ID A0A1C4U866_MICVI Unreviewed; 404 AA.
AC A0A1C4U866;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SCE67842.1};
GN ORFNames=GA0074695_0246 {ECO:0000313|EMBL:SCE67842.1};
OS Micromonospora viridifaciens.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1881 {ECO:0000313|EMBL:SCE67842.1, ECO:0000313|Proteomes:UP000198242};
RN [1] {ECO:0000313|EMBL:SCE67842.1, ECO:0000313|Proteomes:UP000198242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43909 {ECO:0000313|EMBL:SCE67842.1,
RC ECO:0000313|Proteomes:UP000198242};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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DR EMBL; LT607411; SCE67842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4U866; -.
DR OrthoDB; 3176804at2; -.
DR Proteomes; UP000198242; Chromosome i.
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}.
FT DOMAIN 9..114
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 126..223
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 254..398
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 404 AA; 43839 MW; 59F6503409571522 CRC64;
MVEFSLDLNE EQRDLREWVH GFAADVVRPA AAEWDAREET PWPIIQEAAK VGLYGFEFLA
TCWADPTGLA LPIASEELFW GDAGIGLSIF GTSLAVAAIY GAGTPDQMVE WVPQCFGDVD
QPAVAAFCTT EPEAGSDVGA MRTRAVYDEA TDEWVLNGQK AYATNGGIAG VHVVTASVEP
ELGSRGQAAF VVPPGTPGLT ATRKLRKLGL RASHTADVFL DDVRVPGRCL LGEREALLAR
LDRARSGQRA SGQAAMRTFE LSRPTVGAQA LGVARAAYEY ALDYAKERVQ FGRPIIENQA
VAFALADMKM EIDAARLLVW RASWMGRNNR PFTAGEGSMS KLKAGEVAVS VTEKAVQLLG
GAGFLRDHPV ERWYRDAKIY TIFEGTSEIQ RLVISRAISG MQIR
//
