ID A0A0Q7SSZ3_9BURK Unreviewed; 529 AA.
AC A0A0Q7SSZ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:KQY86046.1};
GN ORFNames=ASD35_20690 {ECO:0000313|EMBL:KQY86046.1};
OS Pelomonas sp. Root1444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY86046.1, ECO:0000313|Proteomes:UP000051648};
RN [1] {ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY86046.1, ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY86046.1,
RC ECO:0000313|Proteomes:UP000051648};
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 -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:KQY86046.1}.
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DR EMBL; LMFP01000011; KQY86046.1; -; Genomic_DNA.
DR RefSeq; WP_056875190.1; NZ_LMFP01000011.1.
DR AlphaFoldDB; A0A0Q7SSZ3; -.
DR STRING; 1736464.ASD35_20690; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000051648; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; 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; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000051648}.
FT DOMAIN 6..160
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 174..267
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 278..428
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 529 AA; 57022 MW; EC329A104D015934 CRC64;
MSTSDNLVDE WVGHNLLGTD PALLAALRGA APQAVEPLTR YGAELGSAET AQLARDANRH
GPTLRQLDAR GRRVDLVDFH PAWHQLLAMY RRQGLVADVF ATETPGRWAA FAAGCYLHGQ
VEAGSLCPAT MTQAAIPVLH QQPELFAPLR DKFFSRAHDP REAPISDKAS IWVGMGMTEK
QGGSDLRRVT TTAVAQADGS HAITGHKWFF SAPSSDAHLV LARTEAGPTC FWLPRYTPDG
TRNAVQVMRL KDKLGNRSNA SSEVEFHGAW AQRLGDEGRG IPTLIEMAGY TRLNCVIGSA
ALLRAGLVQA LHNARERFAF GRVLAEQPLM QSVLADVALE SEAAMRLMLR LARGFEQGEP
GWQRLMTPAA KLWVCKRAIE CTGEAMELLG GNGYVEDGVL ARLYREAPVN SIWEGSGNVM
ALDVLRAVAR EPDVALALLD DFAASADAPV RAEAQHLRRL LTGDPAALEP QARRVAQGLV
LCAQAVLMRE QSSTAAADAF IATRFVGDGR LIGTTAVPQA AQILQAALA
//
