ID   YDIO_ECOL6              Reviewed;         383 AA.
AC   P0A9U9; P76200; P76897; Q8X5X5;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable acyl-CoA dehydrogenase YdiO;
DE            EC=1.3.-.-;
GN   Name=ydiO; OrderedLocusNames=c2090;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC         Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80550.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN80550.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000347850.1; NC_004431.1.
DR   AlphaFoldDB; P0A9U9; -.
DR   SMR; P0A9U9; -.
DR   STRING; 199310.c2090; -.
DR   EnsemblBacteria; AAN80550; AAN80550; c2090.
DR   GeneID; 67415599; -.
DR   KEGG; ecc:c2090; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   OMA; LYREAPM; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..383
FT                   /note="Probable acyl-CoA dehydrogenase YdiO"
FT                   /id="PRO_0000201208"
SQ   SEQUENCE   383 AA;  43002 MW;  2391FD85D17C7003 CRC64;
     MDFSLTEEQE LLLASIRELI TTNFPEEYFR TCDQNGTYPR EFMRALADNG ISMLGVPEEF
     GGIPADYVTQ MLALMEVSKC GAPAFLITNG QCIHSMRRFG SAEQLRKTAE STLETGDPAY
     ALALTEPGAG SDNNSATTTY TRKNGKVYIN GQKTFITGAK EYPYMLVLAR DPQPKDPKKA
     FTLWWVDSSK PGIKINPLHK IGWHMLSTCE VYLDNVEVEE SDMVGEEGMG FLNVMYNFEM
     ERLINAARST GFAECAFEDA ARYANQRIAF GKPIGHNQMI QEKLALMAIK IDNMRNMVLK
     VAWQADQHQS LRTSAALAKL YCARTAMEVI DDAIQIMGGL GYTDEARVSR FWRDVRCERI
     GGGTDEIMIY VAGRQILKDY QNK