ID   RIBL_ACIB4              Reviewed;         149 AA.
AC   B5I9H4; B5IC32;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
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}; OrderedLocusNames=Aboo_0747;
GN   ORFNames=ABOONEI_1934, ABOONEI_2228;
OS   Aciduliprofundum boonei (strain DSM 19572 / T469).
OC   Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX   NCBI_TaxID=439481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19572 / T469;
RX   PubMed=18445019; DOI=10.1111/j.1472-4669.2008.00152.x;
RA   Reysenbach A.L., Flores G.E.;
RT   "Electron microscopy encounters with unusual thermophiles helps direct
RT   genomic analysis of Aciduliprofundum boonei.";
RL   Geobiology 6:331-336(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19572 / T469;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT   "Complete sequence of Aciduliprofundum boonei T469.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; DS990515; EDY37013.1; -; Genomic_DNA.
DR   EMBL; DS990517; EDY36241.1; -; Genomic_DNA.
DR   EMBL; CP001941; ADD08556.1; -; Genomic_DNA.
DR   RefSeq; WP_008082530.1; NZ_DS990515.1.
DR   AlphaFoldDB; B5I9H4; -.
DR   SMR; B5I9H4; -.
DR   STRING; 439481.Aboo_0747; -.
DR   EnsemblBacteria; ADD08556; ADD08556; Aboo_0747.
DR   EnsemblBacteria; EDY36241; EDY36241; ABOONEI_2228.
DR   EnsemblBacteria; EDY37013; EDY37013; ABOONEI_1934.
DR   GeneID; 8827694; -.
DR   KEGG; abi:Aboo_0747; -.
DR   eggNOG; arCOG01222; Archaea.
DR   HOGENOM; CLU_034585_2_1_2; -.
DR   OMA; FAKKHAD; -.
DR   OrthoDB; 79845at2157; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000001400; 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; -; 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   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..149
FT                   /note="FAD synthase"
FT                   /id="PRO_0000406231"
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         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT   CONFLICT        25
FT                   /note="R -> K (in Ref. 1; EDY36241)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="D -> E (in Ref. 1; EDY36241)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   149 AA;  17380 MW;  F820A8DD1EC44056 CRC64;
     MVRVMATGVF DILHPGHVLF LREARKLGDE LVVVVARDST VERLKHKPIM NEDIRRFMVE
     SLKPVDRAVL GHKDDMYKTV EDVRPDIIVL GYDQKFDEKE IEEECRKRGI KVKVVRLKKY
     GDSDLNGTRK IIFKIVDRVD DLYAKDRNS