ID A1CGT2_ASPCL Unreviewed; 613 AA.
AC A1CGT2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Flavin-binding monooxygenase, putative {ECO:0000313|EMBL:EAW10087.1};
GN ORFNames=ACLA_045520 {ECO:0000313|EMBL:EAW10087.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10087.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW10087.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027054; EAW10087.1; -; Genomic_DNA.
DR RefSeq; XP_001271513.1; XM_001271512.1.
DR AlphaFoldDB; A1CGT2; -.
DR STRING; 344612.A1CGT2; -.
DR EnsemblFungi; EAW10087; EAW10087; ACLA_045520.
DR GeneID; 4704129; -.
DR KEGG; act:ACLA_045520; -.
DR VEuPathDB; FungiDB:ACLA_045520; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006937_7_0_1; -.
DR OMA; FDQFRIF; -.
DR OrthoDB; 49786at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF5; L-ORNITHINE N(5)-OXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:EAW10087.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
SQ SEQUENCE 613 AA; 69289 MW; 9317D2C83FD26533 CRC64;
MISSVAKIHN RHIYGKDAHT YYPVLAIGAG ESGIATGCRL KEALGFDQFR IFERQSGIGG
TWWSNRYPGV ACDVPALLYS FSFAPKKDWT TLRPPGPEIA QYLADVCEKF AIVDKIQLNT
DVKEMRWLEG AEEWEVTLSH LVPGTGDLSQ EERDALVIRE GERSVYVKTE VVRAKIVVSG
VGCLVEPKTW PKNIPGIETF EGRVVHTARW KEDIDLEGKN VVVVGSGCSA AQVVPVLTRP
ESKVKSVTQL MRSPPWFMAE FLSVDALDKW EKYTPSLFRN VPGLTFSARA LLFFRLEWDF
IRIFKDNGLA RRLRSKLERE FLEHMHSNAP EKYHEILTPN YSLGCKRRIV ESHYFDSIHA
PNFELTTMPL ASVQAKGVTL GPGKVYPPDV IILANGYETN KWLHPLRVVG RGGRTLDEIW
EERGGAQAYL GIAMDHMPNL FLSFGPNTAT GHTSVIFAIE NAINYSLNFI KPILDGHVST
FEVTEEAERR WTDKVQKSLQ STVFRRGACT SWYQSDEGWN SSTYPFTQID YYFRCTFPVW
HHWTARYTPK GLAAQRVRSG LKKVALLAIA TGLFWLTKRP QDINLLIQLA VGLRGSIITG
IRDGLLHVHR MLS
//
