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Database: UniProt
Entry: C8WI82_EGGLE
LinkDB: C8WI82_EGGLE
Original site: C8WI82_EGGLE 
ID   C8WI82_EGGLE            Unreviewed;       379 AA.
AC   C8WI82;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACV55823.1};
GN   OrderedLocusNames=Elen_1859 {ECO:0000313|EMBL:ACV55823.1};
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:ACV55823.1, ECO:0000313|Proteomes:UP000001377};
RN   [1] {ECO:0000313|EMBL:ACV55823.1, 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; ACV55823.1; -; Genomic_DNA.
DR   RefSeq; WP_015760814.1; NC_013204.1.
DR   AlphaFoldDB; C8WI82; -.
DR   STRING; 479437.Elen_1859; -.
DR   PaxDb; 479437-Elen_1859; -.
DR   KEGG; ele:Elen_1859; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_1_11; -.
DR   OrthoDB; 8876745at2; -.
DR   BioCyc; ELEN479437:G1GFY-1869-MONOMER; -.
DR   Proteomes; UP000001377; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001377}.
FT   DOMAIN          5..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          120..214
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          226..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  40763 MW;  0F7DF1BB0C20F7E4 CRC64;
     MYELTQEERM ILSMVDDLCV DVVAERAAAI DEEDEFPQDI YELFVEQGLF ALAYGEEHGG
     VEVSMHCWVQ VIERIARESP AVALMILISA IGSDALVFSG SAEQQRAILP ALAAGEAKIC
     FALTEPNAGS DISAISTTAL PDGDGYTING GKIFITNGAV GDWFTVFARV VEDGQSKPSC
     FIVHRYTPGL VIGRKEDKMG LRGSVTSQLY FENMHVGPEA VVGEVGDGFA IAHHTLNRGR
     LAVAALATGV TAASLAAAAA YAKERIQFGK HIADLQAIRF MLADMEITLE ASRLLLDQAA
     SAFGGDIQTM MKTASVAKVY CSEAAVKAAE TAVQIFGGYG LCKDYPVERY YRDAKSFTIV
     EGTSQVQRSL IAKSVLKEY
//
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