ID A0A0Q8V2A6_9MICO Unreviewed; 544 AA.
AC A0A0Q8V2A6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA alkylation response protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASE16_12760 {ECO:0000313|EMBL:KRC49587.1};
OS Leifsonia sp. Root227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC49587.1, ECO:0000313|Proteomes:UP000051819};
RN [1] {ECO:0000313|EMBL:KRC49587.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC49587.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC49587.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC49587.1,
RC ECO:0000313|Proteomes:UP000051819};
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:KRC49587.1}.
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DR EMBL; LMIO01000003; KRC49587.1; -; Genomic_DNA.
DR RefSeq; WP_055895465.1; NZ_LMIO01000003.1.
DR AlphaFoldDB; A0A0Q8V2A6; -.
DR STRING; 1736496.ASE16_12760; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000051819; 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.
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:UP000051819}.
FT DOMAIN 8..165
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 177..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 281..435
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 544 AA; 57882 MW; 04D19EDF389BF060 CRC64;
MATHAVTNQP PPRVDLDEFA ANIPLAEGVD RHDAGWARAD LAAVGRLVGS ARFQRDAELA
NVHEPELRAF DRWGNRIDEV QYDPSYHRVL GEAVAAGAHT SAFAEPCPGA NVARAAAFML
FAQGEAGHAC PVSMTHAAVP AIVASASPDL AATWLPRLLS REYDPALGAG KRSALFGMAM
TEKQGGSDVR ANTTMAVPDG DGRHLLTGHK WFCSAPMSDA FLVLAQTASG LSCFLVPRVL
DDGSRNVFAI QRLKDKLGNR SNASSEIEFD GTVGHLLGEE GRGVRTILEM VNRTRLDCIL
GSAAGMRQSV AEAVWHVRHR SAFGARLIDQ PAMTAVIADL ALESEAATAV ALRLARAHDD
DATDAERAFR RLATAVTKYW VCKRGPGHAY EAMECLGGNG YTEAFPLARR YREQPVMAIW
EGSGNVIALD VLRALQREPE RLEAFDGELA AARGVHPGFD AHHDAVRATV AGLARSDPLD
AQAAVRPLVA SLALALQASL LLRHAPDAVG VAFVDARLGD ARGALYGELP PAARAAIPAL
VARA
//
