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Database: UniProt
Entry: A0A3R9UYK6_9ACTN
LinkDB: A0A3R9UYK6_9ACTN
Original site: A0A3R9UYK6_9ACTN 
ID   A0A3R9UYK6_9ACTN        Unreviewed;       569 AA.
AC   A0A3R9UYK6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   08-NOV-2023, entry version 15.
DE   SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:RSS05416.1};
GN   ORFNames=EF917_09690 {ECO:0000313|EMBL:RSS05416.1};
OS   Streptomyces sp. WAC00469.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2487415 {ECO:0000313|EMBL:RSS05416.1, ECO:0000313|Proteomes:UP000269080};
RN   [1] {ECO:0000313|EMBL:RSS05416.1, ECO:0000313|Proteomes:UP000269080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC00469 {ECO:0000313|EMBL:RSS05416.1,
RC   ECO:0000313|Proteomes:UP000269080};
RA   Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT   "Unmasking the antibiotic production potential of Actinomycetes through
RT   CRISPR/Cas9 inactivation of ubiquitous gene clusters.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RSS05416.1}.
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DR   EMBL; RPRX01000023; RSS05416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9UYK6; -.
DR   OrthoDB; 9771038at2; -.
DR   Proteomes; UP000269080; 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; 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:UP000269080}.
FT   DOMAIN          35..189
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          203..298
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          308..464
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  60810 MW;  91AABEF12D4380D0 CRC64;
     MASPLARERQ QRPQDGPPAP AGRGGGSGAT HEVTNQPPPL APYDAADDAA LLEGLRREGA
     GWAEEQVRRL GELAGGPEAQ EWAEQANRHE PELRTHDRYG HRIDEVDFHP SWHDLMRTAV
     GEGLAGAPWA DERPGAHVAR TAGGLVWGHT DAGHMCPVSM TYAAVPALRA QPDLAAVYEP
     LLAGRTYEPG LRVPAEKPGL LAGMGMTEKQ GGSDVRTNTT TATPTAEPGV YTLRGHKWFT
     SAPMCDVFLV LAQAPGGLSC FLVPRVLPDG SRNPFRIQRL KDKLGNRSNA SCEPEFDGTV
     AWLVGPEGRG VKTIIEMVNC TRLDCVMMSA ALMRKTLVEA GHHARHRRAF GALLADQPLM
     RNVLADLALE SEAATTLTLR LAGAADRAVR GDAAETAFRR IATAVGKYWV TKRGPAFTAE
     ALECLGGNGY VEESGMPRHY REAPVLSIWE GSGNVNALDV LRAVGREPGT AEALFAELEL
     ARGADARLDA AVTRLKNELV EASPLRARRL VELMALTLQA SLLVRHAPSS VADAFCATRL
     GGDWGHCFGT LPDSADVTGI LARALPGTV
//
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