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Database: UniProt
Entry: A0A2V4NK50_9ACTN
LinkDB: A0A2V4NK50_9ACTN
Original site: A0A2V4NK50_9ACTN 
ID   A0A2V4NK50_9ACTN        Unreviewed;       556 AA.
AC   A0A2V4NK50;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=FAD-binding dehydrogenase {ECO:0000313|EMBL:PYC71679.1};
GN   ORFNames=C7C46_26720 {ECO:0000313|EMBL:PYC71679.1};
OS   Streptomyces tateyamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC71679.1, ECO:0000313|Proteomes:UP000248039};
RN   [1] {ECO:0000313|EMBL:PYC71679.1, ECO:0000313|Proteomes:UP000248039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC71679.1,
RC   ECO:0000313|Proteomes:UP000248039};
RA   Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT   "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
RL   Submitted (MAR-2018) 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:PYC71679.1}.
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DR   EMBL; PYBW01000110; PYC71679.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V4NK50; -.
DR   OrthoDB; 9813348at2; -.
DR   Proteomes; UP000248039; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248039}.
FT   DOMAIN          6..537
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   556 AA;  59364 MW;  839BA507603A6076 CRC64;
     MAVDADVIVI GAGLAGLVAT AELAEAGRRV ILLDQEPAAS LGGQAHWSFG GLFLVDSPEQ
     RRLRIRDSPE LAWQDWLGTA GFDRPEDRWP RAWAEAYVDF AAGEKRAWLR AQGVRFFPVV
     GWAERGGLLA SGPGNSVPRF HITWGTGPGL VEPFGRRVRA AVAKGLVELR FRHRVTELAA
     TAGVTDTVRG ELLVPSAVRR GAASSREVEG AFELRAQAVL IASGGIGGNH ELVRQAWPAR
     LGTPPAKLLS GVPAHVDGLM QQAAGRAGGH LINGDRMWHY TEGIENWDPI WAMHGIRILP
     GPSSLWLDAR GNRLPVPLFP GFDTLGTLEH IMTTGHDHTW FVLTQKIIEK EFALSGSEQN
     PDLTGRSVRQ VLGRALPGAP GPVEAFKKHG ADFVVADTLT ELVAGMNALT TRDGAGEPLI
     EEAALRREIE ARDREVANPF TKDLQLTAIH GARRYLGDKL IRTAAPHRLL DPKAGPLIAV
     RLNILTRKSL GGLETDLDGR VLRADGSVLA GVYAAGEVAG FGGGGVHGYR SLEGTFLGGC
     LFSGRVAGRA LAAATG
//
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