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
//