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Database: UniProt
Entry: A0A0J0UWJ1_9ACTN
LinkDB: A0A0J0UWJ1_9ACTN
Original site: A0A0J0UWJ1_9ACTN 
ID   A0A0J0UWJ1_9ACTN        Unreviewed;       410 AA.
AC   A0A0J0UWJ1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KLR61222.1};
GN   ORFNames=IMCC26207_10861 {ECO:0000313|EMBL:KLR61222.1};
OS   Actinobacteria bacterium IMCC26207.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1641811 {ECO:0000313|EMBL:KLR61222.1, ECO:0000313|Proteomes:UP000036180};
RN   [1] {ECO:0000313|EMBL:KLR61222.1, ECO:0000313|Proteomes:UP000036180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC26207 {ECO:0000313|EMBL:KLR61222.1,
RC   ECO:0000313|Proteomes:UP000036180};
RA   Kim S., Cho J.-C.;
RT   "Genome sequence of freshwater Actinobacteria.";
RL   Submitted (MAY-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:KLR61222.1}.
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DR   EMBL; LCZK01000008; KLR61222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J0UWJ1; -.
DR   STRING; 1641811.IMCC26207_10861; -.
DR   PATRIC; fig|1641811.3.peg.1370; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000036180; 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; PS00072; ACYL_COA_DH_1; 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:UP000036180}.
FT   DOMAIN          9..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..224
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          257..404
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   410 AA;  44494 MW;  7D5C80EC0B9D6D33 CRC64;
     MSEFSMTLNE DQLQIQKWVH DFAENVVRPA AEEWDEREEF PWPIVQQAAD IGLYGFEFIS
     QAMLGDPTGL TMPVALEELF WGDAGIGLAI FGSSLAAAGI AGNGTMEQTL EWVPQCYGTP
     EKIALGAFCV SEPDAGSDVS SLRTRAVYDE AKDEWTLNGT KAWITNGGIA DVHVVVATVD
     PALKGRGQAS FIVGPGTPGL SMGQKYKKHG IRASHTSEVV LDDVKIPGAN LLGGKEKLDE
     KIARAHEALK NPSIRSGKQP AMATFEATRP AVGAQAVGVA RAAYEYALQY AQERTAFGKP
     IIMNQSIAFM LADMATQIEA ARLMVYRAAW LSGNGGGFVN AEGSMSKLMA GRTAVWVTER
     AIQILGGYGY TREYPVERWH RDAKIFDIFE GTEQIQQLVI SRAISGLRIE
//
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