ID RIBL_METJA Reviewed; 149 AA. AC Q58579; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=FAD synthase {ECO:0000255|HAMAP-Rule:MF_02115}; DE EC=2.7.7.2 {ECO:0000269|PubMed:20822113}; 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; OrderedLocusNames=MJ1179; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC RP PARAMETERS, ACTIVITY REGULATION, GENE NAME, PATHWAY, SUBUNIT, AND RP MUTAGENESIS OF CYS-126 AND CYS-143. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=20822113; DOI=10.1021/bi100817q; RA Mashhadi Z., Xu H., Grochowski L.L., White R.H.; RT "Archaeal RibL: a new FAD synthetase that is air sensitive."; RL Biochemistry 49:8748-8755(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. To a lesser extent, is also able to utilize other nucleotides CC such as CTP and GTP as substrates, producing the modified coenzymes, CC flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide CC (FGD), respectively. Does not catalyze the reverse reaction to produce CC FMN and ATP from FAD and PPi. Does not function as a glycerol-3- CC phosphate cytidylyltransferase, as previously annotated in the complete CC genome. {ECO:0000269|PubMed:20822113}. 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:0000269|PubMed:20822113}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:20822113}; CC Note=Divalent metal cations. The best activity is observed with Co(2+), CC where the activity is 4 and 2.5 times greater than that with Mg(2+) and CC Mn(2+), respectively. {ECO:0000269|PubMed:20822113}; CC -!- ACTIVITY REGULATION: Is inhibited by the product PPi. CC {ECO:0000269|PubMed:20822113}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25 uM for ATP {ECO:0000269|PubMed:20822113}; CC KM=63 uM for FMN {ECO:0000269|PubMed:20822113}; CC KM=480 uM for CTP {ECO:0000269|PubMed:20822113}; CC Vmax=14 nmol/min/mg enzyme with ATP and FMN as substrates CC {ECO:0000269|PubMed:20822113}; CC Vmax=10 nmol/min/mg enzyme with CTP and FMN as substrates CC {ECO:0000269|PubMed:20822113}; CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step CC 1/1. {ECO:0000269|PubMed:20822113}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20822113}. CC -!- MISCELLANEOUS: Alkylation of both Cys-126 and Cys-143 results in CC complete loss of enzymatic activity. {ECO:0000269|PubMed:20822113}. CC -!- SIMILARITY: Belongs to the archaeal FAD synthase family. {ECO:0000305}. 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; L77117; AAB99182.1; -; Genomic_DNA. DR PIR; B64447; B64447. DR RefSeq; WP_010870692.1; NC_000909.1. DR AlphaFoldDB; Q58579; -. DR SMR; Q58579; -. DR STRING; 243232.MJ_1179; -. DR PaxDb; 243232-MJ_1179; -. DR EnsemblBacteria; AAB99182; AAB99182; MJ_1179. DR GeneID; 1452077; -. DR KEGG; mja:MJ_1179; -. DR eggNOG; arCOG01222; Archaea. DR HOGENOM; CLU_034585_2_1_2; -. DR InParanoid; Q58579; -. DR OrthoDB; 1912at2157; -. DR PhylomeDB; Q58579; -. DR BioCyc; MetaCyc:MONOMER-16487; -. DR BRENDA; 2.7.7.2; 3260. DR SABIO-RK; Q58579; -. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0002135; F:CTP binding; IDA:UniProtKB. DR GO; GO:0003919; F:FMN adenylyltransferase activity; IDA:UniProtKB. DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006747; P:FAD biosynthetic process; IDA:UniProtKB. DR GO; GO:0046444; P:FMN metabolic process; IDA:UniProtKB. DR CDD; cd02170; cytidylyltransferase; 1. 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 1: Evidence at protein level; KW ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1..149 FT /note="FAD synthase" FT /id="PRO_0000107202" FT BINDING 10..11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115" FT BINDING 15..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115" FT BINDING 95 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115" FT MUTAGEN 126 FT /note="C->S: 2-fold increase in activity with Mg(2+) but FT loss of activity with Co(2+) as cofactor." FT /evidence="ECO:0000269|PubMed:20822113" FT MUTAGEN 143 FT /note="C->S: Nearly no change in activity with Mg(2+) but FT loss of activity with Co(2+) as cofactor." FT /evidence="ECO:0000269|PubMed:20822113" SQ SEQUENCE 149 AA; 17288 MW; 55FD11671ED94594 CRC64; MKKRVVTAGT FDILHPGHYE ILKFAKSLGD ELIVIVARDE TVKKLKGRKP IIPEEQRREM VEALKPVDKA ILGSLKNKLE PILELKPDII VLGPDQTTFD EETLKKELAK YNLYPEIVRF RGYKKCPFHS SFDIVKEIIR RFCNKEIKI //