ID   RIBC_LISMO              Reviewed;         246 AA.
AC   Q8Y914;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=FAD synthetase {ECO:0000303|PubMed:27672192};
DE            EC=2.7.7.2 {ECO:0000269|PubMed:27672192};
DE   AltName: Full=FMN adenylyltransferase {ECO:0000305};
DE   AltName: Full=Flavin adenine dinucleotide synthase {ECO:0000305};
GN   Name=ribC {ECO:0000303|PubMed:27672192};
GN   OrderedLocusNames=lmo0728 {ECO:0000312|EMBL:CAC98806.1};
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=27672192; DOI=10.1128/jb.00388-16;
RA   Matern A., Pedrolli D., Grosshennig S., Johansson J., Mack M.;
RT   "Uptake and metabolism of antibiotics roseoflavin and 8-demethyl-8-
RT   aminoriboflavin in riboflavin-auxotrophic Listeria monocytogenes.";
RL   J. Bacteriol. 198:3233-3243(2016).
CC   -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to
CC       form flavin adenine dinucleotide (FAD) coenzyme (PubMed:27672192). Can
CC       also catalyze, with lower efficiency, the adenylation of the toxic
CC       riboflavin analogs 8-demethyl-8-aminoriboflavin mononucleotide (AFMN)
CC       and roseoflavin mononucleotide (RoFMN) to 8-demethyl-8-aminoriboflavin
CC       adenine dinucleotide (AFAD) and roseoflavin adenine dinucleotide
CC       (RoFAD), respectively (PubMed:27672192). {ECO:0000269|PubMed:27672192}.
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:27672192};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.9 uM for FMN {ECO:0000269|PubMed:27672192};
CC         Vmax=1093 nmol/min/mg enzyme {ECO:0000269|PubMed:27672192};
CC         Note=kcat is 0.51 sec(-1). {ECO:0000269|PubMed:27672192};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1. {ECO:0000269|PubMed:27672192}.
CC   -!- SIMILARITY: Belongs to the RibF family. {ECO:0000305}.
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DR   EMBL; AL591976; CAC98806.1; -; Genomic_DNA.
DR   PIR; AH1165; AH1165.
DR   RefSeq; NP_464255.1; NC_003210.1.
DR   RefSeq; WP_003721848.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y914; -.
DR   SMR; Q8Y914; -.
DR   STRING; 169963.lmo0728; -.
DR   PaxDb; Q8Y914; -.
DR   EnsemblBacteria; CAC98806; CAC98806; CAC98806.
DR   GeneID; 986299; -.
DR   KEGG; lmo:lmo0728; -.
DR   PATRIC; fig|169963.11.peg.750; -.
DR   eggNOG; COG0196; Bacteria.
DR   HOGENOM; CLU_048437_0_2_9; -.
DR   OMA; KSASCFI; -.
DR   PhylomeDB; Q8Y914; -.
DR   BioCyc; LMON169963:LMO0728-MON; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008531; F:riboflavin kinase activity; IBA:GO_Central.
DR   GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009398; P:FMN biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   GO; GO:0006771; P:riboflavin metabolic process; IBA:GO_Central.
DR   CDD; cd02064; FAD_synthetase_N; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR015864; FAD_synthase.
DR   InterPro; IPR023468; Riboflavin_kinase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR22749; PTHR22749; 1.
DR   Pfam; PF06574; FAD_syn; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..246
FT                   /note="FAD synthetase"
FT                   /id="PRO_0000448896"
SQ   SEQUENCE   246 AA;  27714 MW;  A5DF63A4AA84F69C CRC64;
     MEVSHVTLAP NKDSRAAVLT IGKFDGVHIG HQTILNTALS IKKENEILTA ISFSPHPLWA
     LKQIEIYREM LTPRMEKERW LAYYGVNHLI ETEFTSRYAE TTPEEFVTDH LTNLNLSHIV
     VGSEFNFGKG RDSDVDLLRD LCKPYDIGVT SVPVIETNQT KISSTNIRAF IRRGHFQEAE
     ELLGHPWYIT GIVENGEMTG LDDYVLPATG TYQTDSGIVN VTNNRTIEVG LSDGLQQLHM
     KNELSE