IPDE1_MYCTU
ID IPDE1_MYCTU Reviewed; 385 AA.
AC I6Y3V5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Acyl-CoA dehydrogenase IpdE1 {ECO:0000305};
DE EC=1.3.99.- {ECO:0000269|PubMed:32101684};
DE AltName: Full=5OH-HIP-CoA dehydrogenase alpha subunit {ECO:0000305};
GN Name=ipdE1 {ECO:0000303|PubMed:32101684};
GN Synonyms=fadE30 {ECO:0000312|EMBL:CCP46382.1};
GN OrderedLocusNames=Rv3560c {ECO:0000312|EMBL:CCP46382.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBUNIT.
RC STRAIN=H37Rv;
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 (PubMed:32101684). Can
CC also use octanoyl-CoA and dihydroferuloyl-CoA, with lower efficiency.
CC Cannot use 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA)
CC (PubMed:32101684). {ECO:0000269|PubMed:32101684}.
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:0000269|PubMed:32101684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66349;
CC Evidence={ECO:0000269|PubMed:32101684};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:32101684};
CC Note=Binds 2 FAD per heterotetramer. {ECO:0000269|PubMed:32101684};
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:0000269|PubMed:32101684}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46382.1; -; Genomic_DNA.
DR RefSeq; NP_218077.1; NC_000962.3.
DR RefSeq; WP_003419340.1; NZ_NVQJ01000014.1.
DR AlphaFoldDB; I6Y3V5; -.
DR SMR; I6Y3V5; -.
DR STRING; 83332.Rv3560c; -.
DR PaxDb; I6Y3V5; -.
DR PRIDE; I6Y3V5; -.
DR GeneID; 887838; -.
DR KEGG; mtu:Rv3560c; -.
DR PATRIC; fig|83332.111.peg.3965; -.
DR TubercuList; Rv3560c; -.
DR eggNOG; COG1960; Bacteria.
DR OMA; NWHRDLG; -.
DR PhylomeDB; I6Y3V5; -.
DR BioCyc; MetaCyc:G185E-7837-MON; -.
DR UniPathway; UPA01058; -.
DR Proteomes; UP000001584; 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 1: Evidence at protein level;
KW Cholesterol metabolism; FAD; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism.
FT CHAIN 1..385
FT /note="Acyl-CoA dehydrogenase IpdE1"
FT /id="PRO_0000452315"
FT ACT_SITE 244
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 161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:I6YCA3"
FT BINDING 364..366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:I6YCA3"
SQ SEQUENCE 385 AA; 42732 MW; 321B503B13EF41C1 CRC64;
MQDVEEFRAQ VRGWLADNLA GEFAALKGLG GPGREHEAFE ERRAWNQRLA AAGLTCLGWP
EEHGGRGLST AHRVAFYEEY ARADAPDKVN HFGEELLGPT LIAFGTPQQQ RRFLPRIRDV
TELWCQGYSE PGAGSDLASV ATTAELDGDQ WVINGQKVWT SLAHLSQWCF VLARTEKGSQ
RHAGLSYLLV PLDQPGVQIR PIVQITGTAE FNEVFFDDAR TDADLVVGAP GDGWRVAMAT
LTFERGVSTL GQQIVYAREL SNLVELARRT AAADDPLIRE RLTRAWTGLR AMRSYALATM
EGPAVEQPGQ DNVSKLLWAN WHRNLGELAM DVIGKPGMTM PDGEFDEWQR LYLFTRADTI
YGGSNEIQRN IIAERVLGLP REAKG
