ID   RIBL_HALS3              Reviewed;         146 AA.
AC   B0R450;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=OE_2139R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP13515.1; -; Genomic_DNA.
DR   RefSeq; WP_010902542.1; NC_010364.1.
DR   AlphaFoldDB; B0R450; -.
DR   SMR; B0R450; -.
DR   EnsemblBacteria; CAP13515; CAP13515; OE_2139R.
DR   GeneID; 68693626; -.
DR   KEGG; hsl:OE_2139R; -.
DR   HOGENOM; CLU_034585_2_1_2; -.
DR   PhylomeDB; B0R450; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000001321; 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   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   3: Inferred from homology;
KW   ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..146
FT                   /note="FAD synthase"
FT                   /id="PRO_0000406237"
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   146 AA;  16002 MW;  6180FB34D13242F8 CRC64;
     MTRVVAQGTF DLIHPGHVHY LEDAAAMGDE LHVILARREN VTHKDPPVLP NRQRRDVVAA
     LDPVDHARIG HPEDIFAPIE AIDPDVIALG FDQHHDAAAI EAELADRGLD CAVERASPRE
     ARYDDEVLSS GDIADRVLAQ RGDSDP
//