOMAIN 1..97 FT /note="Lumazine-binding" FT /evidence="ECO:0000259|PROSITE:PS51177" FT REPEAT 98..194 FT /note="Lumazine-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524" FT DOMAIN 98..194 FT /note="Lumazine-binding" FT /evidence="ECO:0000259|PROSITE:PS51177" SQ SEQUENCE 217 AA; 23618 MW; 1B1C124B42C524C3 CRC64; MFTGIVEAVG TLTAITPKGE DISVTVSSNK LDMSDVKLGD SIATNGVCLT VVAFNDHSYT ADLSLETLNK TGFTHYQAGD KVNLEKAMLP TTRFGGHIVS GHVDGVGEIV ERNQVGRSIE FWVAMPEELN KYVAEKGSIT VDGISLTVNA LRKNAFKLTI VPHTGEETTI ADFHVGRKVN LEVDVLARYM ERLLTSQQAA QPESRITMEF LQQNGFA //