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Database: UniProt
Entry: A0A2M9IEE0_9ACTN
LinkDB: A0A2M9IEE0_9ACTN
Original site: A0A2M9IEE0_9ACTN 
ID   A0A2M9IEE0_9ACTN        Unreviewed;       385 AA.
AC   A0A2M9IEE0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PJM92956.1};
GN   ORFNames=CG719_25090 {ECO:0000313|EMBL:PJM92956.1};
OS   Streptomyces sp. CB01373.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020325 {ECO:0000313|EMBL:PJM92956.1, ECO:0000313|Proteomes:UP000232070};
RN   [1] {ECO:0000313|Proteomes:UP000232070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01373 {ECO:0000313|Proteomes:UP000232070};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJM92956.1}.
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DR   EMBL; NNBK01000016; PJM92956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9IEE0; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000232070; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232070}.
FT   DOMAIN          13..123
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;  41361 MW;  177E23A33606273D CRC64;
     MAGSADFDLY RPSEEHGMLR DAVRSLAEAK IAPYAAVVDE EARFPQEALE ALVANDLHAV
     HVPEEYGGAG ADALATVIVI EEVARVCASS SLIPAVNKLG SLPVMLSGSE ELKKRYLTPL
     AKGNAMFSYC LSEPDAGSDA AGMKTKAVRE GDTYVLNGVK RWITNAGVSD FYTVMAVTDP
     DKRSKGISAF VVEKSDPGVS FGAPEKKLGI KGSPTREVYL DNVRIPADRM IGAEGTGFAT
     AMKTLDHTRI TIAAQALGIA QGALDYAKGY VKERKQFGKP IADFQGIQFM LADMAMKIEA
     ARNLTYAAAA KSERGDSDLT FQGAAAKCFA SDVAMEVTTD AVQLLGGYGY TRDYPVERMM
     RDAKITQIYE GTNQVQRIVM ARNLP
//
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