ID A0A1Q3GFE3_9BACT Unreviewed; 396 AA.
AC A0A1Q3GFE3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OJJ14196.1};
GN ORFNames=BKI52_43785 {ECO:0000313|EMBL:OJJ14196.1};
OS marine bacterium AO1-C.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae.
OX NCBI_TaxID=1905359 {ECO:0000313|EMBL:OJJ14196.1, ECO:0000313|Proteomes:UP000186474};
RN [1] {ECO:0000313|EMBL:OJJ14196.1, ECO:0000313|Proteomes:UP000186474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-C {ECO:0000313|EMBL:OJJ14196.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) 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:OJJ14196.1}.
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DR EMBL; MLAY01000025; OJJ14196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3GFE3; -.
DR STRING; 1905359.BKI52_43785; -.
DR Proteomes; UP000186474; 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:SF3; ACYL-COA DEHYDROGENASE FADE29; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000186474}.
FT DOMAIN 47..130
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 135..229
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 241..392
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 396 AA; 44726 MW; 72E29ABFD0789B8C CRC64;
MDTSIQTDLE TFRTETRAWL EENCPTSLRK PIKSAEDYFW GGRNPHYNSD DQKLWFERMR
DRGWTAPTWP TQYGGGGLST QENKVLLEEM AKLQCPTPLF SFGLSMLGPA LLKFGNEEQK
AQYLTEITHG KVWWCQGYSE PGAGSDLAGL QTRAEDQGDH FLVNGQKVWT SYADKSDMIF
CLVRTNPDAK KHTGISFMLI DMKSEGVSTR PIKLISGKSV FCETFFDNVK VPKENLVGEL
NAGWSIAKYL LTHERSMIGG IGDVRNEKPL FQRAVEALGL ENGRLSDPVL RTDIARWMID
QEGLMWTIER TTDESKAGQP IGAKSSFFKY YYTEQNKLKY ELLMALEGMD ALAWGEEYND
GKLARDFCRT KGNSIEGGTS EIQLNIISKR ILGLPG
//
