ID A0A164SYJ1_9NOCA Unreviewed; 407 AA.
AC A0A164SYJ1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KZF12880.1};
GN ORFNames=A2J03_16755 {ECO:0000313|EMBL:KZF12880.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF12880.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF12880.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF12880.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-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|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:KZF12880.1}.
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DR EMBL; LVCV01000037; KZF12880.1; -; Genomic_DNA.
DR RefSeq; WP_068368833.1; NZ_LVCV01000037.1.
DR AlphaFoldDB; A0A164SYJ1; -.
DR OrthoDB; 2769798at2; -.
DR Proteomes; UP000077673; 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 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; 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 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:UP000077673}.
FT DOMAIN 136..231
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 248..399
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 55..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 43629 MW; 61FD7E86FDA49845 CRC64;
MINLELPKKL RAQANQAHQV AAEIFRPISR KYDLAEHEYP VELDTMASMV EGMSDAGTEV
GGAAGGREKD SENAKKPSKT ANANGGNMAA LVNVIETCWG DVGLTLSIPY QGLGNSAIAA
VSTDEQLERF GKVWASMAIT EPSFGSDSAA VTTTAVLDGD EWVLNGEKIY VTAGERSTHI
VVWASVDKSK GRAAIKSFVV PRDAPGLSVA RLEHKLGIKA SDTAALLLED CRIPKDNLLG
SAEVNTEKGF AGVMQTFDNT RPLVAGMAIG VARAALEELR SILVEAGVEI SYTTPAYNQH
AAAAEFLRLE ADWEAAHLLA LRAAWMADNK EPNSLQASMA KAKAGRSATD ITLKAVELAG
SYGYSERLLL EKWSRDSKIL DIFEGTQQIQ QLIVARRVLG KTSAELK
//
