ID E3HVM9_ACHXA Unreviewed; 384 AA.
AC E3HVM9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Acyl-CoA dehydrogenase, N-terminal domain protein 4 {ECO:0000313|EMBL:ADP15032.1};
DE EC=1.3.-.- {ECO:0000313|EMBL:ADP15032.1};
GN OrderedLocusNames=AXYL_01694 {ECO:0000313|EMBL:ADP15032.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP15032.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP15032.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP15032.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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}.
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DR EMBL; CP002287; ADP15032.1; -; Genomic_DNA.
DR RefSeq; WP_013392371.1; NC_014640.1.
DR AlphaFoldDB; E3HVM9; -.
DR STRING; 762376.AXYL_01694; -.
DR KEGG; axy:AXYL_01694; -.
DR PATRIC; fig|762376.5.peg.1692; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_4; -.
DR OrthoDB; 7795946at2; -.
DR Proteomes; UP000006876; Chromosome.
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; 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; 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:ARBA00022630};
KW Oxidoreductase {ECO:0000313|EMBL:ADP15032.1}.
FT DOMAIN 8..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..216
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 228..377
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 384 AA; 41666 MW; 79365F36E5389694 CRC64;
MDFSLDSTQI ELRDSLRRYL TAEVAPIVNR YEAEARVVPQ EMVRAMRDFG LLGGMLQEKD
GGYGLPMTTY GMLIAELARV WPSLRSIVST SNLAASVLSD GGSPYLKEKY LPRVLSGEAI
ASFALSEPNI GSDAANVETR AVETATGWRV NGRKLYISLG TVCELGVVFV QTQRQSGERG
VSCLLFERAM PGFSSSPIHK MGMLSCPLGE LLFEDVEIPA ANLIGTEGKG FALAKKYLNI
GRCVVAFSAL GIAEAAYEAA VKYAGDRVQF GRPIGGFQLV QHMIADMMTL VETSRLLCWR
AADALDRNAA DSQMLCSMAK RHATDAVLRV AELSMQVHGG AGYTTLFPVE RHYRDARHLS
IAEGTNQIQA LLMAQSVLGI SALK
//
