ID RIBL_HALVD Reviewed; 142 AA. AC D4GVJ2; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 1. DT 27-MAR-2024, entry version 60. DE RecName: Full=FAD synthase {ECO:0000255|HAMAP-Rule:MF_02115}; DE EC=2.7.7.2 {ECO:0000255|HAMAP-Rule:MF_02115}; DE AltName: Full=FMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_02115}; DE AltName: Full=Flavin adenine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_02115}; GN Name=ribL {ECO:0000255|HAMAP-Rule:MF_02115}; GN OrderedLocusNames=HVO_1015; OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales; OC Haloferacaceae; Haloferax. OX NCBI_TaxID=309800; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM B-1768 / DS2; RX PubMed=20333302; DOI=10.1371/journal.pone.0009605; RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.; RT "The complete genome sequence of Haloferax volcanii DS2, a model RT archaeon."; RL PLoS ONE 5:E9605-E9605(2010). CC -!- FUNCTION: Catalyzes the transfer of the AMP portion of ATP to flavin CC mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) CC coenzyme. {ECO:0000255|HAMAP-Rule:MF_02115}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02115}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02115}; CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_02115}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02115}. CC -!- SIMILARITY: Belongs to the archaeal FAD synthase family. CC {ECO:0000255|HAMAP-Rule:MF_02115}. 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; CP001956; ADE04925.1; -; Genomic_DNA. DR RefSeq; WP_004043927.1; NZ_AOHU01000092.1. DR AlphaFoldDB; D4GVJ2; -. DR SMR; D4GVJ2; -. DR STRING; 309800.HVO_1015; -. DR PaxDb; 309800-C498_13684; -. DR EnsemblBacteria; ADE04925; ADE04925; HVO_1015. DR GeneID; 8926321; -. DR KEGG; hvo:HVO_1015; -. DR eggNOG; arCOG01222; Archaea. DR HOGENOM; CLU_034585_2_1_2; -. DR OrthoDB; 1912at2157; -. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000008243; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046444; P:FMN metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_02115; FAD_synth_arch; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR024902; FAD_synth_RibL. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00125; cyt_tran_rel; 1. DR PANTHER; PTHR43793; FAD SYNTHASE; 1. DR PANTHER; PTHR43793:SF1; FAD SYNTHASE; 1. DR Pfam; PF01467; CTP_transf_like; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. PE 3: Inferred from homology; KW ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1..142 FT /note="FAD synthase" FT /id="PRO_0000406238" FT BINDING 9..10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115" FT BINDING 14..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115" FT BINDING 92 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115" SQ SEQUENCE 142 AA; 15973 MW; 1FB2D51BA439572C CRC64; MRRVIAQGTF DILHPGHVHY LSDAASLGDE LHVIIARGEN VTHKPKPILD GRQRRDMVAA LDVVDEAHLG HVEDIFVPIE EIDPDVIVLG YDQHHDEDGI KAALDARGID CEVTRATPRE LRHDDELLST GRIIDRIVER RC //