ID   FAD1_SCHPO              Reviewed;         265 AA.
AC   O74841;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 126.
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;
GN   ORFNames=SPCC1235.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Adenylates FMN to FAD. {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   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. FAD1 subfamily.
CC       {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; CU329672; CAA21108.1; -; Genomic_DNA.
DR   PIR; T40878; T40878.
DR   RefSeq; NP_587730.1; NM_001022725.2.
DR   AlphaFoldDB; O74841; -.
DR   SMR; O74841; -.
DR   STRING; 284812.O74841; -.
DR   iPTMnet; O74841; -.
DR   MaxQB; O74841; -.
DR   PaxDb; 4896-SPCC1235-04c-1; -.
DR   EnsemblFungi; SPCC1235.04c.1; SPCC1235.04c.1:pep; SPCC1235.04c.
DR   GeneID; 2539270; -.
DR   KEGG; spo:SPCC1235.04c; -.
DR   PomBase; SPCC1235.04c; -.
DR   VEuPathDB; FungiDB:SPCC1235.04c; -.
DR   eggNOG; KOG2644; Eukaryota.
DR   HOGENOM; CLU_056971_0_1_1; -.
DR   InParanoid; O74841; -.
DR   OMA; EEFVQWS; -.
DR   PhylomeDB; O74841; -.
DR   Reactome; R-SPO-196843; Vitamin B2 (riboflavin) metabolism.
DR   UniPathway; UPA00277; UER00407.
DR   PRO; PR:O74841; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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   GO; GO:0046444; P:FMN metabolic process; ISS:PomBase.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
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; PF01507; PAPS_reduct; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..265
FT                   /note="Probable FAD synthase"
FT                   /id="PRO_0000100690"
SQ   SEQUENCE   265 AA;  30608 MW;  BC6C662E6F43A6F3 CRC64;
     MDELERVYQS IKNIFTHSAP SEKLVGLQNR LSISLRFIEY AFETYQPERL AMSFNGGKDC
     LVLFLLCIYY LKEKYKEQAQ AKLSNIPFVF VRPRDEFPEM DDFVNECQSK YRLNIIKISL
     PMKEAFCKFL KEHKHIQAIL IGIRRLDPHG LHRIAFEVTD KGWPKFMRIQ PILDWSYTEI
     WDLLLETNTK YCSLYDRGYT SLGGVSDTSP NPALKNPDGT YSPAYLLSDG SLERAGRNNT
     VPFSRTNSRF LYDSGASSYA SSEVS
//