ID   FAD1_PONAB              Reviewed;         491 AA.
AC   Q5RCH4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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}.
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DR   EMBL; CR858296; CAH90533.1; -; mRNA.
DR   AlphaFoldDB; Q5RCH4; -.
DR   SMR; Q5RCH4; -.
DR   STRING; 9601.ENSPPYP00000000889; -.
DR   eggNOG; KOG2644; Eukaryota.
DR   InParanoid; Q5RCH4; -.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000001595; Unplaced.
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; 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   Acetylation; ATP-binding; Cytoplasm; FAD; Flavoprotein; FMN;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..491
FT                   /note="FAD synthase"
FT                   /id="PRO_0000302739"
FT   REGION          17..108
FT                   /note="Molybdenum cofactor biosynthesis protein-like"
FT   REGION          302..459
FT                   /note="FAD synthase"
FT   REGION          461..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFF5"
FT   MOD_RES         282
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R123"
FT   MOD_RES         282
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R123"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFF5"
SQ   SEQUENCE   491 AA;  54307 MW;  BD18AD9F84592F52 CRC64;
     MTSRASELSP GRSVTAGIII VGDEILKGHT QDTNTFFLCR TLRSLGVQVC RVSVAPDEVA
     TIAAEVTSFS NRFTHVLTAG GIGPTHDDVT FEAVAQAFGD ELKPHPELEA ATKALGGEGW
     EKLSLVPSSA CLHYGTDPRT GHPFRFPLVS VRNVYLFPSI PELLRRVLEG MKGLFQNPAV
     QFHSKELYVA ADEASIAPIL AEAQAHFGRR LGLGSYPDWG SNYYQVKLTL DSRGRRIPGG
     NAWPNLTARL PQGSLVPYMP NAVEQASEAV YKLAESGSSL GKKVAGALQT IETALAQYSL
     TQLCVGFNGG KDCTALLHLF HAAVQRKLPD VPNPLQILYI RSISPFPELE QFLQDTIKRY
     NLQMLEAEGS MKQALGELQA RHPQLEAVLM GTRRTDPYSC SLCPFSPTDP GWPAFMRINP
     LLDWTYRDIW DFLRQLFVPY CILYDRGYTS LGSRENTVRD PALKRLSPGG HPTYRPAYLL
     ENEEEERNSR T
//