ID A0A0C4YFD5_9BURK Unreviewed; 603 AA.
AC A0A0C4YFD5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AJG19456.1};
DE EC=1.3.8.7 {ECO:0000313|EMBL:AJG19456.1};
GN ORFNames=RR42_m2064 {ECO:0000313|EMBL:AJG19456.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG19456.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG19456.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG19456.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010536; AJG19456.1; -; Genomic_DNA.
DR RefSeq; WP_043346274.1; NZ_CP010536.1.
DR AlphaFoldDB; A0A0C4YFD5; -.
DR STRING; 68895.RR42_m2064; -.
DR KEGG; cbw:RR42_m2064; -.
DR Proteomes; UP000031843; Chromosome main.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AJG19456.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT DOMAIN 34..154
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 160..273
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 296..458
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 475..599
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 603 AA; 65451 MW; 7F4A27597502B7FE CRC64;
MSTKYKAPVD DYVFLLHDVI APVAPHALGE MTRDDTRQVL EQAARFFEEV WAPLDGPADE
EGCHFEDGVV RTPDGYRAGY AALCEAGWNR VSAPEEFGGT GLPELIGQAV HEFTASACNS
LGLYAGLTGG AHATVSRNGE PWMLQYIVAP MVEGRWAGTM CLTEPHCGTD LRLMKTRAVP
QPDGSWRLNG TKTFISGGDH DLTENIIHLV LAKVPDEDGR IREDLSTVRL FLVSKRVVDS
ETGALGGPNG VVVAGVEHKM GLKGSATCTM SFEHALAYPL RESSQSGGTQ RKTSAGMSGM
FDMMNSARLG TGLQAVSSAT RAYGHAADYA RERLAGRAAK AEDRTGGAAD PIVVHPDVRR
LLLKQASFLE AARALALHVR TLLDEPDEAI RANRSAIGSL LTPVIKAFFS DRSFESANDA
MQLMGGHGYI RDNGVEQLVR DCRIFQLYEG ANGVQALDLV LRKLPAAGGR ALADFLDLVD
ATASEAEQQE PLRAYAEALR KAVQEIRASA NWFADPARDP YDAGASSSDF LAMMGIVACA
WMWLRMSNVA LPLLPHADNK QFLERKLELA RYWFARELPL VFALRERVET GAACLMALPA
DQF
//
