ID A0A0Q7ZZ95_9ACTN Unreviewed; 365 AA.
AC A0A0Q7ZZ95;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQZ74882.1};
GN ORFNames=ASD66_00370 {ECO:0000313|EMBL:KQZ74882.1};
OS Nocardioides sp. Root151.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ74882.1, ECO:0000313|Proteomes:UP000051274};
RN [1] {ECO:0000313|EMBL:KQZ74882.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ74882.1,
RC ECO:0000313|Proteomes:UP000051274};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ74882.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ74882.1,
RC ECO:0000313|Proteomes:UP000051274};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:KQZ74882.1}.
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DR EMBL; LMGG01000001; KQZ74882.1; -; Genomic_DNA.
DR RefSeq; WP_056889726.1; NZ_LMGG01000001.1.
DR AlphaFoldDB; A0A0Q7ZZ95; -.
DR Proteomes; UP000051274; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd00567; ACAD; 1.
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; 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:SF20; ACYL-COA DEHYDROGENASE FADE28; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000051274}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 232..355
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 365 AA; 38303 MW; 0C5F47E8350D594F CRC64;
MHFGLSEEQE ELAGAVRTLV ERRAGQVDLR AATQAARGFD EALWETLCGQ IGVAALAIPE
EYGGAGFSTF ETHVVLETLG RTLTPTPLLG SGVLATRAVL LAGTPDDCAR LLPPLAEGTH
VAALAWADAS GQWRADGSDV RATADGDSWR LDGAATLVLD AHGADLLMVV AATEDGPRLF
EADLSAGVER TATPALDLTL QLDTVTFDGA PATPVGGVLT DELATLRAEA TVAVTALQVG
GAQGALDRTV AHLKEREQFG RPLGSFQALK HRVADLLVAV ETSRSISWSA AWAAAQGDAD
VVRQAALAKA WCSEAFAEVA AEMVQLHGGI AITWEHDAHL FFKRAHATGE LFGSAREHRR
SLLPA
//
