ID A0A1F4JS33_9BURK Unreviewed; 378 AA.
AC A0A1F4JS33;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OGB25111.1};
GN ORFNames=A3I66_23060 {ECO:0000313|EMBL:OGB25111.1};
OS Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797562 {ECO:0000313|EMBL:OGB25111.1, ECO:0000313|Proteomes:UP000176765};
RN [1] {ECO:0000313|EMBL:OGB25111.1, ECO:0000313|Proteomes:UP000176765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGB25111.1}.
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DR EMBL; MESE01000055; OGB25111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4JS33; -.
DR STRING; 1797562.A3I66_23060; -.
DR Proteomes; UP000176765; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 7..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 121..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 230..378
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 378 AA; 41923 MW; 00BD087414DB339C CRC64;
MHPWSNDELE MLRDTARRFL AEHVTPNEKR WDAQQHVDRA IWNRAGDIGL LCASIPSEYG
GAGGDFRHEA VLYEEQAAAN NVSCGFQVHS GICAHYFAKY GTEQQKLYYL PKMASGELVC
AIAMTEPGTG SDLQAVKTRA QRDGDHYVIN GAKTFITNGG LCDLILLVAK TDPAQGAKGI
SLIIVETADL AGFKRGRLLE KIGQHGQDTA ELFFDDVRVP VDNLLGGHEG QGFVQLMQQL
PQERLIIGVS AVGAMEKAVE LTAQYTKQRH AFGKPLFDLQ NTRFTLAECK TETHIARVFI
DDCIAKHVRG ELDNATASMA KWWCTQKQCE IIDRCLQLFG GYGYMAEYPI AKMYADARVQ
KIYGGANELM KELIARAM
//
