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 27-MAR-2024, entry version 107. 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; 7955-ENSDARP00000094012; -. DR GeneID; 445492; -. DR KEGG; dre:445492; -. DR AGR; ZFIN:ZDB-GENE-040822-44; -. DR CTD; 80308; -. DR ZFIN; ZDB-GENE-040822-44; flad1. DR eggNOG; KOG2644; Eukaryota. DR HOGENOM; CLU_030805_8_0_1; -. DR InParanoid; Q68EH8; -. DR OrthoDB; 5475801at2759; -. 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; Chromosome 16. DR Bgee; ENSDARG00000070390; Expressed in granulocyte and 23 other cell types or 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; HUPs; 1. DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 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 PANTHER; PTHR23293:SF9; FAD SYNTHASE; 1. DR PANTHER; PTHR23293; FAD SYNTHETASE-RELATED FMN ADENYLYLTRANSFERASE; 1. 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; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 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 //