ID A0A255DCH5_9MYCO Unreviewed; 415 AA.
AC A0A255DCH5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OYN76321.1};
GN ORFNames=CG716_22105 {ECO:0000313|EMBL:OYN76321.1};
OS Mycolicibacterium sphagni.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1786 {ECO:0000313|EMBL:OYN76321.1, ECO:0000313|Proteomes:UP000216063};
RN [1] {ECO:0000313|EMBL:OYN76321.1, ECO:0000313|Proteomes:UP000216063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33027 {ECO:0000313|EMBL:OYN76321.1,
RC ECO:0000313|Proteomes:UP000216063};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OYN76321.1}.
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DR EMBL; NOZR01000022; OYN76321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255DCH5; -.
DR OrthoDB; 571684at2; -.
DR Proteomes; UP000216063; Unassembled WGS sequence.
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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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; PF08028; Acyl-CoA_dh_2; 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 4: Predicted;
FT DOMAIN 49..134
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 255..390
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 43704 MW; BF08EE5DF05C9AB6 CRC64;
MTAQTSEASS PVAPRPGFTS EPLGGTVAER LDRLTAVVDD LRHSDPAAER GRVLQYDAVE
AIRRTGVLTL RVPAQYGGPG GSVRDVLTAV IRIARGSSNV AQALRPHFGF AERLLSNRAT
EAEREEWFPR VNTGVIIGNA ITDAKGKTPA GADTTLLADG DGVLRLNGYK FYSTGTLFAD
LIAVSASDSE GRDLQAIVPA GREGVELFDD WEGFGQRTTA SGGTRFTNVE VQPHEVTTVS
DGKHLGHSTA FLQLYLAAVA AGIAAAARDD AVWYVQTKAR PASHSLADTA ARDPFTLQAV
GEISANASAA EALVLGAADA LDAVVDSGRI ADADELARVA IVVAEAQLIA ERLTLAAAER
LFDTGGASAT ARALNLDRHW RNVRTVATHN PLAYKAHASG NYLVNGVWPP ANGYF
//