ID A0A0Q5LEE6_9BURK Unreviewed; 391 AA.
AC A0A0Q5LEE6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQR41447.1};
GN ORFNames=ASF94_13265 {ECO:0000313|EMBL:KQR41447.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR41447.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR41447.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR41447.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR41447.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR41447.1,
RC ECO:0000313|Proteomes:UP000051403};
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 -!- 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:KQR41447.1}.
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DR EMBL; LMOV01000028; KQR41447.1; -; Genomic_DNA.
DR RefSeq; WP_056670244.1; NZ_LMOV01000028.1.
DR AlphaFoldDB; A0A0Q5LEE6; -.
DR STRING; 1736280.ASF94_13265; -.
DR OrthoDB; 6184213at2; -.
DR Proteomes; UP000051403; 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 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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051403}.
FT DOMAIN 18..111
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 233..366
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 391 AA; 42980 MW; 76075E15BDB9F1E4 CRC64;
MNAALHPSLE DSLSLLIEEL RHSAVERDRA GGHAAEEKER IREAGLLRLS IPPGYGGLGL
PWPGIYRIVR RVAAVDSALA HLLAFHHLQV ATVLIYGDED QRRRWLTRTI EEGGWWGNAV
NPRDTRLVAT DTAQGYQLDG AKGFCSGTRG SRFLTLSARH AASHDVVLGI VETQQPGITV
HDDWDPIGQR QTDSGSVGFK HVPLRREDVL RAHGATPTAA HTLRNCFAQL VLVNLYLGIA
IGALEEARVY LHREGRPWIA APVDHASKDP YTLQRVGELH VQISAATALA ERAALSVQAA
YERGEQLTPQ ERGEAAIAVA EAKVMAHRAG LQAGQELFEV VGARGTRASL GYDRFWRNVR
THTLHDPLDY KLNALGRWAL NGELPSPDQY N
//
