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Database: UniProt
Entry: A0A0L0BJF2_9MICC
LinkDB: A0A0L0BJF2_9MICC
Original site: A0A0L0BJF2_9MICC 
ID   A0A0L0BJF2_9MICC        Unreviewed;       387 AA.
AC   A0A0L0BJF2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KNC19359.1};
GN   ORFNames=AC792_07230 {ECO:0000313|EMBL:KNC19359.1};
OS   Arthrobacter sp. RIT-PI-e.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC19359.1, ECO:0000313|Proteomes:UP000053253};
RN   [1] {ECO:0000313|Proteomes:UP000053253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253};
RA   Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) 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:KNC19359.1}.
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DR   EMBL; LGIU01000051; KNC19359.1; -; Genomic_DNA.
DR   RefSeq; WP_049829875.1; NZ_LGIU01000051.1.
DR   AlphaFoldDB; A0A0L0BJF2; -.
DR   STRING; 1681197.AC792_07230; -.
DR   PATRIC; fig|1681197.3.peg.2958; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000053253; 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; 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.
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:UP000053253}.
FT   DOMAIN          21..120
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          128..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          240..380
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   387 AA;  41912 MW;  9F16405FEDC62AE5 CRC64;
     MESQLPTADF LGVESLLAPH EQEKLQDVRD FLAKEVAPRA TEWWDRAEFP HEILPKLAEL
     GLSTPVAQGY SHLFSGLLIA ELTRADTSIA TFFMVHHDLF VEALHTFGSA EQKARLLQDA
     TDLRITGAFA LTEPQHGSDV AGRMDTTAVR DGDTWVVNGA KRWIGNGTFC DRLVLWAQEP
     ATGAVRGFLL DATLPGVTRT PIRNKTALRT VQNADIALTG VRIPEADRLA GIGSFEDTRQ
     LLLGSRILVG WQAVGQQLAA FDVARQYAVE RHQFGRPVAG FQLIQDQLVT LLGNTVSSMA
     VMARISALQE QGAADMAQAA FAKSFTTGRM RESVALGCGI LGGNGILTDH GMAKIFADAE
     AVYTYEGTYE INSLIVGRAL TGISAFT
//
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