ID A0A2P8Q8M7_9ACTN Unreviewed; 397 AA.
AC A0A2P8Q8M7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PSM42590.1};
GN ORFNames=C6Y14_15440 {ECO:0000313|EMBL:PSM42590.1};
OS Streptomyces dioscori.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=2109333 {ECO:0000313|EMBL:PSM42590.1, ECO:0000313|Proteomes:UP000240429};
RN [1] {ECO:0000313|EMBL:PSM42590.1, ECO:0000313|Proteomes:UP000240429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A217 {ECO:0000313|EMBL:PSM42590.1,
RC ECO:0000313|Proteomes:UP000240429};
RA Zhikuan W.;
RT "Streptomyces dioscori sp. nov., a novel endophytic actinobacterium
RT isolated from bulbil of Dioscorea bulbifera L.";
RL Submitted (MAR-2018) 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:PSM42590.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PYBJ01000008; PSM42590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8Q8M7; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000240429; 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 GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
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; IPR045008; ACX4-like.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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; 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:UP000240429}.
FT DOMAIN 21..133
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 138..231
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 246..390
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 397 AA; 43363 MW; 00286B8DC32F59A7 CRC64;
MRSSKDDGIV ADFYDFESAL SDEERKILLK TRAFMHDEVK PLVNENWAAG TFPKELITKF
RESGLVGLSY EGYGEHGPAV SHLLTGMMAL EMSRVDASVA TFFGVHTGLA MYSVHAGGSQ
EQRDRWLPGM AAMDTIGAFA LTEPLDGSDV AAGMGTTAER QGDTWVLNGA KRWIGNATFA
DHVVVWARDL ADDQVKGFMV GKGTPGFTTE KIANKISLRI VENADITLTD VRVPEADRLQ
NVESFRDVAE VLRATRSGVA WQALGVMIGA YELALAYATE REQFGRPLAG FQLVQDLLVK
SLGNITACWG MLLQLARLQD SGVFKDQHSS LAKAHVTARM REVVGWAREI FGGNGIVLDY
DVARFFSDAE AIYSFEGTRE MNTLIVGKAV TGESAFV
//
