ID A0A1Y6G8P1_9BACI Unreviewed; 412 AA.
AC A0A1Y6G8P1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SMQ86690.1};
GN ORFNames=SAMN05444673_6690 {ECO:0000313|EMBL:SMQ86690.1};
OS Bacillus sp. OV166.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ86690.1, ECO:0000313|Proteomes:UP000194454};
RN [1] {ECO:0000313|EMBL:SMQ86690.1, ECO:0000313|Proteomes:UP000194454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV166 {ECO:0000313|EMBL:SMQ86690.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXWM01000002; SMQ86690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6G8P1; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000194454; Unassembled WGS sequence.
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; 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.
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}.
FT DOMAIN 27..134
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 137..231
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 260..398
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 412 AA; 44942 MW; 1182522BF6CDEE1B CRC64;
MSVSSTAVVN DGIMRIPGWW SCPPGYEHLQ EKAHEIGKNY LLERSFIADR ESQYPHESML
KIAESGFGAV TVPVEYGGLG TGLTGFAVLA ESIAQYCASS AMCWVMHTAA VQTLFASGNE
EQRRRFIPEV IKGKVGALAF SEPATGSHFW NVVSTAPRHG DGYLLNADKS FVTSAGAADW
YIVCTSSPES PLEDKLTFLL VEDGQDGITQ YPFSAMGLRG NSSGPMKFRD VFVPKENLLG
TEGGMAYYND NVIDPLFLLG TAAVWTGIAQ GAINEAIDGA KKKVHADTGK SVASYQVIRH
ELAKAQILVD SSRSMLYRVA ENFDRAVKNG IPLQDVLLPV WELKTYAADM VIQVTNQALQ
VAGGRGYLTG RIEKYLRDGR AGAVMGPTNE ILREWIGLSL LQSPWYNQDI KK
//
