ID A0A0Q8DR13_9ACTN Unreviewed; 391 AA.
AC A0A0Q8DR13;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KRA31451.1};
GN ORFNames=ASD81_18640 {ECO:0000313|EMBL:KRA31451.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA31451.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA31451.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA31451.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA31451.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA31451.1,
RC ECO:0000313|Proteomes:UP000051699};
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 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:KRA31451.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMGV01000007; KRA31451.1; -; Genomic_DNA.
DR RefSeq; WP_056713719.1; NZ_LMGV01000007.1.
DR AlphaFoldDB; A0A0Q8DR13; -.
DR OrthoDB; 142556at2; -.
DR Proteomes; UP000051699; 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 PIRSF; PIRSF016578; HsaA; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051699}.
FT DOMAIN 12..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 128..222
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..384
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 391 AA; 42010 MW; 9918476F8A1AABA5 CRC64;
MKNADFPTYA LTEEHQAIRE AVRAICDAKV APFAAIVDEE ARYPQEAHDA LVAADFHAPH
IPEEFGGAGA DALATAIVIE EVARACVSSS LIPVVNKLGS LPVEIGGSEE LKKKYLGALA
RGEGGFSYCL SEPDAGSDAA NQKTRAVRDG DGWVLNGVKR WISNAGVSEY YTVLAKTDPD
LRTKGISAFV VEKSDEGVTF GAPEKKLGIK GSPTCEVYFD NVRIPGDRII GEEGKGFEYA
MKTLDHTRVT IAAQALGVAQ GALDYALGYA KERKQFGSAI SDFQGMQFML ADMGMKIEAA
RQLTYAAAAR SERGDADLGF FSAAAKCFAS DVAMEVTTNA VQVLGGYGYT RDYPVERMMR
DAKITQIYEG TNQVQRIVMA RQLLAGVQST L
//
