ID   YDIO_ECOLI              Reviewed;         383 AA.
AC   P0A9U8; 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 115.
DE   RecName: Full=Probable acyl-CoA dehydrogenase YdiO;
DE            EC=1.3.-.-;
GN   Name=ydiO; OrderedLocusNames=b1695, JW5275;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-117.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
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}.
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DR   EMBL; U00096; AAC74765.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15464.2; -; Genomic_DNA.
DR   PIR; G64927; G64927.
DR   RefSeq; NP_416210.4; NC_000913.3.
DR   RefSeq; WP_000347850.1; NZ_STEB01000003.1.
DR   AlphaFoldDB; P0A9U8; -.
DR   SMR; P0A9U8; -.
DR   BioGRID; 4260291; 263.
DR   STRING; 511145.b1695; -.
DR   PaxDb; P0A9U8; -.
DR   PRIDE; P0A9U8; -.
DR   EnsemblBacteria; AAC74765; AAC74765; b1695.
DR   EnsemblBacteria; BAA15464; BAA15464; BAA15464.
DR   GeneID; 67415599; -.
DR   GeneID; 945626; -.
DR   KEGG; ecj:JW5275; -.
DR   KEGG; eco:b1695; -.
DR   PATRIC; fig|1411691.4.peg.563; -.
DR   EchoBASE; EB3731; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   InParanoid; P0A9U8; -.
DR   OMA; LYREAPM; -.
DR   PhylomeDB; P0A9U8; -.
DR   BioCyc; EcoCyc:G6918-MON; -.
DR   PRO; PR:P0A9U8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0071271; P:1-butanol biosynthetic process; IMP:CACAO.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..383
FT                   /note="Probable acyl-CoA dehydrogenase YdiO"
FT                   /id="PRO_0000201206"
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