ID A0A0A2ML70_9FLAO Unreviewed; 601 AA.
AC A0A0A2ML70;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGO92321.1};
GN ORFNames=Q766_12680 {ECO:0000313|EMBL:KGO92321.1};
OS Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO92321.1, ECO:0000313|Proteomes:UP000030111};
RN [1] {ECO:0000313|EMBL:KGO92321.1, ECO:0000313|Proteomes:UP000030111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO92321.1,
RC ECO:0000313|Proteomes:UP000030111};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO92321.1}.
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DR EMBL; JRLY01000010; KGO92321.1; -; Genomic_DNA.
DR RefSeq; WP_026990124.1; NZ_JRLY01000010.1.
DR AlphaFoldDB; A0A0A2ML70; -.
DR STRING; 1121898.GCA_000422725_01223; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000030111; Unassembled WGS sequence.
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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-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.
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:UP000030111}.
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..418
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 469..572
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 601 AA; 66080 MW; 7DAF8424D1CB3EFC CRC64;
MSDTLEKQLA RGGQFLVKET QSEDVFTPED FSEEQQMMRD SVKEFIDREI WPNKDRFEKK
DYALTEESMR KAGELGFLGV AVPEEYGGLG MGFVSTMLVC DYISGATGSF STAFGAHTGI
GTMPITLYGT EEQKHKYVPK LASGEWFGAY CLTEPGAGSD ANSGKTKAVL SEDGTHYKIT
GQKMWISNAG FCSVFIVFAR IGDDKNITGF IVDNDPSNGI SLGEEEHKLG IRASSTRQVF
FNDTKVPVEN MLSERGNGFK IAMNALNVGR IKLAAACLDA QRRTISNSVK YANERVQFNT
PIANFGAIRA KLAEMAANCY AGESAAYRAA KNIEDRINAR VANGESHQDA ELKGVEEFAI
ECSILKVAVS EDIQNCADEG IQIFGGMGFS EDTPMESAWR DARIARIYEG TNEINRMLSV
GMLVKKAMKG HVDLLGPAMK VAEELMGIPS FDTPDYSELF AEEKEIVGKL KKAFLMVAGS
AVQKYGPALD EHQQLLMAAS DILIEIYMAE SVILRTEKLA KSKGADAVKE QIAMAQLYLY
HAVDLVNTKG KEGIASFSEG DEQRMMLMGL RRFTKYNNMP NVVALRETIA AKIVAENNYP
F
//
