3O1D_RHOOP
ID 3O1D_RHOOP Reviewed; 507 AA.
AC Q04616;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=3-oxosteroid 1-dehydrogenase;
DE EC=1.3.99.4 {ECO:0000269|PubMed:7916596};
DE AltName: Full=Steroid 1:2-dehydrogenase {ECO:0000303|PubMed:7916596};
OS Rhodococcus opacus (Nocardia opaca).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=37919;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IMET 7030;
RA Drobnic K.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, PROTEIN SEQUENCE OF 2-15,
RP FUNCTION AS A KETOSTEROID DEHYDROGENASE, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=7916596; DOI=10.1006/bbrc.1993.1077;
RA Drobnic K., Krizaj I., Gubensek F., Komel R.;
RT "Improved purification of steroid 1:2-dehydrogenase from Nocardia opaca and
RT partial characterization of its cloned gene sequence.";
RL Biochem. Biophys. Res. Commun. 190:509-515(1993).
CC -!- FUNCTION: Catalyzes the elimination of the C-1 and C-2 hydrogen atoms
CC of the A-ring from the polycyclic ring structure of 3-ketosteroids.
CC {ECO:0000269|PubMed:7916596}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 3-oxosteroid = a 3-oxo-Delta(1)-steroid + AH2;
CC Xref=Rhea:RHEA:13329, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:20156, ChEBI:CHEBI:47788; EC=1.3.99.4;
CC Evidence={ECO:0000269|PubMed:7916596};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; steroid degradation.
CC {ECO:0000305|PubMed:7916596}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: By steroids. {ECO:0000269|PubMed:7916596}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. 3-
CC oxosteroid dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; U59422; AAB02831.1; -; Genomic_DNA.
DR PIR; PC1242; PC1242.
DR AlphaFoldDB; Q04616; -.
DR SMR; Q04616; -.
DR UniPathway; UPA00722; -.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0047571; F:3-oxosteroid 1-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006706; P:steroid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; FAD; Flavoprotein;
KW Lipid metabolism; Membrane; Oxidoreductase; Steroid metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7916596"
FT CHAIN 2..507
FT /note="3-oxosteroid 1-dehydrogenase"
FT /id="PRO_0000064377"
FT REGION 299..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 54005 MW; 067F865E9E7ED984 CRC64;
MQDWTSECDL LVVGSGGGAL TGAYTAAAQG LTTIVLEKTD RFGGTSAYSG ASIWLPGTQV
QERAGLPDST ENARSYLRAL LGDAESERQD AYVETAPAVV ALLEQNPNIE FEFRAFPDYY
KAEGRMDTGR SINPLDLDPA DIGDLAGRCV RNCTKTDRMD HAPGRMIGGR ALIAVSAAVQ
STARQNFAPE SVLTSLIVED GRVVGGLRSN PRYRQRIKAN RGVLMHAGGG FEGNAEMREQ
AGTPGKAIWS MGPSGPTPAT RSPPELAGRR RNSLARSGVV LPRGRAARRR RLHGRVRGGL
VVDSPGSVPQ RVASVRPVRT SHGCSPDDNG SAVPSFMIFD SREVTDCPPS ASRTRPPPST
SKPEPGSVPT LSKNSLPRPD YRPERIAQHC RKVQRCRKLG VDEEFHRGED PYDAFFCPPN
GGANAALTAI ENGPFYAARD RLSDLGTKGG LVTDVNGRVL RADGSAIDGL YAAGNTSASV
APFYPGPGVP LGTAMVFSYR AAQDMAK
