ID A1CBU3_ASPCL Unreviewed; 567 AA.
AC A1CBU3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=3-ketosteroid-delta-1-dehydrogenase, putative {ECO:0000313|EMBL:EAW13211.1};
GN ORFNames=ACLA_016570 {ECO:0000313|EMBL:EAW13211.1};
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:EAW13211.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW13211.1, 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; DS027049; EAW13211.1; -; Genomic_DNA.
DR RefSeq; XP_001274637.1; XM_001274636.1.
DR AlphaFoldDB; A1CBU3; -.
DR STRING; 344612.A1CBU3; -.
DR EnsemblFungi; EAW13211; EAW13211; ACLA_016570.
DR GeneID; 4706695; -.
DR KEGG; act:ACLA_016570; -.
DR VEuPathDB; FungiDB:ACLA_016570; -.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_022946_0_0_1; -.
DR OMA; PEDHWPR; -.
DR OrthoDB; 1819728at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR014614; KsdD_DH.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR43260; 3-KETOSTEROID-DELTA-1-DEHYDROGENASE; 1.
DR PANTHER; PTHR43260:SF1; KSDD-LIKE STEROID DEHYDROGENASE RV0785; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PIRSF; PIRSF036654; UCP036654; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 8..540
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 567 AA; 62004 MW; 1FC6DE31150D9E5C CRC64;
MASSEEPVII VGAGLAGLVA AYELSQRNIH TIIVDQENAA NLGGQAFWSL GGIFCVDSSN
QRRLGIRDSR ELAMQDWFNS AGFDRETDLW PRKWAEAFVN FATDDLESYL NALGVRFTSV
GWAERGSGMA GGHGNSVPRF HITWGTGPAI VEAFAGPVRE AEKKGLVDFR FRHRVNEIVV
DPDTGAALGV RGQVLEPTNA ERGVSSSRVG IYDFELLGPA VLISSGGIGG NLGLVKKYWP
VDRLGPKVPR SFVLGVPAHV DGRMIEISQK VGANVINSDR MWHYTEGLTN WDPIWPQHGI
RVIPGPSSLW LDATGRRLPP FLYPGCDTLA TLRHICSTGY DYTWFVLNKT IIAREFALSG
SEQNPDITNK SILLLLQRLF GSNGTGPVQA FMKNGEDFIV EPALEELLER MGQLGQKHGG
PLLDKDQVQR EIKLRDSQTD NEYTKDAQLM LIRNARNFWP DKYTRVVKPH KLLDPRHGPL
IAVRMNLLTR KTLGGLETDL SANVLRSDGT RFTNLYAAGE VVGFGGGGVH GYNSLEGTFL
GGCIFLGRTA GIAIAEGLAG LLVQIES
//
