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Database: UniProt
Entry: A0A0N8WGD2_9FLAO
LinkDB: A0A0N8WGD2_9FLAO
Original site: A0A0N8WGD2_9FLAO 
ID   A0A0N8WGD2_9FLAO        Unreviewed;       380 AA.
AC   A0A0N8WGD2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQC31171.1};
GN   ORFNames=AAY42_15705 {ECO:0000313|EMBL:KQC31171.1};
OS   Allomuricauda eckloniae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=346185 {ECO:0000313|EMBL:KQC31171.1, ECO:0000313|Proteomes:UP000050827};
RN   [1] {ECO:0000313|EMBL:KQC31171.1, ECO:0000313|Proteomes:UP000050827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK169 {ECO:0000313|EMBL:KQC31171.1,
RC   ECO:0000313|Proteomes:UP000050827};
RA   Kwon Y.M., Kim S.-J.;
RT   "Complete genome of flavobacterium.";
RL   Submitted (APR-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:KQC31171.1}.
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DR   EMBL; LCTZ01000002; KQC31171.1; -; Genomic_DNA.
DR   RefSeq; WP_055396905.1; NZ_LCTZ01000002.1.
DR   AlphaFoldDB; A0A0N8WGD2; -.
DR   STRING; 346185.AAY42_15705; -.
DR   PATRIC; fig|1547436.3.peg.3237; -.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000050827; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050827}.
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          231..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41356 MW;  DF930F43F1CE10DC CRC64;
     MDFTLSEEQL MIKQAAKDFA QNELLPGVIE RDDAQKFPTE LLNKMGELGF MGMMVDEKYG
     GSGLDTLSYV LAMEELSKID ASASVMVSVN NSLVCWGLET YGTEAQKQKY LTRLSTGEII
     GAFCLSEPEA GSDATSQKTT AIDNGDHYIL NGTKNWITNG SAAEVYLVVA QTDVEKGHKG
     INVLIVEKGA EGFEIGPKEN KLGIRGSDTH SLLFNDVKVP KENRIGEDGF GFKFAMKTLA
     GGRIGIAAQA LGIAAGAYEL SKKYSKERKA FGTEIANHQA IAFKLADMHT KIQAARHLVY
     QAACDKDNGD DYTLSGAMAK LYASEVAMET AVEAVQIHGG NGFVKDYHVE RFMRDAKITQ
     IYEGTSEIQK IVISRSILKS
//
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