ID   Y5835_MYCS2             Reviewed;         547 AA.
AC   A0R4H4; I7G8Z6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=KsdD-like steroid dehydrogenase MSMEG_5835;
DE            EC=1.3.99.-;
GN   OrderedLocusNames=MSMEG_5835, MSMEI_5677;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION AS A KETOSTEROID DEHYDROGENASE, AND DISRUPTION PHENOTYPE.
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: Able to catalyze the elimination of the C-1 and C-2 hydrogen
CC       atoms of the A-ring from the polycyclic ring structure of 3-
CC       ketosteroids, but the ketosteroid dehydrogenase activity is low
CC       compared to KsdD in the cholesterol degradation process. The low
CC       activity could be due to different substrate specificity.
CC       {ECO:0000269|PubMed:16000729}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- DISRUPTION PHENOTYPE: Cells accumulate a small amount of 4-androstene-
CC       3,17-dione (AD) and 9alpha-hydroxy-4-androstene-3,17-dione (9OHAD) in
CC       the first 24-48 hours of cholesterol degradation process.
CC       {ECO:0000269|PubMed:16000729}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK72138.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42112.1; -; Genomic_DNA.
DR   RefSeq; WP_011730832.1; NZ_SIJM01000007.1.
DR   RefSeq; YP_890062.1; NC_008596.1.
DR   AlphaFoldDB; A0R4H4; -.
DR   SMR; A0R4H4; -.
DR   STRING; 246196.MSMEI_5677; -.
DR   EnsemblBacteria; ABK72138; ABK72138; MSMEG_5835.
DR   EnsemblBacteria; AFP42112; AFP42112; MSMEI_5677.
DR   GeneID; 66737123; -.
DR   KEGG; msg:MSMEI_5677; -.
DR   KEGG; msm:MSMEG_5835; -.
DR   PATRIC; fig|246196.19.peg.5679; -.
DR   eggNOG; COG3573; Bacteria.
DR   OMA; PEDHWPR; -.
DR   OrthoDB; 153138at2; -.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IMP:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
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   InterPro; IPR014614; UCP036654.
DR   PANTHER; PTHR43260; PTHR43260; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PIRSF; PIRSF036654; UCP036654; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Lipid degradation; Lipid metabolism; Oxidoreductase;
KW   Reference proteome; Steroid metabolism.
FT   CHAIN           1..547
FT                   /note="KsdD-like steroid dehydrogenase MSMEG_5835"
FT                   /id="PRO_0000403954"
FT   BINDING         5..36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   547 AA;  59024 MW;  0F43A352A91799CC CRC64;
     MADADVIVVG AGLAGLVAAC ELVERGHSVI IVDQENAANI GGQAFWSFGG LFFVNSPEQR
     RLGIRDSQEL ALQDWLGTAG FDRPEDHWPR EWAHAYVDFA AGEKRSWLRA RGLQTFPLVG
     WAERGGYDAL GHGNSVPRFH ITWGTGPALV EIFARRIRDS VRVRFAHRHR VDELIVNAGL
     VAGVRGSILE PSNAPRGVAS SRKVVGDFEF RASAVIVASG GIGGNLELVR KNWPARLGRV
     PDQLISGVPA HVDGRMIGIA ESAGAHVINN DRMWHYTEGI TNYDPVWPNH GIRILPGPSS
     LWLDANGDRL PVPLYPGYDT LGTLEHICRS GQDYTWFILN ARIIAKEFAL SGQEQNPDLT
     SRNVRDLLSR VKPGAPAPVQ AFVDHGVDFV SATSLRDLVA GMNDLPDVVP LDYAKVAAEV
     TARDREVANR FTKDGQITAI RAARNYLGDR FTRVVAPHRL TDPKAGPLIA VKLHILTRKT
     LGGLETDLDS RVLKEDGTTF GGLYAAGEAA GFGGGGVHGY RSLEGTFLGG CIFSGRAAGR
     GAAADIA