ID A0A0Q9KAU7_9MICO Unreviewed; 558 AA.
AC A0A0Q9KAU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:KRE36907.1};
GN ORFNames=ASG73_11290 {ECO:0000313|EMBL:KRE36907.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE36907.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE36907.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE36907.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE36907.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE36907.1,
RC ECO:0000313|Proteomes:UP000051572};
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|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {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:KRE36907.1}.
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DR EMBL; LMRZ01000005; KRE36907.1; -; Genomic_DNA.
DR RefSeq; WP_055994984.1; NZ_LMRZ01000005.1.
DR AlphaFoldDB; A0A0Q9KAU7; -.
DR STRING; 1736393.ASG73_11290; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000051572; Unassembled WGS sequence.
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 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; 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.
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}.
FT DOMAIN 8..167
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 182..283
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 293..443
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 558 AA; 59478 MW; 759FB5DB768BFAAE CRC64;
MSTHEVTNQV PPYGGHDVFG SDPVLSEGVT RWVPMPQRNE AITELTALGE LAGSSRAEQW
ADLAQRNTPR LVTHDRWGHR VDEVEFDPAW HELMSVAAGA GLTAVPWTQP PASGAHVRRA
AGFVTWSQVE PGHICPITMT NAAVPALRHS PELAVRWEGK LASREYDFGL REVQTKAGAI
AGMGMTEKQG GSDVRANSTL AVRTPGGPLT GDTYRLTGHK WFCSAPMSDV FLVLAKTSPE
AAPSCFLVPR VLEDGSRNPF ALQRLKDKLG DRSNASSEIE LDGTWGALVG EEGRGVRTII
EMVSATRLDC VLGSAATMRA ALTRAVHHTS HRRAFGATLV DQPLMRNVLT DLALESEAAT
LLGLRLAHAL DEGDTELTRL GVAVGKYWVC KRTSPFVAEA MECLGGNGYV EEHGMARLYR
QAPLNSIWEG SGNVNALDVL RAISREPASL MALLKEASTA RGHLSVLDAA LDDLERDCAG
LAALDGADIA MGARRLVERL ALTLQASLMV LHSPAEMAEA FVASRLGGAT GASFGTLDAG
LVTLSGATAI TRSNPALP
//
