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Database: UniProt
Entry: A0A1Q5I6F1_9ACTN
LinkDB: A0A1Q5I6F1_9ACTN
Original site: A0A1Q5I6F1_9ACTN 
ID   A0A1Q5I6F1_9ACTN        Unreviewed;       393 AA.
AC   A0A1Q5I6F1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OKJ52673.1};
GN   ORFNames=AMK29_31195 {ECO:0000313|EMBL:OKJ52673.1};
OS   Streptomyces sp. CB02261.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ52673.1, ECO:0000313|Proteomes:UP000186742};
RN   [1] {ECO:0000313|EMBL:OKJ52673.1, ECO:0000313|Proteomes:UP000186742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02261 {ECO:0000313|EMBL:OKJ52673.1,
RC   ECO:0000313|Proteomes:UP000186742};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ52673.1}.
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DR   EMBL; LIVX01000012; OKJ52673.1; -; Genomic_DNA.
DR   RefSeq; WP_073819509.1; NZ_LIVX01000012.1.
DR   AlphaFoldDB; A0A1Q5I6F1; -.
DR   OrthoDB; 3404950at2; -.
DR   Proteomes; UP000186742; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_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; ISOVALERYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          31..104
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          239..371
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   393 AA;  42522 MW;  542DEE421A874B35 CRC64;
     MQTIEAPPRE ELVRRATDLI PLLQRNAPVG EENRNLSQET VEALTEAGIL KMRVPHRYGG
     YQSDMRTVVD TLAELARGDG SAAWTASVWA ISSWMVGLFP DEVQDEVFST PDVRISGILS
     PTAMATPVPG GIVLNGKWSF NSGVQHSHWN TNAAILIGED GEPQPIMVAI PVSDLTIVDD
     WHTAGLRGTG SVSTIAENLF VPQERVLPMV PVLMGQHRSV LNAGSPLYSA PFMPTACATI
     SAPALGLARA AKDAFLDRLP GRKITYTAYE SQAEAPLTHL QVAEATVKID EADFHAHRAA
     AMVDTKGAAG EEWTLEERAR VRLDLGAVTQ RAKEAVDLLN TASGGSSIYS SVPIQRIERD
     VQTINLHAIL HPNTNLELYG RIVCGQEPNT VYL
//
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