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
//