3O1D_MYCS2
ID 3O1D_MYCS2 Reviewed; 569 AA.
AC A0R4S9; I7GFW5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=3-oxosteroid 1-dehydrogenase;
DE EC=1.3.99.4;
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=ksdD; OrderedLocusNames=MSMEG_5941, MSMEI_5781;
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, CATALYTIC ACTIVITY, AND DISRUPTION
RP 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: 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. Is
CC also involved in the formation of 1,4-androstadiene-3,17-dione (ADD)
CC from 4-androstene-3,17-dione (AD) to. {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:0000269|PubMed:16000729};
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:0000269|PubMed:16000729};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- DISRUPTION PHENOTYPE: Cells show an accumulation of 4-androstene-3,17-
CC dione (AD) in the cholesterol degradation process.
CC {ECO:0000269|PubMed:16000729}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. 3-
CC oxosteroid dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; CP000480; ABK75912.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42214.1; -; Genomic_DNA.
DR RefSeq; YP_890167.2; NC_008596.1.
DR AlphaFoldDB; A0R4S9; -.
DR SMR; A0R4S9; -.
DR STRING; 246196.MSMEI_5781; -.
DR PRIDE; A0R4S9; -.
DR EnsemblBacteria; ABK75912; ABK75912; MSMEG_5941.
DR EnsemblBacteria; AFP42214; AFP42214; MSMEI_5781.
DR KEGG; msg:MSMEI_5781; -.
DR KEGG; msm:MSMEG_5941; -.
DR PATRIC; fig|246196.19.peg.5780; -.
DR eggNOG; COG1053; Bacteria.
DR OMA; HNEQMRV; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 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 1: Evidence at protein level;
KW FAD; Flavoprotein; Lipid degradation; Lipid metabolism; Oxidoreductase;
KW Reference proteome; Steroid metabolism.
FT CHAIN 1..569
FT /note="3-oxosteroid 1-dehydrogenase"
FT /id="PRO_0000403951"
FT REGION 127..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 569 AA; 61453 MW; CF3DEDA6936BC517 CRC64;
MFYMTGQEYD VVVVGSGAAG MVAALTAAHQ GLSTVVVEKA PHYGGSTARS GGGVWIPNNE
ILKRDGVKDT PDEARKYLHA IIGDVVPAEK IDTYLDRGPE MLSFVLKHSP LKLCWVPGYS
DYYPETPGGK PTGRSVEPKP FDANKLGPDL KGLEPPYGKV PMNMVVMQQD YVRLNQLKRH
PRGVLRSLKV GIRATWGKVS GKNLVGMGRA LIAPLRIGLR EAGVPVLLNT ALTDLYVEDG
RVLGIYVRDT TAGDDAEPRL IRARHGVILG SGGFEHNEQM RVKYQRAPIT TEWTVGAVAN
TGDGIVAAEK LGAALELMED AWWGPTVPLV GAPWFALSER NSPGSIIVNM SGKRFMNESM
PYVEACHHMY GGQYGQGPGP GENIPAWLIF DQQYRDRYIF AGLQPGQRIP SKWLESGVIV
KADTLVELAE KTGLPADQFT STIERFNGFA RSGVDEDFHR GESAYDRYYG DPTNKPNPNL
GEIKHGPFYA AKMVPGDLGT KGGIRTDVRG RALRDDDSVI EGLYAAGNVS SPVMGHTYPG
PGGTIGPAMT FGYLAALDIA ATAAASRKG
