ID A0A0U3Q058_9ACTN Unreviewed; 559 AA.
AC A0A0U3Q058;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:ALV37285.1};
GN ORFNames=AS200_38240 {ECO:0000313|EMBL:ALV37285.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV37285.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV37285.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV37285.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; CP013743; ALV37285.1; -; Genomic_DNA.
DR RefSeq; WP_058926865.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3Q058; -.
DR STRING; 1725411.AS200_38240; -.
DR KEGG; scx:AS200_38240; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000068029; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR CDD; cd01154; AidB; 1.
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; IPR034184; AidB.
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:UP000068029}.
FT DOMAIN 21..175
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 189..284
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 294..450
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 60069 MW; AD68075E042F7399 CRC64;
MVSTPSPARP QPQYATHDVT NQPPPLTPYD ASEDTALLEG LRREGAGWAE EDVRRLGLRA
ASAEAQEWAE LANVHEPVLR THDRYGNRID EVDFHPAWHH LMRTAVAEGL AGAPWADARP
GAHVARTAGG LVWGHTDAGH GCPTSMTYAA VPALRAQPDL AEVYEPLLTA REYDPALRVP
TEKPGLLAGM GMTEKQGGSD VRTNTTTAWP TAEPGVYQLR GHKWFTSAPM CDVFLVLAQA
PEGLSCFLVP RVLPDGSRNT FRIQRLKDKL GNRSNASSEP EFDGTVAWLV GPEGRGVKTI
IEMVNCTRLD CVMMSATLMR KTLVEAGHHV RHRSAFGARL IDQPLMRNVL ADLALESEAA
TTLTLRLAGA ADRAVRGDAA EAAFRRIATA VGKYWVTKRG PAFTAEALEC LGGNGYVEES
GMPRHYREAP LLSIWEGSGN VNALDVLRAL RREPGTAQAL FDELALARGA DARLDAAVVR
LEGLVATGSE AGARRLVELM ALALQASLLV RHAPPAVADA FCATRLGGDW GHAFGTLPDA
ADLDPILERA LPDGGALLP
//