ID A0A806NBS7_BRUSS Unreviewed; 202 AA. AC A0A806NBS7; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE SubName: Full=Riboflavin synthase, alpha subunit {ECO:0000313|EMBL:AIJ71688.1}; DE EC=2.5.1.9 {ECO:0000313|EMBL:AIJ71688.1}; GN Name=ribE {ECO:0000313|EMBL:AIJ71688.1}; GN ORFNames=DK67_1676 {ECO:0000313|EMBL:AIJ71688.1}; OS Brucella suis bv. 3 str. 686. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=520487 {ECO:0000313|EMBL:AIJ71688.1, ECO:0000313|Proteomes:UP000028800}; RN [1] {ECO:0000313|EMBL:AIJ71688.1, ECO:0000313|Proteomes:UP000028800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=686 {ECO:0000313|EMBL:AIJ71688.1, RC ECO:0000313|Proteomes:UP000028800}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W., RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. 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; CP007719; AIJ71688.1; -; Genomic_DNA. DR RefSeq; WP_004691908.1; NZ_DS999743.1. DR GeneID; 55590482; -. DR KEGG; bsz:DK67_1676; -. DR Proteomes; UP000028800; Chromosome 1. DR GO; GO:0016740; F:transferase activity; 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 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 4: Predicted; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000313|EMBL:AIJ71688.1}. FT DOMAIN 1..101 FT /note="Lumazine-binding" FT /evidence="ECO:0000259|PROSITE:PS51177" FT REPEAT 1..101 FT /note="Lumazine-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524" FT REPEAT 102..198 FT /note="Lumazine-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524" FT DOMAIN 102..198 FT /note="Lumazine-binding" FT /evidence="ECO:0000259|PROSITE:PS51177" FT REGION 4..6 FT /note="Lumazine 1 binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000498-1" FT REGION 47..49 FT /note="Lumazine 2 binding; shared with one trimeric FT partner" FT /evidence="ECO:0000256|PIRSR:PIRSR000498-1" FT REGION 66..68 FT /note="Lumazine 2 binding; shared with one trimeric FT partner" FT /evidence="ECO:0000256|PIRSR:PIRSR000498-1" FT REGION 105..107 FT /note="Lumazine 2 binding; shared with one trimeric FT partner" FT /evidence="ECO:0000256|PIRSR:PIRSR000498-1" FT REGION 149..151 FT /note="Lumazine 1 binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000498-1" FT REGION 163..168 FT /note="Lumazine 1 binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000498-1" FT BINDING 140 FT /note="Lumazine 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000498-1" SQ SEQUENCE 202 AA; 22190 MW; 836517E20697DAF8 CRC64; MFTGIITDIG KVDRVKPLNE GVLLRIETAY DPETIELGAS IACSGVCLTV VALPEKGSNA RWFEVEAWEE ALRLTTISNW QSGRKINLER SLKLGDEMGG HLVSGHVDGQ AEIVERKDEG DAVRFTLRAP EELAPFIAQK GSVALDGTSL TVNGVNANEF DVLLIRHSLE VTTWGERKAG DKVNIEIDQL ARYAARLAQY QK //