ID A0A0A0JQR5_9MICO Unreviewed; 408 AA.
AC A0A0A0JQR5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGN39825.1};
GN ORFNames=N801_18855 {ECO:0000313|EMBL:KGN39825.1};
OS Knoellia aerolata DSM 18566.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385519 {ECO:0000313|EMBL:KGN39825.1, ECO:0000313|Proteomes:UP000030013};
RN [1] {ECO:0000313|EMBL:KGN39825.1, ECO:0000313|Proteomes:UP000030013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18566 {ECO:0000313|EMBL:KGN39825.1,
RC ECO:0000313|Proteomes:UP000030013};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia aerolata.";
RL Submitted (AUG-2013) 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:KGN39825.1}.
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DR EMBL; AVPL01000069; KGN39825.1; -; Genomic_DNA.
DR RefSeq; WP_035940291.1; NZ_AVPL01000069.1.
DR AlphaFoldDB; A0A0A0JQR5; -.
DR STRING; 1385519.N801_18855; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 2769798at2; -.
DR Proteomes; UP000030013; 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:UP000030013}.
FT DOMAIN 137..232
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 249..400
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 408 AA; 43375 MW; 8A4055A2BF0F949E CRC64;
MIDLEVPRKF LPLVERARGV AEEVFRPISR TYDRAEHEYP RELDLLSAVI DGMSSSGAGQ
GAGASSVVAA VGSGERHPAA PTVRNGSNLS SVLSILETCR GDVGLTLSIP RQGLGNAAIA
AVATDEQKAR YAGRWAAMAI TEPETGSDSG AIRTTAVKDG DEYVLNGEKI YVTSGERADL
VVVWATLDRS LGKRAIRSFV VSRANPGLKL VRLEHKLGIR ASDTAAFHLD DCRVPAQDLL
GDPDITTAGG FGGAMQTFDN TRPLVAAMAL GLTRACLDTT TELLADAGVH VDWDRPAHVQ
HAAAARLLQM EAEYEAAHAL TLRAAWMADN GRPNSMEASM AKAKAGRTGV AVSLACVELA
GATGYGEREL LEKWARDSKI LDIFEGTQQI QLLVVARHLL GLSSSQLK
//
