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Database: UniProt
Entry: A0A0D3LII0_9BACT
LinkDB: A0A0D3LII0_9BACT
Original site: A0A0D3LII0_9BACT 
ID   A0A0D3LII0_9BACT        Unreviewed;       599 AA.
AC   A0A0D3LII0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AHM61537.1};
GN   ORFNames=D770_16415 {ECO:0000313|EMBL:AHM61537.1};
OS   Flammeovirgaceae bacterium 311.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX   NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM61537.1, ECO:0000313|Proteomes:UP000064112};
RN   [1] {ECO:0000313|EMBL:AHM61537.1, ECO:0000313|Proteomes:UP000064112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=311 {ECO:0000313|EMBL:AHM61537.1,
RC   ECO:0000313|Proteomes:UP000064112};
RA   Fang C.;
RT   "Complete bacteria genome obtained just from illumina data.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; CP004371; AHM61537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D3LII0; -.
DR   STRING; 1257021.D770_16415; -.
DR   KEGG; fbt:D770_16415; -.
DR   PATRIC; fig|1257021.3.peg.3724; -.
DR   OrthoDB; 9764422at2; -.
DR   Proteomes; UP000064112; 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; 2.
DR   InterPro; IPR049426; Acyl-CoA-dh-like_C.
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:SF38; ACYL-COA DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF21263; Acyl-CoA-dh_C; 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.
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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064112}.
FT   DOMAIN          32..145
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          149..243
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          256..417
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          468..571
FT                   /note="Acyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21263"
SQ   SEQUENCE   599 AA;  65969 MW;  E7DFBC7AF4D18393 CRC64;
     MEATDKREAT KGGEFLIKET TADQVFIPEE WSEEQRMIAQ TCKDFLETEI YPRLEEIDSM
     KHPELMPNLM DKAGELGLLG TSVPEQYGGF GMDFNTSMLV AEATGPGHSF AVALSAHTGI
     GTLPILYYGN EEQKAKYLPK LATGEYKAAY CLTEPDSGSD ANSGKTKAVL NPEGTHYIIN
     GQKMWITNGG FADIYIVFAK IGDDENLSAF IVERSFGGIT MNEEEKKMGI KGSSTRQIFF
     NDCAVPKENM LSERQNGFKI AVNILNIGRI KLAAAAFGAC KAVTANAVQY ANERKQFGQA
     IANFGAIKHK LAEMAARTYA SESAGYRAGQ NIDDAYESLS AGGMDEAQAK LKSVEEFAIE
     CAILKVHGSE VLDYVVDEGV QIYGGMGFSA DAPMDRAYRD ARINRIFEGT NEINRMLTID
     MIMKRAMKGQ IDLMSAAMAV QKDLTSIPDF GAQEEEGLFV KEKKVLNNLK KAGLMIAGAA
     AQKFMQKLGQ EQEILMNLAD MLIQGYAAES ALLRTEKLAG MRGEEAVQAQ IDMTRIYLHH
     AVETVGKAGR EAIYAFAEGD EQRLMLMGLK RYTKIDPFNL KEARRRVADI MIEKNGYPF
//
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