ID   A0A3A5MKB7_9MICO        Unreviewed;       400 AA.
AC   A0A3A5MKB7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RJT89371.1};
GN   ORFNames=D6T64_07295 {ECO:0000313|EMBL:RJT89371.1};
OS   Cryobacterium melibiosiphilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=995039 {ECO:0000313|EMBL:RJT89371.1, ECO:0000313|Proteomes:UP000272015};
RN   [1] {ECO:0000313|EMBL:RJT89371.1, ECO:0000313|Proteomes:UP000272015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh39 {ECO:0000313|EMBL:RJT89371.1,
RC   ECO:0000313|Proteomes:UP000272015};
RA   Liu Q., Xin Y.-H.;
RT   "Novel species of Cryobacterium.";
RL   Submitted (SEP-2018) 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:RJT89371.1}.
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DR   EMBL; QZVS01000074; RJT89371.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A5MKB7; -.
DR   OrthoDB; 3404950at2; -.
DR   Proteomes; UP000272015; 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          15..85
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          242..370
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   400 AA;  43296 MW;  8F4B0D6CF484FF6C CRC64;
     MPRDIAGPLD TALLERIRSR ASGHDHGNTF FHEDLAELTA CGYLRALVPT EFGGLGLSLA
     QTTRLQTRLA AHAPATALAI NMHLVWTGVA KALHERGDDS LDFLLREAGQ GEIFAFGVSE
     PGNDLVLFDS VTDARPDPAG GFRFTGTKVF TSLSPAWTRL GTFGRDDSVP GDPRMVWAFL
     DRATPGIRQK DDWDTLGMRA SQSQSTVLEG ALAPEDRVVR RLPVGPNNDP LIFAIFANFE
     ILLASVYAGI GQRAVELAVD SATRRTSRKN DGRRHAQDPI VRWRVADAAI AMDGLYPQID
     ALARDIDAQV DRDSFRDIQW YALLSGLKFR ATETAKAVVD QAVRVTGGSA YAAGSEIGRL
     YRDVLAGLFH PSDADSAHST VATAWLGPLA VPATPPNTER
//