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Database: UniProt
Entry: W9ICC3_FUSOX
LinkDB: W9ICC3_FUSOX
Original site: W9ICC3_FUSOX 
ID   W9ICC3_FUSOX            Unreviewed;       260 AA.
AC   W9ICC3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=FAD synthase {ECO:0000256|ARBA:ARBA00012393};
DE            EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393};
DE   AltName: Full=FAD pyrophosphorylase {ECO:0000256|ARBA:ARBA00031145};
DE   AltName: Full=FMN adenylyltransferase {ECO:0000256|ARBA:ARBA00031871};
GN   ORFNames=FOYG_07776 {ECO:0000313|EMBL:EWY90166.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY90166.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY90166.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001332};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004726}.
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DR   EMBL; JH717843; EWY90166.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9ICC3; -.
DR   HOGENOM; CLU_056971_0_0_1; -.
DR   OrthoDB; 5475801at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          60..228
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          224..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  29766 MW;  EEF0ECB021943890 CRC64;
     MISTPPPRSL RDKCLELQQK VEAFIAEEAD TQTLRDVQDQ VRKSIEVVDE ALEKYRPEQI
     SLSYNGGKDC LVLLILLLAR MGRHYYSTSD TTNGTSELTP PEKLQCVYIV AAHPFPEVDT
     FVETSSEEYG LEVARYVLPM KKGLEIYLEE RPSIKAVFVG TRRTDPHGEN LTFFDPTDAG
     WPSFMRIHPV IDWHYVQIWA FIRHLGIEYC PLYDQGYTSL GGIKDTHPNP HLKKQGQNGE
     GFRPAYELTQ DDEERLGRDS
//
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