ID Q6FEG3_ACIAD Unreviewed; 625 AA.
AC Q6FEG3;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CAG67545.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:CAG67545.1};
GN Name=acdB {ECO:0000313|EMBL:CAG67545.1};
GN OrderedLocusNames=ACIAD0624 {ECO:0000313|EMBL:CAG67545.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG67545.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG67545.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CR543861; CAG67545.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6FEG3; -.
DR STRING; 202950.GCA_001485005_00857; -.
DR KEGG; aci:ACIAD0624; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_6; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430}.
FT DOMAIN 28..58
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 68..183
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 189..298
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 308..476
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 493..619
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 625 AA; 68530 MW; B255CCAF6666B6C2 CRC64;
MSAGHPHRYS QDIINAGLTS IEETDMPQYK APLRDMQFVL HELLNANEHY AKLPAFQENV
SRELVDQYLE AAADFCENEL SPLNQVGDRE GCTWNDGVVT TPTGFKEAYQ KYIELGFPSL
SAEEQYGGQG LPNSLGIAIS EMVGSSNWAW GMYPGLSHGA VRTLEHHGSE QQKDTYLPNL
VSGVWTGTMC LTESHAGSDL GIIRSKAEPN EDGSYAISGE KIFISAGEHD MADNIIHIVL
ARLPGAPKGT KGISLFIVPK FLVNEDGSLG ERNHVRCGSI EHKMGIHGNA TCVINFDRAK
GYLIGPENRG LNCMFTFMNT ARIGTAVQGL AASESSFQGA LTYAKDRLAM RSLSGPKAPE
KDADPIIVHP AVRNMLLTQK AFAEGGRALV YLLAQYADVV EHGITEEERK FADNILSLLT
PIAKAFLTET GSESAKHGVQ VFGGHGFISE HGMEQIVRDT RIACLYEGTT EIQALDLLGR
KVLQTQGAML RDFTKIIHKF VEANKDNAAM KEFIEPLASL NKEWGDVTMQ IGMRAMQNPD
EVGAAAVDYL YFSGYVTLAY LWARMAEVAQ QKLAAGTTDA DFYNAKVTTA RFYFKKILPR
VRSHVDVLST GVESLMALDA EHFAF
//
