ID G8QZW7_OWEHD Unreviewed; 602 AA.
AC G8QZW7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AEV32607.1};
GN OrderedLocusNames=Oweho_1618 {ECO:0000313|EMBL:AEV32607.1};
OS Owenweeksia hongkongensis (strain DSM 17368 / CIP 108786 / JCM 12287 / NRRL
OS B-23963 / UST20020801).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Owenweeksiaceae;
OC Owenweeksia.
OX NCBI_TaxID=926562 {ECO:0000313|EMBL:AEV32607.1, ECO:0000313|Proteomes:UP000005631};
RN [1] {ECO:0000313|EMBL:AEV32607.1, ECO:0000313|Proteomes:UP000005631}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963
RC {ECO:0000313|Proteomes:UP000005631};
RX PubMed=23450211; DOI=10.4056/sigs.3296896;
RA Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., Del Rio T.G.,
RA Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Rohde M., Tindall B.J., Detter J.C., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Genome sequence of the orange-pigmented seawater bacterium Owenweeksia
RT hongkongensis type strain (UST20020801(T)).";
RL Stand. Genomic Sci. 7:120-130(2012).
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; CP003156; AEV32607.1; -; Genomic_DNA.
DR RefSeq; WP_014201963.1; NC_016599.1.
DR AlphaFoldDB; G8QZW7; -.
DR STRING; 926562.Oweho_1618; -.
DR KEGG; oho:Oweho_1618; -.
DR PATRIC; fig|926562.3.peg.1619; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_3_10; -.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000005631; Chromosome.
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; 2.
DR InterPro; IPR049426; Acyl-CoA-dh-like_C.
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; PF21263; Acyl-CoA-dh_C; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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:UP000005631}.
FT DOMAIN 34..147
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 151..245
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 257..418
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 470..573
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 602 AA; 66820 MW; A9085326A35ACDA2 CRC64;
MSTTTAEEQK FLRGGEFIIR ESKSEDIFIP EDFNEEQNMM AQATTEFMEK EVVPYRERFE
KKDYTFTEEL MKKVGELGLL GITVSEEYGG LGMDFNTSML VTDKISGVTG SLSTAYGAHT
GIGVLPIALY GNEEQKKKYL PKLVTGEYMG AYCLTEPGAG SDANSGKTKA ELTADGKHYK
INGQKIWISN AGFADIFTVF ARIEDDKYLT GFIVERGTEG LSFGEEENKL GIRSSSTRQV
FFNDMLVPVE NLLGERNGGF KIAMNALNYG RIKLAVATLD ANKRVITHSV EYGNERKQFG
QSITNFGAIQ QKLADMATLT WAAESASYRA GQDVENHIIR LQEGGMSAPE AKLKGVEEYA
IECAILKVFG SEVNSFVVDE GVQIYGGMGY SADAPMEAAY RDARITRIYE GTNEINRMHS
VGMLLKKAMK GEVDLMTPAM KIGSELMSIP SFDTPDYSVL FTEEKEMVEK LKKAFLMVAG
KAVEKFTIEI ENEQQLLMNA ADMLLQVYAA ESAILRAEKL ANKNGEDAAA NQIDMARLNL
HFAIEKVGQA GREAIYSFTE GDEQRMLLMG LKRFTKVQNP VNVKETRKRI AGKVIAENKY
PF
//
