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Database: UniProt
Entry: A0A231PKR8_9ACTN
LinkDB: A0A231PKR8_9ACTN
Original site: A0A231PKR8_9ACTN 
ID   A0A231PKR8_9ACTN        Unreviewed;       385 AA.
AC   A0A231PKR8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OXS35262.1};
GN   ORFNames=CHR28_12210 {ECO:0000313|EMBL:OXS35262.1};
OS   Streptomyces sp. XY006.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2021410 {ECO:0000313|EMBL:OXS35262.1, ECO:0000313|Proteomes:UP000215527};
RN   [1] {ECO:0000313|EMBL:OXS35262.1, ECO:0000313|Proteomes:UP000215527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XY006 {ECO:0000313|EMBL:OXS35262.1,
RC   ECO:0000313|Proteomes:UP000215527};
RA   Shan W., Liu H., Zhou Y., Yu X.;
RT   "Draft Genome Sequence of Streptomyces sp. XY006, an Endophyte Isolated
RT   from Tea (Camellia sinensis).";
RL   Submitted (JUL-2017) 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:OXS35262.1}.
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DR   EMBL; NOKT01000008; OXS35262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231PKR8; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000215527; 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; 2.
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}.
FT   DOMAIN          13..124
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          129..223
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          235..384
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   385 AA;  41585 MW;  23164AA8E6BEDBEC CRC64;
     MAGSADFDLY RPSEEHDMLR DAVRSLAEAK IAPHAAAVDE EARFPREALQ ALVANDLHAV
     HVPEEYGGSG ADALATVIVI EEVARVCASS SLIPAVNKLG SLPVILSGSE ELKKKYMTPL
     AKGEGMFSYC LSEPDAGSDA AGMKTRAVRD GDFWVLNGVK RWITNAGESE YYTVMAVTDP
     EKRSKGISAF VVEKSDEGVS FGAPEKKLGI KGSPTREVYL DNVRIPADRM IGEEGTGFAT
     AMKTLDHTRI TIAAQALGIA QGALDYAKGY VKERKQFGKP IADFQGIQFM LADMSMKISA
     ARALTYQAAA ASQRVDADLT YLGAAAKCFA SDVAMEVTTD AVQLLGGYGY TRDYPVERMM
     RDAKITQIYE GTNQVQRIVM ARNLP
//
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