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Database: UniProt
Entry: A0A1V1VYL2_9ACTN
LinkDB: A0A1V1VYL2_9ACTN
Original site: A0A1V1VYL2_9ACTN 
ID   A0A1V1VYL2_9ACTN        Unreviewed;       454 AA.
AC   A0A1V1VYL2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:GAW53265.1};
GN   ORFNames=PD653_0663 {ECO:0000313|EMBL:GAW53265.1};
OS   Nocardioides sp. PD653.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=393303 {ECO:0000313|EMBL:GAW53265.1, ECO:0000313|Proteomes:UP000194147};
RN   [1] {ECO:0000313|Proteomes:UP000194147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD653 {ECO:0000313|Proteomes:UP000194147};
RA   Ito K., Takagi K., Tanaka N., Kanesaki Y., Iwasaki A.;
RT   "Nocardioides sp. PD653 draft genome sequence.";
RL   Submitted (NOV-2016) 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:GAW53265.1}.
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DR   EMBL; BDJG01000008; GAW53265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1VYL2; -.
DR   OrthoDB; 142556at2; -.
DR   Proteomes; UP000194147; 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; 1.
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; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194147}.
FT   DOMAIN          98..207
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          216..305
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          324..451
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   454 AA;  46863 MW;  147B7D3A106B3D0F CRC64;
     MSLTKSLKPG GKHGLSSTET RDPIGYAVAA LSRLAQSDVL DRIGLRKQTE QAVFTATRSG
     FRTITAASRT FAKAGSPARS GVRPAAARAT GVFDLTPTED EQMLVDVVTE FAAEVVRPAA
     AEADETCSAP EAVLKAGLDI GLPILGLPES LGGISEERSA MAGALVAEAL ARGDLGLAVA
     SLAPGSVATA LGLWGTDAQQ QTYLPAFTGS DVPAAAIALT EPTVLFDVLL PATTAERTAD
     GYVLNGVKSA VPLGAAAELF VIGASLDGAP VLFLVESGTA GIDVVADPAM GVRAAGLTKL
     TLTDVAVPAD AVLGATDGST YTECVRLARL AWCALSVGTG QAVLDYVVPY VKEREAFGEP
     VAHRQSVAFM VADIAIELQS MRLLTWKAAA RAAAGKDFAR EVALARRLCA DKGMQIGLDG
     VQLLGGHGFV KEHPVERWYR DLRAIGVMEG AVLV
//
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