ID A0A1I0PRR6_9FLAO Unreviewed; 379 AA.
AC A0A1I0PRR6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SEW17021.1};
GN ORFNames=SAMN05421841_1371 {ECO:0000313|EMBL:SEW17021.1};
OS Chryseobacterium wanjuense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=356305 {ECO:0000313|EMBL:SEW17021.1, ECO:0000313|Proteomes:UP000199469};
RN [1] {ECO:0000313|EMBL:SEW17021.1, ECO:0000313|Proteomes:UP000199469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17724 {ECO:0000313|EMBL:SEW17021.1,
RC ECO:0000313|Proteomes:UP000199469};
RA de Groot N.N.;
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}.
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DR EMBL; FOIU01000001; SEW17021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0PRR6; -.
DR STRING; 356305.SAMN05421841_1371; -.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000199469; 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 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; 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 10..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..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; 41488 MW; 2E1D870D0091F823 CRC64;
MNTETIDNIK MIAETAKEFA EKNIRPNIME WDESQTFPKD LFHQLGEMGF MGIVIPEQYG
GSGLGYHEYV TILDEISQVD PSIGLSVAAH NSLCTNHIYE FGNEEQRNKW LPQLASGKVI
GAWGLTEHNT GSDSGGMSTT AVKDGDEWII NGAKNFITHA ISGDIAVVMT RTGEKGAKNN
STAFVLEKGM AGFTSGKKEN KLGMRASETA ELIFDNVRVP DSHRLGEVGE GFKQAMKILD
GGRISIAALS LGTARGAYKA ALKYAKERHQ FGKSISEFQA INFMLADMAT EIDAAELLIH
RASTLKNAKQ KMTREGAMAK LYASEACVRI SNNAVQIFGG YGYTKDFPAE KFYRDSKLCT
IGEGTSEIQR LVIGRDITK
//
