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Database: UniProt
Entry: A0A066YXW0_9ACTN
LinkDB: A0A066YXW0_9ACTN
Original site: A0A066YXW0_9ACTN 
ID   A0A066YXW0_9ACTN        Unreviewed;       405 AA.
AC   A0A066YXW0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KDN82740.1};
GN   ORFNames=KCH_54750 {ECO:0000313|EMBL:KDN82740.1};
OS   Kitasatospora cheerisanensis KCTC 2395.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN82740.1, ECO:0000313|Proteomes:UP000027178};
RN   [1] {ECO:0000313|EMBL:KDN82740.1, ECO:0000313|Proteomes:UP000027178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN82740.1,
RC   ECO:0000313|Proteomes:UP000027178};
RA   Nam D.H.;
RT   "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL   Submitted (MAY-2014) 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:KDN82740.1}.
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DR   EMBL; JNBY01000103; KDN82740.1; -; Genomic_DNA.
DR   RefSeq; WP_035866898.1; NZ_KK853997.1.
DR   AlphaFoldDB; A0A066YXW0; -.
DR   PATRIC; fig|1348663.4.peg.5297; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_11; -.
DR   OrthoDB; 3861575at2; -.
DR   Proteomes; UP000027178; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027178}.
FT   DOMAIN          10..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..223
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          250..399
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   405 AA;  43582 MW;  6C886DD48D740185 CRC64;
     MTTFSLDPGP DQIAVRDWLH GFAADVIRPA AAEWDEREET PWPIIQEAAK LGIYSLDFYA
     QQFFDPSGVG IPIAMEELFW GDAGIGLAIT GTTLAAVAVL ANGTDEQIGT WAPQMFGTPD
     DVKVAAFCSS EPDAGSDVSA LRTRAVYDQA KDEWVLNGTK TWATNGGIAH VHVVVATVDP
     ELGARGQASF LIPPGTKGLS QGQKFKKHGI RASHTAEVVL DDVRIPGHCL LGGKEKLDAR
     LARAREGTKG GGKNAAMATF EASRPAVGAQ AIGIARAAYE VALDYAKTRV QFGRPIIENQ
     GVAFQFADMK TRIDASRLLV WRASWMAVNN QPFTNAEGSM SKLYAGETAK FVTAQAMQIL
     GGNGFTREYP VERMHRDSAI YTVFEGTSEI QRLVIARAIS GAPIR
//
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