ID   RIBL_HALLT              Reviewed;         153 AA.
AC   B9LSN4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=Hlac_2406;
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
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}.
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; CP001365; ACM57981.1; -; Genomic_DNA.
DR   RefSeq; WP_015911100.1; NC_012029.1.
DR   AlphaFoldDB; B9LSN4; -.
DR   SMR; B9LSN4; -.
DR   GeneID; 7400524; -.
DR   KEGG; hla:Hlac_2406; -.
DR   eggNOG; arCOG01222; Archaea.
DR   HOGENOM; CLU_034585_2_1_2; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000000740; Chromosome 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..153
FT                   /note="FAD synthase"
FT                   /id="PRO_0000406241"
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   153 AA;  16936 MW;  BCCD541325192B02 CRC64;
     MTRVVAQGTF DLLHPGHVHY LEDAATYGDE LHAIVARRTN VTHKPAPILC AEQRRDMVAA
     LTAVDEAHLG HPEDVFVPIQ RLDPDVIVLG FDQHHDEADI AAALAERGID CRVERASGRD
     PRYEDELLSS GDIVDRILKQ RGSDCDGARE GQR
//