ID   A0A1M3F6U3_9CELL        Unreviewed;       385 AA.
AC   A0A1M3F6U3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OJV80183.1};
GN   ORFNames=BGO37_01990 {ECO:0000313|EMBL:OJV80183.1};
OS   Cellulomonas sp. 73-92.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895740 {ECO:0000313|EMBL:OJV80183.1, ECO:0000313|Proteomes:UP000184539};
RN   [1] {ECO:0000313|EMBL:OJV80183.1, ECO:0000313|Proteomes:UP000184539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-92 {ECO:0000313|EMBL:OJV80183.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV80183.1}.
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DR   EMBL; MKTH01000014; OJV80183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3F6U3; -.
DR   STRING; 1895740.BGO37_01990; -.
DR   Proteomes; UP000184539; 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          17..102
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          240..364
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   385 AA;  41493 MW;  CB2186078C31842C CRC64;
     MPRTHRMLLT DDLLATIRER AAGHDRDNTF PDDDLADLRA AGYLLAFVPP ELGGRGLTLE
     EVAREQVRLA GAAPATALSI NMHLVVTGMA AVLHARGDES MAFVLRDAAA GEVFAFGNSE
     AGNDLVMFGS RTRAQRQPDG GYRYFGTKIF TSLAPVWTRL ATFGLDDEHP DGPRLVHGVV
     TREGTTTKDD WDTLGMRASQ SRTTVLEGAY APADRIVRAL PPGPNADPFI VALFAVFEIL
     LAAVYTGIGR RALALGVEAT RRRTSMKYDG RAYSQDPDIR WKVADAALAQ DGAELEVFAL
     ARGIDEAEDY GSRLFAQLVG LKVRATEAAR VVVDLALRVS GGAGYSTGQE LNRLYRDVLA
     GIYHPSDDES AHATVAQSLL GPLEA
//