ID D7BTB6_STRBB Unreviewed; 599 AA.
AC D7BTB6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Acyl-CoA dehydrogenase FadE10 {ECO:0000313|EMBL:ADI05331.1};
GN Name=fadE10 {ECO:0000313|EMBL:ADI05331.1};
GN OrderedLocusNames=SBI_02210 {ECO:0000313|EMBL:ADI05331.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI05331.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI05331.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI05331.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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}.
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DR EMBL; CP002047; ADI05331.1; -; Genomic_DNA.
DR RefSeq; WP_014174810.1; NC_016582.1.
DR AlphaFoldDB; D7BTB6; -.
DR STRING; 749414.SBI_02210; -.
DR KEGG; sbh:SBI_02210; -.
DR PATRIC; fig|749414.3.peg.2284; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_492503_0_0_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd00567; ACAD; 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; 2.
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:SF43; ACYL-COA DEHYDROGENASE; 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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:UP000000377}.
FT DOMAIN 46..133
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 155..250
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 284..414
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 564..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 65399 MW; F18492E7B0686B44 CRC64;
MSRPLNAINV PGRTSFLEEI FRGVLRLDLV HPFPVQPESD RKQGDALVAD AKEFARGLVD
PALVEKTGEL PREAIKRLRE SSYLKLQSPR KLGGLALSDL NAFRVIQAIS SWSLPLGLVV
AVQNSIGFAP LVQILPEGPL RDMLSERVAR GLISAFADTE PSGAANLRRE TVAVPTEDGH
GYLVSGEKVF SGNAPFAELL GVVATVQEDG REMRRLVVVD PDAPGVRRSA EHEFMGIKGF
PNGGFTLDRV RVPRDHVFVE KPSAHDVRIT AQAGGLAILG RMYLIAAPSL AIAKLCLEWS
RGFVRRRRVD GVPLGEYEEI QHLIGQSLAD TFALEAVAEW SLLCEDAGLN PLFEQVVAKN
LCSLLCWGVV DRTMSLFAAE GYETAASKAA RGAPPVPLER SFRDARNLRI SGGVDFQLDY
WLSKLAIFSY HRAGVLDEGQ GAEQAAEARE RLTVALTPRN QRHLAELHDS VEEFRARCAA
LAKAYPDDET LFAQEHTLIA VARWATEIMA ASLVLARAAR RTAEHDTEAQ DLADIYCTGA
LRRIAEYARE ALEEERPDTG RVTQRWITGD GHGGLLDDIV ADVTDPDTSG PDTSGPDVS
//
