IPDE2_MYCTU
ID IPDE2_MYCTU Reviewed; 318 AA.
AC I6YCF5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Acyl-CoA dehydrogenase IpdE2 {ECO:0000305};
DE EC=1.3.99.- {ECO:0000269|PubMed:32101684};
DE AltName: Full=5OH-HIP-CoA dehydrogenase beta subunit {ECO:0000305};
GN Name=ipdE2 {ECO:0000303|PubMed:32101684};
GN Synonyms=fadE33 {ECO:0000312|EMBL:CCP46386.1};
GN OrderedLocusNames=Rv3564 {ECO:0000312|EMBL:CCP46386.1};
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; CCP46386.1; -; Genomic_DNA.
DR RefSeq; NP_218081.1; NC_000962.3.
DR RefSeq; WP_003419352.1; NZ_NVQJ01000014.1.
DR AlphaFoldDB; I6YCF5; -.
DR SMR; I6YCF5; -.
DR STRING; 83332.Rv3564; -.
DR PaxDb; I6YCF5; -.
DR DNASU; 888458; -.
DR GeneID; 45427548; -.
DR GeneID; 888458; -.
DR KEGG; mtu:Rv3564; -.
DR PATRIC; fig|83332.111.peg.3969; -.
DR TubercuList; Rv3564; -.
DR eggNOG; COG1960; Bacteria.
DR OMA; DYRTIDN; -.
DR PhylomeDB; I6YCF5; -.
DR UniPathway; UPA01058; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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 1: Evidence at protein level;
KW Cholesterol metabolism; FAD; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism.
FT CHAIN 1..318
FT /note="Acyl-CoA dehydrogenase IpdE2"
FT /id="PRO_0000452317"
FT BINDING 210
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:I6Y3Q0"
FT BINDING 277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:I6Y3Q0"
SQ SEQUENCE 318 AA; 33558 MW; 1C732510B2294D5B CRC64;
MTPPEERQML RETVASLVAK HAGPAAVRAA MASDRGYDES LWRLLCEQVG AAALVIPEEL
GGAGGELADA AIVVQELGRA LVPSPLLGTT LAELALLAAA KPDAQALTEL AQGSAIGALV
LDPDYVVNGD IADIVVAATS GQLTRWTRFS AQPVATMDPT RRLARLQSEE TEPLCPDPGI
ADTAAILLAA EQIGAAERCL QLTVEYAKSR VQFGRPIGSF QALKHRMADL YVTIAAARAV
VADACHAPTP TNAATARLAA SEALSTAAAE GIQLHGGIAI TWEHDMHLYF KRAHGSAQLL
ESPREVLRRL ESEVWESP
