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RIBL_HALJB
ID   RIBL_HALJB              Reviewed;         142 AA.
AC   D8J4S4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
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=HacjB3_10790;
OS   Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / KCTC
OS   4019 / B3).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halalkalicoccus.
OX   NCBI_TaxID=795797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18796 / CECT 7217 / JCM 14584 / KCTC 4019 / B3;
RX   PubMed=20601480; DOI=10.1128/jb.00663-10;
RA   Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT   "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely
RT   halophilic archaeon.";
RL   J. Bacteriol. 192:4528-4529(2010).
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; CP002062; ADJ15541.1; -; Genomic_DNA.
DR   RefSeq; WP_008416928.1; NZ_AXZD01000008.1.
DR   AlphaFoldDB; D8J4S4; -.
DR   SMR; D8J4S4; -.
DR   STRING; 795797.C497_11877; -.
DR   EnsemblBacteria; ADJ15541; ADJ15541; HacjB3_10790.
DR   GeneID; 9419968; -.
DR   KEGG; hje:HacjB3_10790; -.
DR   eggNOG; arCOG01222; Archaea.
DR   HOGENOM; CLU_034585_2_1_2; -.
DR   OMA; FAKKHAD; -.
DR   OrthoDB; 79845at2157; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000000390; 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..142
FT                   /note="FAD synthase"
FT                   /id="PRO_0000406235"
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   142 AA;  15831 MW;  DEE37D58BFB4CE45 CRC64;
     MVRALAQGTF DLLHPGHIHY LEEAARMGDE LYVIVARSAN VTHKRAPVLD GRQRRDMIGA
     LEVVDHALLG HESDIFVPIE EIDPDVIVLG HDQHHDEAAI ERALGDRGID CGVRRASPRD
     PAYDGELLST GRIVDRICER RC
 
 
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