ID A0A0C4Y4Y5_9BURK Unreviewed; 595 AA.
AC A0A0C4Y4Y5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AJG17928.1};
DE EC=1.3.8.7 {ECO:0000313|EMBL:AJG17928.1};
GN ORFNames=RR42_m0515 {ECO:0000313|EMBL:AJG17928.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG17928.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG17928.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG17928.1};
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; AJG17928.1; -; Genomic_DNA.
DR RefSeq; WP_043343616.1; NZ_CP010536.1.
DR AlphaFoldDB; A0A0C4Y4Y5; -.
DR STRING; 68895.RR42_m0515; -.
DR KEGG; cbw:RR42_m0515; -.
DR OrthoDB; 9764895at2; -.
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; IPR020953; Acyl-CoA_DH_N_bac.
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 Pfam; PF12418; AcylCoA_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:AJG17928.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT DOMAIN 3..35
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 42..159
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 164..272
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..451
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 470..591
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 595 AA; 64634 MW; FE4C6357805F830C CRC64;
MGQYTAPLRD MQFVLHELLG VEAELKALPK HADVDADTIN QVLEQAGKFC SEVVFPLNQS
GDREGCTYVG DGVVTAPKGF KEAYKQYVEA GWPALGCDPE YGGQGLPILV NNALYEMLNS
ANQAWTMYPG LSHGAYEALH AHGTPELQKV YLPKLVSGEW TGTMCLTEPH CGTDLGILRS
KAEPQADGSY TITGTKIFIS AGEHDLSANI IHLVLARLPD APQGTKGISL FVVPKFVPDA
SGNPGERNGI KCGSIEHKMG IHGNATCVMN LDGARGWLVG EPNKGLNAMF VMMNAARLGV
GMQGLGLTEV AYQNSLAYAK DRLQMRALTG PKAPDKPADP IIVHPDVRRM LLTQKAFAEG
GRAFSYWTAL QIDRELSHPD ESVRKEAGDL VALLTPVIKA FLTDNAFTAT NEGMQVFGGH
GYIAEWGMEQ YVRDARINMI YEGTNTIQAL DLLGRKILGD MGAKMKAFGK IVQAFVEEEG
TNEAMQEFVN PLADLGDKVQ KLTMEIGMKA MGNPDEVGAA AVPYLRVVGH LVFSYFWARM
AKIALEKEAS GDKFYTTKLA TARFYFARLL PETASQIRMA RAGSATLMAL DADLF
//
