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Database: UniProt
Entry: A0A0D0NAK8_KITGR
LinkDB: A0A0D0NAK8_KITGR
Original site: A0A0D0NAK8_KITGR 
ID   A0A0D0NAK8_KITGR        Unreviewed;       379 AA.
AC   A0A0D0NAK8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KIQ65245.1};
GN   ORFNames=TR51_14935 {ECO:0000313|EMBL:KIQ65245.1};
OS   Kitasatospora griseola (Streptomyces griseolosporeus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ65245.1, ECO:0000313|Proteomes:UP000032066};
RN   [1] {ECO:0000313|EMBL:KIQ65245.1, ECO:0000313|Proteomes:UP000032066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ65245.1,
RC   ECO:0000313|Proteomes:UP000032066};
RA   Arens J.C., Haltli B., Kerr R.G.;
RT   "Draft genome sequence of Kitasatospora griseola MF730-N6, a bafilomycin,
RT   terpentecin and satosporin producer.";
RL   Submitted (FEB-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:KIQ65245.1}.
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DR   EMBL; JXZB01000002; KIQ65245.1; -; Genomic_DNA.
DR   RefSeq; WP_043911429.1; NZ_JXZB01000002.1.
DR   AlphaFoldDB; A0A0D0NAK8; -.
DR   STRING; 2064.TR51_14935; -.
DR   PATRIC; fig|2064.6.peg.3209; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000032066; 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; 2.
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:UP000032066}.
FT   DOMAIN          9..120
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..213
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  40417 MW;  CA5C6723C046D4C5 CRC64;
     MAVDRLLPTE EAADLIALTR DLADKELAPK VESHEKQELY PEGLFALLGQ AGLLGLPYSE
     EFGGGGQPYE VYLQVLEELA SRWAAVAVAT SVHTLACHPL NAFGTPEQKE QWLPRMLAGE
     MIGGYSLSEP NAGSDAAALT CKAEPVDGGY RITGTKAWIT HGGKADFYAL FARTAPGAHG
     ISCFLAPGQV EGLTFGAPEE KMGLNGVPTT AAYWDGALLA PERRIGAEGQ GLSIAFSALD
     SGRLGIAACA TGLAQAALDT AVAYANERTT FGRKIVDHQG LGFLLADMAA AVDSARATYL
     DAARRRDLGR PFSRQASVAK LIATDAAMKV TTDAVQVLGG YGYTRDFPVE RYMREAKIMQ
     IFEGTNQIQR LVISRQFAR
//
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