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Database: UniProt
Entry: C0NPN0_AJECG
LinkDB: C0NPN0_AJECG
Original site: C0NPN0_AJECG 
ID   C0NPN0_AJECG            Unreviewed;       323 AA.
AC   C0NPN0;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=HCBG_05110 {ECO:0000313|EMBL:EEH06890.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH06890.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) 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; GG663368; EEH06890.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NPN0; -.
DR   STRING; 447093.C0NPN0; -.
DR   VEuPathDB; FungiDB:I7I50_04705; -.
DR   HOGENOM; CLU_056971_0_1_1; -.
DR   InParanoid; C0NPN0; -.
DR   OrthoDB; 5475801at2759; -.
DR   Proteomes; UP000001631; 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:UP000001631};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          99..271
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   323 AA;  36608 MW;  B1011DFFC9185BCF CRC64;
     MSTRAAGDAL LPNGLEPAQE ECTQENGHTH AQEQECQHLH EEHSQPPLST VVENLHKQVT
     SFLSEPHDAS SMLYRVQNQT RISLNVIQEA LKRFSLNELS LSYNGGKDCL VMLILFLSCL
     HPLPTTESLS KDGKPTPPPT TIPAIYAQPH HPFRSVEEFV ASSSHDYHLS LVRYTTDPPR
     STLRTVFAAY LDHHPQIRAI FVGTRRTDPH GEKLTHFDHT DHGWPGFMRI HPVIDWHYAE
     IWAFIRHLGI EYCPLYDEGY TSLGGTNDTH PNPKLKIISN ENSNDDPIQR PSSSSYTSNG
     GKARYSPAYE LMDDDEERLG RDW
//
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