ID   RIBL_METFA              Reviewed;         150 AA.
AC   C7P607;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=Mefer_0147;
OS   Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)
OS   (Methanococcus fervens).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573064;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4213 / JCM 15782 / AG86;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lupa-Sieprawska M., Whitman W.B.;
RT   "Complete sequence of chromosome of Methanocaldococcus fervens AG86.";
RL   Submitted (AUG-2009) 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; CP001696; ACV23989.1; -; Genomic_DNA.
DR   RefSeq; WP_012795011.1; NC_013156.1.
DR   AlphaFoldDB; C7P607; -.
DR   SMR; C7P607; -.
DR   STRING; 573064.Mefer_0147; -.
DR   EnsemblBacteria; ACV23989; ACV23989; Mefer_0147.
DR   GeneID; 8364809; -.
DR   KEGG; mfe:Mefer_0147; -.
DR   eggNOG; arCOG01222; Archaea.
DR   HOGENOM; CLU_034585_2_1_2; -.
DR   OMA; FAKKHAD; -.
DR   OrthoDB; 79845at2157; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000001495; 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; Transferase.
FT   CHAIN           1..150
FT                   /note="FAD synthase"
FT                   /id="PRO_0000406247"
FT   BINDING         11..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT   BINDING         16..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
SQ   SEQUENCE   150 AA;  17249 MW;  8BD35C0D4B039447 CRC64;
     MVKKRVVTAG TFDILHPGHY EVLKFAKSLG DELIVIVARD ETVKKIKGRK PIIPEEQRRE
     MVEALKPVDK AILGSLKNKL EPILELKPDV IVLGPDQTTF DEETLKEELA KYGLHPEIVR
     FKGYKKCPFH SSFDIVKEII RRFCNKEIKI