ID A0A176L948_9ACTN Unreviewed; 557 AA.
AC A0A176L948;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=FAD-binding dehydrogenase {ECO:0000313|EMBL:OAB01006.1};
GN ORFNames=A6P39_09205 {ECO:0000313|EMBL:OAB01006.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAB01006.1};
RN [1] {ECO:0000313|EMBL:OAB01006.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAB01006.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAB01006.1}.
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DR EMBL; LWRP01000054; OAB01006.1; -; Genomic_DNA.
DR RefSeq; WP_067042194.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176L948; -.
DR STRING; 710705.A6P39_09205; -.
DR OrthoDB; 9813348at2; -.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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}.
FT DOMAIN 4..538
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 557 AA; 60417 MW; EC4268CE6E22A42C CRC64;
MDADVIVVGA GLAGLVAAHE LTSRGRRVAL VDQENAANLG GQAFWSFGGL FLVDSPEQRR
LGIKDSFDLA WNDWQGSAQF DRLEDEDSWA VRWARAYVEF AAGEKRSWLR GHGIELLPTV
GWAERGDLRA TGHGNSVPRF HIAWGTGTGV VEPFVEYARR AARDGLLTFH HRHQVDELVI
EDGTARGVRG TVLAEDRSPR GVASSRDRAG DFELTAQAVV VTTGGIGANH DIVRRYWPER
LGTPPAEMVT GVPAYVDGRM LDISAGAGVR LVNRDRMWHY TEGLQNWDPI WPGHGIRILP
GPSSVWLDAL GRRLPDPCLP GYDTLSTLRH LRTTEDIAGY DHSWFILTRK IIEKEFALSG
SEQNPDITAK DRGAVLRDRL LGKGAPGPVQ AFVDKGADFV TAGNLEQLVG RMNDLTGKPL
LDAAGVRRQI EARDLQIANP YSKDSQVQGI RNARRYIGDR LGRVAVPHRI LDPAAGPLIG
VRLRVLTRKT LGGIQTDLDS RALAADGTPI EGLYAAGEVA GFGGGGVHGY NALEGTFLGG
CLYSGRAAGR HAARQTG
//