ID A0A069IA93_9BURK Unreviewed; 429 AA.
AC A0A069IA93;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KDP86497.1};
GN ORFNames=CF70_007130 {ECO:0000313|EMBL:KDP86497.1};
OS Cupriavidus sp. SK-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP86497.1, ECO:0000313|Proteomes:UP000023560};
RN [1] {ECO:0000313|EMBL:KDP86497.1, ECO:0000313|Proteomes:UP000023560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-3 {ECO:0000313|EMBL:KDP86497.1,
RC ECO:0000313|Proteomes:UP000023560};
RA Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT "Cupriavidus sp. strain SK-3.";
RL Submitted (MAY-2014) 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:KDP86497.1}.
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; JFJV02000157; KDP86497.1; -; Genomic_DNA.
DR RefSeq; WP_051648552.1; NZ_JFJV02000157.1.
DR AlphaFoldDB; A0A069IA93; -.
DR OrthoDB; 7316074at2; -.
DR Proteomes; UP000023560; 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; IPR013107; Acyl-CoA_DH_C.
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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 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.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 47..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 159..248
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 288..401
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 45766 MW; DDA620B33300A14A CRC64;
MHLKPTGTTS RQRISGWHRE SGFTPAAPPP DATGTAGAAR PLRTDEALRA LSARFAARAA
THDRDATFAF ENIAELHQLG LLDLTVPRAL GGAGAGLAEA RRVVHHVAAG DPSTALVLVM
QILGHRNLAQ DTQWPADVRE QVQRSAVEQG ALINSLRVEP ALGSPARGGL PATVARRQGD
GWLLSGHKIY STGIPALSWL AVWGRTDEPS PRTGVFLVPR DAPGISVLPT WDHLGMRATG
SHDVVFDNTP LPAAYAVDLR LPEAWAERHD PAWAVWTSTL LGTLYNAVAH SARDWFVAWL
NLRAPGSLGA PLATLPRFQE AVGRIDSWLL ANRILLDRFS ADADAGAPAS ATDSNLLKLN
ITDNAIAAVE LAVRLAGNPA LSRGNPLERH YRNVLCSRIH TPQNDAILVS AGEQALRAAA
HAYPPGTNA
//
