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Database: UniProt
Entry: C8WI72_EGGLE
LinkDB: C8WI72_EGGLE
Original site: C8WI72_EGGLE 
ID   C8WI72_EGGLE            Unreviewed;       382 AA.
AC   C8WI72;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACV55813.1};
GN   OrderedLocusNames=Elen_1849 {ECO:0000313|EMBL:ACV55813.1};
OS   Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS   KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV55813.1, ECO:0000313|Proteomes:UP000001377};
RN   [1] {ECO:0000313|EMBL:ACV55813.1, ECO:0000313|Proteomes:UP000001377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 /
RC   NCTC 11813 / VPI 0255 / 1899 B {ECO:0000313|Proteomes:UP000001377};
RX   PubMed=21304654; DOI=10.4056/sigs.33592;
RA   Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT   0255).";
RL   Stand. Genomic Sci. 1:174-182(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP001726; ACV55813.1; -; Genomic_DNA.
DR   RefSeq; WP_009304338.1; NC_013204.1.
DR   AlphaFoldDB; C8WI72; -.
DR   STRING; 479437.Elen_1849; -.
DR   PaxDb; 479437-Elen_1849; -.
DR   KEGG; ele:Elen_1849; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_11; -.
DR   OMA; CLEDAWA; -.
DR   OrthoDB; 3176804at2; -.
DR   BioCyc; ELEN479437:G1GFY-1859-MONOMER; -.
DR   Proteomes; UP000001377; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd00567; ACAD; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 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_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; ISOVALERYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
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; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001377}.
FT   DOMAIN          6..98
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          120..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          230..373
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   382 AA;  42883 MW;  53B829D776708B99 CRC64;
     MDFELTDKQR KLVQAFRAFG EETFTPEHVH QWRRDQGLPD EVAKGFVDLY FGLEELEDGD
     GTFSLCSQAL IIEELSRCAG ATLPFQNDLF NLSIVRQFAD EGEFADVLKD YRETGRLLFA
     LAISEPEAGS DAMNMQTYTR TVDEHLILNG RKTYVNNGEY APYIMVAAID RDCEAPGKYP
     PMTFWLLPRD LKGVSAYPIN KIGQSMLPFA TLVFDNVELS PAYRLNGRQE GFRQLFRLLE
     FGRVFTCASS LGMARAAMED AVAHARSRKA FGVQIGRFQQ IEQMLTDMEV SIYNMSSMLY
     RAALAVDNGG PDERLSVALM KRYVPDAATE VASSAMQILG GMGYTEGARV SQLWQDCRGN
     QIAEGTDQIM VYIASPLIME KY
//
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