ID A0A1Q5E845_9ACTN Unreviewed; 552 AA.
AC A0A1Q5E845;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OKJ04240.1};
GN ORFNames=AMK18_03415 {ECO:0000313|EMBL:OKJ04240.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKJ04240.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKJ04240.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKJ04240.1,
RC ECO:0000313|Proteomes:UP000186839};
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 -!- 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:OKJ04240.1}.
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DR EMBL; LISW01000001; OKJ04240.1; -; Genomic_DNA.
DR RefSeq; WP_073861584.1; NZ_LISW01000001.1.
DR AlphaFoldDB; A0A1Q5E845; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000186839; 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; 2.40.110.20; -; 1.
DR Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF3; ACYL-COA DEHYDROGENASE AIDB-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 1.
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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000186839}.
FT DOMAIN 20..173
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 188..282
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 292..448
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 59381 MW; 51E1657FD697BDD5 CRC64;
MPETVAPRSN PTAATHEVTN QAPPLTGHDA ADDAVLLEGL RREGAEWHTE ELHRLGRLVG
SAQAQEWAEQ ANTNEPVLRT HDRYGNRVDE VDFHPAYHHL MNASVSAGLA GAAWADERPG
AHVARAAGFM VMSTLEAGHL CPVSMTYAVV PALRHAPDLA KTYEPLLTSR VYEAGLRTPA
EKPGLLAGMG MTEKQGGTDV RANTTAATEA GDGTWRLRGH KWFTSAPMND LFLVLAQTPG
GLSCFLVPRV LPDGSRNTFR IQRLKDKLGN RSNASSEPEF DDTVAWLVGP EGKGVRTIID
MVTMTRLDCV IGSAAGIRAA LAQAAHHVRH RSVFGAKLID QPLMRNVIGD LAVESEAATT
LGLRLAGAAD RAQRGDAQER AFLRLATAVS KYWVCKRQPV AVAEALECLG GNGYVEDSGM
PRMYREAPLN GIWEGSGNVN ALDLLRALAR EPESLDAFRA EVEAASGADR RLDAAWQELR
GELVLTEDAP LRARRLIERA ALVLQGSLLV RHAPTAVADA FCASRLAGDR GLAFGTLAPD
TDFAGLLERL PA
//
