ID A0A1V4MCC6_9FIRM Unreviewed; 379 AA.
AC A0A1V4MCC6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OPL12359.1};
GN ORFNames=AVO34_07545 {ECO:0000313|EMBL:OPL12359.1};
OS Firmicutes bacterium ML8_F2.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1775675 {ECO:0000313|EMBL:OPL12359.1, ECO:0000313|Proteomes:UP000189969};
RN [1] {ECO:0000313|EMBL:OPL12359.1, ECO:0000313|Proteomes:UP000189969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML8_F2 {ECO:0000313|EMBL:OPL12359.1};
RA Hamilton T.L., Pearson A., Macalady J.;
RT "Carbon and sulfur cycling below the chemocline in a meromictic lake.";
RL Submitted (DEC-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:OPL12359.1}.
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DR EMBL; LQBG01000054; OPL12359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4MCC6; -.
DR Proteomes; UP000189969; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR CDD; cd01158; SCAD_SBCAD; 1.
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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..377
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 379 AA; 41393 MW; 47E7D33FCCFF9B1D CRC64;
MNFTLTEMQE MTRQMVRDFA EKELKPGVAE RDEKEIFNRD LFDKMGQLGL TGIPWPEEYG
GGGCDFLSYI IAVEELSRVE ASAGTTMSAH ISLAGWPVYK YGSEEQKKKF LVPMALGEKL
GAYALTESTA GTDAAAVQTT AVLEDNKYIL NGNKIFTTNA GEAEIYIVFA ATDKEKKARG
ISGFIVEKGA PGLSFGKKEK KMGLRSSVTA EMIFENCEVP KENLLGNEGE GFKIAMSTLD
GGRNGIAAQA VGIAQGALDE AVSYAKTREQ FGRPIGSFQA ISFMLADMAT KIEAARLLTY
QAAYLENEGM PYGKASAMAK LYASETAMEV TTNAVQIFGG YGYTKDYPVE RLMRDAKITQ
IYEGTSEVQR LVISRYLLS
//
