ID   FLAD1_XENLA             Reviewed;         496 AA.
AC   Q6ING7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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; BC072314; AAH72314.1; -; mRNA.
DR   RefSeq; NP_001085184.1; NM_001091715.1.
DR   AlphaFoldDB; Q6ING7; -.
DR   SMR; Q6ING7; -.
DR   DNASU; 432268; -.
DR   GeneID; 432268; -.
DR   KEGG; xla:432268; -.
DR   CTD; 432268; -.
DR   Xenbase; XB-GENE-5915969; flad1.L.
DR   OrthoDB; 1437247at2759; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 432268; Expressed in camera-type eye and 19 other tissues.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
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..496
FT                   /note="FAD synthase"
FT                   /id="PRO_0000302741"
FT   REGION          18..109
FT                   /note="Molybdenum cofactor biosynthesis protein-like"
FT   REGION          307..464
FT                   /note="FAD synthase"
SQ   SEQUENCE   496 AA;  55709 MW;  D4252F3B84B672E3 CRC64;
     MTSTSPCLAT NVPPVTAGII IIGDEILKGH TQDTNSFFMC KKLRSIGVQV NKISVIPDDI
     DIIAGEIAGF SSRYTYVLTS GGIGPTHDDV TFEGVAKAFG EKTFPHPELV SLVQTFFGKS
     ESWCPEMKLA QIPVSSRLNY GTDKRTGDCF KYPLVSVGNV YVFPGIPSLL EKSLEGLDHL
     FRNDKTHFHY REICVSADEV AIAGVLGEVN GRFRKHVSLG SYPDWSNNYF RVLLVLDSHS
     EAHLEEAHKF LIEHLPPGVV VPFVKDPVTQ AAAQVYQLAH SGSPLGDKVA AALKTLEEAL
     DTYSLEKICV AFNGGKDCTA LLHLFHATVQ RKFPDQKDKL QALYIRIVSP FPEMEQFMQS
     TTKRYNLQIY TIQGYIKQAL VELKVEQPNL EAVLMGTRRS DPYSRTLTPM CLTDPDWPKY
     MRVNPLLDWS YRDIWDFLRT LFIPYCILYD KGYTSLGSME NTVKNPALRF TTPAGAESYH
     PAYKLQNEEE ERVSRK