ID A0A0R2QDC9_9ACTN Unreviewed; 401 AA.
AC A0A0R2QDC9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KRO46269.1};
GN ORFNames=ABR56_04335 {ECO:0000313|EMBL:KRO46269.1};
OS Acidimicrobium sp. BACL27 MAG-120823-bin4.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=1655564 {ECO:0000313|EMBL:KRO46269.1, ECO:0000313|Proteomes:UP000050870};
RN [1] {ECO:0000313|EMBL:KRO46269.1, ECO:0000313|Proteomes:UP000050870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL17 MAG-120823-bin4 {ECO:0000313|EMBL:KRO46269.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRO46269.1}.
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DR EMBL; LIAO01000210; KRO46269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2QDC9; -.
DR Proteomes; UP000050870; Unassembled WGS sequence.
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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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.
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|RuleBase:RU362125}.
FT DOMAIN 40..114
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 118..212
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 224..381
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 401 AA; 43531 MW; B6377F27B0E88E61 CRC64;
MVAVETENVL TDADVSALVG SLLEKYPPNK TKAVDFLGAQ FDAGLAWVHF EVGNGGLGAS
PKYQKIVNEA IAVANGPSSY ARNPIGYGMC APTIIQWGTD SQKKKYLRSL FTGEEIWCQL
FSEPGSGSDF AGLSAKGVRD GDEWIINGQK VWTTLAHLSK YGLLVVRTDP QAVKHAGLTA
VIVDMKAPGV EVRPLRQMTG EAEFNEVYFT DVRVPVAETL GGTGDGWRVS LTTLMNERVA
IGGAIPRKAT GPIREAIKIW ESLSPEMQSS ATKDELMKLW IKAEVLRLTN IRAGQNRRIG
TPGPEGSIGK VASAELNKDT YEFCVGLLGA NGMLYGSYEM VRPETAMSFD SVPKAFLRSR
ANSIEGGTTE VMKNILGERI LGLPGDVRVD RDKPWHEVPR N
//
