ID   3O1D_MYCTO              Reviewed;         566 AA.
AC   Q7D5C1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=3-oxosteroid 1-dehydrogenase;
DE            EC=1.3.99.4 {ECO:0000250|UniProtKB:P71864};
DE   AltName: Full=3-keto-Delta(4)-steroid Delta(1)-dehydrogenase;
DE            Short=KSDD;
DE   AltName: Full=3-oxo-Delta(4)-steroid 1-dehydrogenase;
DE            Short=KSTD;
GN   Name=kstD; OrderedLocusNames=MT3641;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   FUNCTION.
RX   PubMed=16000729; DOI=10.1099/mic.0.27953-0;
RA   Brzostek A., Sliwinski T., Rumijowska-Galewicz A., Korycka-Machala M.,
RA   Dziadek J.;
RT   "Identification and targeted disruption of the gene encoding the main 3-
RT   ketosteroid dehydrogenase in Mycobacterium smegmatis.";
RL   Microbiology 151:2393-2402(2005).
CC   -!- FUNCTION: Involved in the degradation of cholesterol (PubMed:16000729).
CC       Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-
CC       ring from the polycyclic ring structure of 3-ketosteroids (By
CC       similarity). Is also involved in the formation of 3-keto-1,4-diene-
CC       steroid from 3-keto-4-ene-steroid (By similarity).
CC       {ECO:0000250|UniProtKB:P71864, ECO:0000269|PubMed:16000729}.
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:0000250|UniProtKB:P71864};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + a 3-oxo-Delta(4)-steroid = a 3-oxo-Delta(1,4)-steroid +
CC         AH2; Xref=Rhea:RHEA:53132, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:47909, ChEBI:CHEBI:77166;
CC         Evidence={ECO:0000250|UniProtKB:P71864};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. 3-
CC       oxosteroid dehydrogenase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK48000.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7D5C1; -.
DR   SMR; Q7D5C1; -.
DR   EnsemblBacteria; AAK48000; AAK48000; MT3641.
DR   KEGG; mtc:MT3641; -.
DR   HOGENOM; CLU_011398_4_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0047571; F:3-oxosteroid 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic 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.
DR   SUPFAM; SSF56425; SSF56425; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Lipid degradation; Lipid metabolism; Oxidoreductase;
KW   Steroid metabolism.
FT   CHAIN           1..566
FT                   /note="3-oxosteroid 1-dehydrogenase"
FT                   /id="PRO_0000403953"
FT   BINDING         10..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   566 AA;  61078 MW;  3F21B3B5547F3204 CRC64;
     MFYMTVQEFD VVVVGSGAAG MVAALVAAHR GLSTVVVEKA PHYGGSTARS GGGVWIPNNE
     VLKRRGVRDT PEAARTYLHG IVGEIVEPER IDAYLDRGPE MLSFVLKHTP LKMCWVPGYS
     DYYPEAPGGR PGGRSIEPKP FNARKLGADM AGLEPAYGKV PLNVVVMQQD YVRLNQLKRH
     PRGVLRSMKV GARTMWAKAT GKNLVGMGRA LIGPLRIGLQ RAGVPVELNT AFTDLFVENG
     VVSGVYVRDS HEAESAEPQL IRARRGVILA CGGFEHNEQM RIKYQRAPIT TEWTVGASAN
     TGDGILAAEK LGAALDLMDD AWWGPTVPLV GKPWFALSER NSPGSIIVNM SGKRFMNESM
     PYVEACHHMY GGEHGQGPGP GENIPAWLVF DQRYRDRYIF AGLQPGQRIP SRWLDSGVIV
     QADTLAELAG KAGLPADELT ATVQRFNAFA RSGVDEDYHR GESAYDRYYG DPSNKPNPNL
     GEVGHPPYYG AKMVPGDLGT KGGIRTDVNG RALRDDGSII DGLYAAGNVS APVMGHTYPG
     PGGTIGPAMT FGYLAALHIA DQAGKR