ID A0A0Q8Q9V1_9ACTN Unreviewed; 544 AA.
AC A0A0Q8Q9V1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:KRB78382.1};
GN ORFNames=ASE01_03655 {ECO:0000313|EMBL:KRB78382.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB78382.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB78382.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78382.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB78382.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78382.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KRB78382.1}.
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DR EMBL; LMIA01000007; KRB78382.1; -; Genomic_DNA.
DR RefSeq; WP_056748953.1; NZ_LMIA01000007.1.
DR AlphaFoldDB; A0A0Q8Q9V1; -.
DR STRING; 1736488.ASE01_03655; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000050886; 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:UP000050886}.
FT DOMAIN 8..160
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 175..272
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..437
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 544 AA; 58652 MW; C56AAFB352C18B3D CRC64;
MTTHEVFNQV PPLVGHDTSA DPALLEGVER EGAGWALPEI QEVGRLAGTA EARDWGRLAE
RVPPRLLTHD RYGNRVDEVD YVPAYHQLME TAIGHGIHAA PWAEDRPGAH VARAAKFYAW
NVDAGHGCPI SMTYAVVPAL RANPALAAQF EPLLTNREYD FGLRDPATKR GLIAGMSMTE
KQGGSDVRAN TTAATPIAGQ SDGSYRVVGH KWFTSAPMSD MFLTLAQAPG GLSCFLLPRV
LPGGEANPIR FQRLKDKLGN RSNASSEIEY DNAIGWLVGE EGKGVKTIVE MVNMTRLDCV
IGSASGMRLA LTHAAHHARH RSAFGKPLID QPLMRNVLAD LAVESEAATT AMMRLAGAND
RAIHGDTGEA ALRRLALAAT KYYVCKRGPV LANEALECLG GNGYVEDFDL ARVYRELPLL
SIWEGSGNVA ALDALRAIGR EPESLDAFFA EADLAAGADA RYDDAVTSLK KELTNFDDIE
LRARRLVEQI AVVFQAGLLL RHAPSAVADA FCATRLARDW GSAFGTLPAG LDLAPILART
ETTF
//