ID   FAD1_DANRE              Reviewed;         497 AA.
AC   Q68EH8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=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=flad1; ORFNames=zgc:91843;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; BC080254; AAH80254.1; -; mRNA.
DR   RefSeq; NP_001003997.1; NM_001003997.1.
DR   AlphaFoldDB; Q68EH8; -.
DR   SMR; Q68EH8; -.
DR   STRING; 7955.ENSDARP00000094012; -.
DR   PaxDb; Q68EH8; -.
DR   Ensembl; ENSDART00000103235; ENSDARP00000094012; ENSDARG00000070390.
DR   GeneID; 445492; -.
DR   KEGG; dre:445492; -.
DR   CTD; 80308; -.
DR   ZFIN; ZDB-GENE-040822-44; flad1.
DR   eggNOG; KOG2644; Eukaryota.
DR   GeneTree; ENSGT00390000007266; -.
DR   HOGENOM; CLU_030805_8_0_1; -.
DR   InParanoid; Q68EH8; -.
DR   OMA; PDWSNNY; -.
DR   PhylomeDB; Q68EH8; -.
DR   TreeFam; TF314056; -.
DR   Reactome; R-DRE-196843; Vitamin B2 (riboflavin) metabolism.
DR   UniPathway; UPA00277; UER00407.
DR   PRO; PR:Q68EH8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000070390; Expressed in granulocyte and 23 other tissues.
DR   ExpressionAtlas; Q68EH8; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..497
FT                   /note="FAD synthase"
FT                   /id="PRO_0000302740"
FT   REGION          19..110
FT                   /note="Molybdenum cofactor biosynthesis protein-like"
FT   REGION          308..465
FT                   /note="FAD synthase"
SQ   SEQUENCE   497 AA;  55610 MW;  D71C34BE8FA99DFF CRC64;
     MAQNCNTSST QKNGSATAAI LIIGDEILKG HTVDTNSAFL CRGLRKLGIT VERITVVPDV
     QEVIAKEVSQ LSSTVTHLIT SGGIGPTHDD VTFESVAMAF GEELYAHPEM TKLVEGFFGT
     VTSDSAPMKL AMVPASAKLN FGIDPQTGQR NRFPLVSVHN VYIFPGIPSL LEKSFNGLSH
     LFSGSGTTFH TREVFVNADE TEIAQSLSKL QAGWGKRVSL GSYPDWLSNY HRVRLVLDTD
     SVEEVERART QLIEELPKGS VVPLVTDPIS VAAQEVYSLS KSETQLGKKV AAALGTIEMA
     LDKYSVNEIC VGFNGGKDCT ALLHLYYAAL KRRYPDGKDR LKALYIRIVS PFPEMERFLQ
     DTIKRYDLEL FSVEGSIRQA LNEVKERRPD LRAVLMGTRR TDPYSHTLTP FCPTDPGWPD
     YMRVNPLLEW TYHDIWSFLR TLYVPYCILY DKGYTSLGSM DNSYRNPSLK MVDERGATRY
     KPAYMLENEE EERNSRE