ID   FAD1_CAEBR              Reviewed;         523 AA.
AC   Q626I0; A8WP73;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Probable FAD synthase;
DE            EC=2.7.7.2;
DE   AltName: Full=FAD pyrophosphorylase;
DE   AltName: Full=FMN adenylyltransferase;
DE   AltName: Full=Flavin adenine dinucleotide synthase;
DE   Includes:
DE     RecName: Full=Molybdenum cofactor biosynthesis protein-like region;
DE   Includes:
DE     RecName: Full=FAD synthase region;
GN   Name=flad-1 {ECO:0000312|WormBase:CBG00973a};
GN   ORFNames=CBG00973 {ECO:0000312|WormBase:CBG00973a};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to
CC       form flavin adenine dinucleotide (FAD) coenzyme. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1.
CC   -!- DOMAIN: The molybdenum cofactor biosynthesis protein-like region may
CC       not be functional.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PAPS reductase
CC       family. FAD1 subfamily. {ECO:0000305}.
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; HE600951; CAP22279.1; -; Genomic_DNA.
DR   RefSeq; XP_002629740.1; XM_002629694.1.
DR   AlphaFoldDB; Q626I0; -.
DR   SMR; Q626I0; -.
DR   STRING; 6238.CBG00973; -.
DR   EnsemblMetazoa; CBG00973a.1; CBG00973a.1; WBGene00024275.
DR   GeneID; 8573234; -.
DR   KEGG; cbr:CBG_00973; -.
DR   CTD; 8573234; -.
DR   WormBase; CBG00973a; CBP00276; WBGene00024275; Cbr-flad-1.
DR   eggNOG; KOG2644; Eukaryota.
DR   HOGENOM; CLU_030805_8_0_1; -.
DR   InParanoid; Q626I0; -.
DR   OMA; PDWSNNY; -.
DR   OrthoDB; 1437247at2759; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006747; P:FAD biosynthetic process; IBA:GO_Central.
DR   CDD; cd00885; cinA; 1.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR012183; FAD_synth_MoaB/Mog-bd.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF01507; PAPS_reduct; 2.
DR   PIRSF; PIRSF036620; MPTbdFAD; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
PE   3: Inferred from homology;
KW   ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..523
FT                   /note="Probable FAD synthase"
FT                   /id="PRO_0000302742"
FT   REGION          20..111
FT                   /note="Molybdenum cofactor biosynthesis protein-like"
FT   REGION          332..489
FT                   /note="FAD synthase"
SQ   SEQUENCE   523 AA;  59503 MW;  5025F6031432F6A1 CRC64;
     MRAIFRATKR MPPGQRKTAA IVVIGDEILK GTTRDTNSHF LCKRLHKLGV NIKKIAVVGD
     EISEISREVQ SASSAYDYVI TSGGVGPTHD DKTYLGLAHA FTDQLHFSDE IRQAVNRFLP
     TYIDKKKSEG VEEGIEEVVR VVTEKLCTIP KMSQLLWGTQ KVDGRVSTFP VVRVANVVAL
     PGVPKFCERA FDELQDQLFP VEERQSMFFD TIYTDLDEFD FSRRLADVAA RFEEQNVQIG
     SYPELKNKFF KTKLTIETES SESMEAVRIA LKELLVGHIV YYDSHAWTDT VAKWRAFKKR
     ELVEAKNVDF VRKLEEAEKI VEDIVERYPL DQIALSFNGG KDCTVLLHLL RLKVDEKYGA
     SKAIQGFHIM VEDQFPEATQ FIIDAAQFYN IQVLEFPGPL KIGLAGLKKQ RPSIIPVLMG
     SRATDPNGKY MKTPVEWTDS DWPKVLRVCP ILNWTYSDVW HMLRGLCVPY CKLYDQGYTS
     LGGRDNTVKH PALRIVASDG KEHYLPAYKL HNDAEERSNR SNL