ID   A9QAE5_RHOER            Unreviewed;       574 AA.
AC   A9QAE5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=3-ketosteroid-delta1-dehydrogenase {ECO:0000313|EMBL:ABW74859.1};
GN   Name=kstD3 {ECO:0000313|EMBL:ABW74859.1};
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833 {ECO:0000313|EMBL:ABW74859.1};
RN   [1] {ECO:0000313|EMBL:ABW74859.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SQ1 {ECO:0000313|EMBL:ABW74859.1};
RX   PubMed=18031290; DOI=10.1042/BJ20071130;
RA   Knol J., Bodewits K., Hessels G.I., Dijkhuizen L., van der Geize R.;
RT   "3-Keto-5alpha-steroid Delta(1)-dehydrogenase from Rhodococcus erythropolis
RT   SQ1 and its orthologue in Mycobacterium tuberculosis H37Rv are highly
RT   specific enzymes that function in cholesterol catabolism.";
RL   Biochem. J. 410:339-346(2008).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; EU014895; ABW74859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9QAE5; -.
DR   SMR; A9QAE5; -.
DR   BRENDA; 1.3.99.4; 5389.
DR   SABIO-RK; A9QAE5; -.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          7..535
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   574 AA;  61246 MW;  B0F0FCDD567D58B2 CRC64;
     MSKQEYDIVV VGSGAAGMTA ALTAAHQGLS VVIVEKAAHY GGSTARSGGG VWIPNNEALQ
     ADGVTDTPEA ARSYLHSIIG DVVAPERIDT YLERGPEMLS FVLKNSPLEL QWVPGYSDYY
     PEAPGGRLGG RSVEPTPFDG NKLGADRKNL EPDYVKAPKN FVITQADYKW LNLLMRNPRG
     PLRAMKVGMR FLAAKATKKD LLVRGQALVA GIRLGLQSAG VPILLNTPLT SLYTEDGAVR
     GVNVLIDGEE QVIRARHGVV LGSGGFEHNK EMREKYQRAP IGTEWTVGAK ANTGDGIRAG
     QEVGAAVDFM DDAWWGPSIP LTGGPWFALS ERTLPGCMMV NMSGKRFGNE AAPYVEATHA
     MYGGEYGQGE GAGENIPTWM ILDQRYRNRY TFAGITPRSP FPGRWLKAGI VVKAGTIAEL
     AEKTGLPVAS LTETVDRFNG FARNGKDEDF GRGDSGYDAY YGDPRLKNPS LAEISKAPFY
     AIKMVPGDLG TKGGICTDVN GRALREDGSV IDGLYAAGNA SAPVMGHTYA GPGATIGPAM
     TFGYLAVLDI VERAKKAEST EAPAAEKTAV DHAN
//