ID   IPDE1_MYCS2             Reviewed;         392 AA.
AC   A0R4Z9;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Acyl-CoA dehydrogenase IpdE1 {ECO:0000305};
DE            EC=1.3.99.- {ECO:0000250|UniProtKB:I6Y3V5};
DE   AltName: Full=5OH-HIP-CoA dehydrogenase alpha subunit {ECO:0000305};
GN   Name=ipdE1 {ECO:0000303|PubMed:32101684};
GN   OrderedLocusNames=MSMEG_6012 {ECO:0000312|EMBL:ABK71994.1};
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:I6Y3V5}.
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:I6Y3V5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66349;
CC         Evidence={ECO:0000250|UniProtKB:I6Y3V5};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:I6Y3V5};
CC       Note=Binds 2 FAD per heterotetramer. {ECO:0000250|UniProtKB:I6Y3V5};
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:I6Y3V5}.
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; ABK71994.1; -; Genomic_DNA.
DR   RefSeq; WP_003897413.1; NZ_SIJM01000017.1.
DR   RefSeq; YP_890237.1; NC_008596.1.
DR   AlphaFoldDB; A0R4Z9; -.
DR   SMR; A0R4Z9; -.
DR   STRING; 246196.MSMEI_5852; -.
DR   EnsemblBacteria; ABK71994; ABK71994; MSMEG_6012.
DR   GeneID; 66737297; -.
DR   KEGG; msm:MSMEG_6012; -.
DR   PATRIC; fig|246196.19.peg.5848; -.
DR   eggNOG; COG1960; Bacteria.
DR   OMA; NWHRDLG; -.
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   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
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; PF02770; Acyl-CoA_dh_M; 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..392
FT                   /note="Acyl-CoA dehydrogenase IpdE1"
FT                   /id="PRO_0000452316"
FT   ACT_SITE        254
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:I6YCA3"
FT   BINDING         126..129
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:I6YCA3"
FT   BINDING         171
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:I6YCA3"
FT   BINDING         371..373
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:I6YCA3"
SQ   SEQUENCE   392 AA;  43608 MW;  CB3A15C34D21BA87 CRC64;
     MIEVQEFRAE VRQWLADNLV GDFAALKGLG GPGREHEAFE ERRAWNQHLA AAGLTCLGWP
     VEHGGRGLSV AHRVAFYEEY ARANAPDKVN HFGEELLGPT LIEYGTPEQQ KRFLPKILDV
     TELWCQGYSE PNAGSDLANV STTAELVGDA EASGATGNQY WVINGQKVWT SLAHWAQWCF
     VVARTEKGSK RHAGLSYLLV PLDQPGVEIR PINQLTGDSE FNEVFFDDAR TEAGLVVGQP
     GDGWRVAMGT LTFERGVSTL GQQIRYAREH SNLVELAKRT GAADDPLIRE RLVQSWTGLQ
     AMRSYALATM DVEQPGQDNV SKLLWANWHR ELGEIAMDVQ GMAGLTLENG EFDEWQRLYL
     FSRADTIYGG SNEIQRNIIA ERVLGLPREV KG