ID   FAD1_CAEEL              Reviewed;         519 AA.
AC   Q22017; Q58AA6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
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:R53.1a};
GN   ORFNames=R53.1 {ECO:0000312|WormBase:R53.1a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q22017-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q22017-2; Sequence=VSP_027956;
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}.
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DR   EMBL; Z66515; CAA91346.1; -; Genomic_DNA.
DR   EMBL; Z66515; CAI70410.1; -; Genomic_DNA.
DR   PIR; T24243; T24243.
DR   RefSeq; NP_001022286.1; NM_001027115.2. [Q22017-1]
DR   RefSeq; NP_001022287.1; NM_001027116.3. [Q22017-2]
DR   AlphaFoldDB; Q22017; -.
DR   SMR; Q22017; -.
DR   STRING; 6239.R53.1a.2; -.
DR   EPD; Q22017; -.
DR   PaxDb; Q22017; -.
DR   PeptideAtlas; Q22017; -.
DR   EnsemblMetazoa; R53.1a.1; R53.1a.1; WBGene00011271. [Q22017-1]
DR   EnsemblMetazoa; R53.1b.1; R53.1b.1; WBGene00011271. [Q22017-2]
DR   GeneID; 3565030; -.
DR   KEGG; cel:CELE_R53.1; -.
DR   UCSC; R53.1a.1; c. elegans. [Q22017-1]
DR   CTD; 3565030; -.
DR   WormBase; R53.1a; CE02303; WBGene00011271; flad-1. [Q22017-1]
DR   WormBase; R53.1b; CE38215; WBGene00011271; flad-1. [Q22017-2]
DR   eggNOG; KOG2644; Eukaryota.
DR   GeneTree; ENSGT00390000007266; -.
DR   InParanoid; Q22017; -.
DR   OMA; PDWSNNY; -.
DR   OrthoDB; 1437247at2759; -.
DR   PhylomeDB; Q22017; -.
DR   Reactome; R-CEL-196843; Vitamin B2 (riboflavin) metabolism.
DR   UniPathway; UPA00277; UER00407.
DR   PRO; PR:Q22017; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011271; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q22017; baseline and differential.
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; 1.
DR   PIRSF; PIRSF036620; MPTbdFAD; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; ATP-binding; FAD; Flavoprotein; FMN;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..519
FT                   /note="Probable FAD synthase"
FT                   /id="PRO_0000302743"
FT   REGION          17..108
FT                   /note="Molybdenum cofactor biosynthesis protein-like"
FT   REGION          328..485
FT                   /note="FAD synthase"
FT   VAR_SEQ         1..9
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_027956"
SQ   SEQUENCE   519 AA;  58965 MW;  8B53D20915C85B59 CRC64;
     MRAMFRTPRM PQRKTAAILV IGDEILKGTT RDTNSHFLCK RLHKLGVNIR KISVIGDDIS
     EISREVQSAS GAYDYVITSG GVGPTHDDKT YLGLAHAFTD QMQFSDEIRQ AVNRFLPTYT
     AKKRAEGVGE GLEEAVRLAT EKLCTIPKMS QLLWGTQKIN GSLSTFPVVR ISNVVALPGV
     PKFCERAFDE LQDQLFPIEE RQSLCFETLY TDLDEFDFSK KLTDLAAQFE DRNVQIGSYP
     ELKNKFFKTK LTIETESSET MEAVVTSLRE LLAGHIVYYD SHAWLDIVTK WKAFKKRKAS
     ENQIEFIQKL NEAESIVEEI VEKYPLEQIA LSFNGGKDCT VLLHLLRLKV DEKYGPSTPI
     QGFHIMVEDQ FPEATQFIID AAKFYNIQVL EFPGPLKTGL AALKKTRPSI IPVLMGSRAT
     DPNGKYMKTP VEWTDSDWPQ VLRVCPILNW TYTDVWHMLR GLCVPYCKLY DQGYTSLGGR
     DNTVKHPALR IVSSDGREHY LPAYKLHNDA EERCNRSNI