ID   IPDE2_MYCS2             Reviewed;         311 AA.
AC   A0R502;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Acyl-CoA dehydrogenase IpdE2 {ECO:0000305};
DE            EC=1.3.99.- {ECO:0000250|UniProtKB:I6YCF5};
DE   AltName: Full=5OH-HIP-CoA dehydrogenase beta subunit {ECO:0000305};
GN   Name=ipdE2 {ECO:0000303|PubMed:32101684};
GN   OrderedLocusNames=MSMEG_6016 {ECO:0000312|EMBL:ABK70325.1};
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   PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=32101684; DOI=10.1021/acs.biochem.0c00005;
RA   Gadbery J.E., Round J.W., Yuan T., Wipperman M.F., Story K.T., Crowe A.M.,
RA   Casabon I., Liu J., Yang X., Eltis L.D., Sampson N.S.;
RT   "IpdE1-IpdE2 is a heterotetrameric acyl coenzyme A dehydrogenase that is
RT   widely distributed in steroid-degrading bacteria.";
RL   Biochemistry 59:1113-1123(2020).
CC   -!- FUNCTION: Involved in cholesterol degradation. Catalyzes the
CC       dehydrogenation of 5OH-HIP-CoA to 5OH-HIPE-CoA.
CC       {ECO:0000250|UniProtKB:I6YCF5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-[(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-
CC         inden-4-yl]propanoyl-CoA + A = (2E)-3-[(3aS,4S,5R,7aS)-5-hydroxy-7a-
CC         methyl-1-oxo-octahydro-1H-inden-4-yl]prop-2-enoyl-CoA + AH2;
CC         Xref=Rhea:RHEA:66348, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:83738, ChEBI:CHEBI:167059;
CC         Evidence={ECO:0000250|UniProtKB:I6YCF5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66349;
CC         Evidence={ECO:0000250|UniProtKB:I6YCF5};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:I6YCF5};
CC       Note=Binds 2 FAD per heterotetramer. {ECO:0000250|UniProtKB:I6YCF5};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000269|PubMed:32101684}.
CC   -!- SUBUNIT: Heterotetramer composed of 2 IpdE1 subunits and 2 IpdE2
CC       subunits. {ECO:0000250|UniProtKB:I6YCF5}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant grows normally on glycerol but
CC       shows impaired growth on cholesterol. It accumulates 5OH-HIP in the
CC       culture supernatant. {ECO:0000269|PubMed:32101684}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK70325.1; -; Genomic_DNA.
DR   RefSeq; WP_011730975.1; NZ_SIJM01000017.1.
DR   RefSeq; YP_890240.1; NC_008596.1.
DR   AlphaFoldDB; A0R502; -.
DR   SMR; A0R502; -.
DR   STRING; 246196.MSMEI_5856; -.
DR   EnsemblBacteria; ABK70325; ABK70325; MSMEG_6016.
DR   GeneID; 66737301; -.
DR   KEGG; msm:MSMEG_6016; -.
DR   PATRIC; fig|246196.19.peg.5853; -.
DR   eggNOG; COG1960; Bacteria.
DR   OMA; DYRTIDN; -.
DR   OrthoDB; 760677at2; -.
DR   UniPathway; UPA01058; -.
DR   Proteomes; UP000000757; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
KW   Cholesterol metabolism; FAD; Flavoprotein; Lipid metabolism;
KW   Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism.
FT   CHAIN           1..311
FT                   /note="Acyl-CoA dehydrogenase IpdE2"
FT                   /id="PRO_0000452318"
FT   BINDING         206
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y3Q0"
FT   BINDING         273
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y3Q0"
SQ   SEQUENCE   311 AA;  33149 MW;  90605A3DC3AAFE6E CRC64;
     MSEERELLRE TVAALVEKHA SPEAVRAAME SELGYDPNLW RLLCEQVGAA ALVIPEEFGG
     AGGELADAAV VLEELGKALV PTPLLGTTLA EIALLSVGRT EPLEELAEGA KIGTVVFNPE
     FVINGDIADI MIAADGETLT QWDTFTAQPK PTMDMTRRLA SVIPGATTTL GDDQGLADTA
     ALLMAAEQIG AASRCLDLTV AYSKDRVQFG RPIGSFQALK HRMADLYVKV ASARAVVHDS
     IATPSSTSAA LARYFASEAL SAVTSEAVQI HGGIAITWEH DIQLYFKRAH GSAQLLGPPR
     EQLRRLEAEV F