ID A0A1Q3S8E5_9BURK Unreviewed; 549 AA. AC A0A1Q3S8E5; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 11-DEC-2019, entry version 12. DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:OJV72678.1}; GN ORFNames=BGO22_10720 {ECO:0000313|EMBL:OJV72678.1}; OS Hydrogenophaga sp. 70-12. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hydrogenophaga. OX NCBI_TaxID=1895769 {ECO:0000313|EMBL:OJV72678.1, ECO:0000313|Proteomes:UP000186676}; RN [1] {ECO:0000313|EMBL:OJV72678.1, ECO:0000313|Proteomes:UP000186676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-12 {ECO:0000313|EMBL:OJV72678.1}; RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K., RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.; RT "Genome-resolved meta-omics ties microbial dynamics to process performance RT in biotechnology for thiocyanate degradation."; RL Submitted (SEP-2016) 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:OJV72678.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MKSS01000008; OJV72678.1; -; Genomic_DNA. DR Proteomes; UP000186676; 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 InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR InterPro; IPR041504; AidB_N. 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; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU362125}; KW Flavoprotein {ECO:0000256|RuleBase:RU362125}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}. FT DOMAIN 9..167 FT /note="AidB_N" FT /evidence="ECO:0000259|Pfam:PF18158" FT DOMAIN 181..277 FT /note="Acyl-CoA_dh_M" FT /evidence="ECO:0000259|Pfam:PF02770" FT DOMAIN 289..446 FT /note="Acyl-CoA_dh_1" FT /evidence="ECO:0000259|Pfam:PF00441" FT REGION 183..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 549 AA; 58977 MW; 5ACCB6948308B7D1 CRC64; MLSTHEVFNQ PAPLVDVNLF DTNRALQAAL AFNAPGLDTA GLRALGATVG SAGMQAHARL ANVFTPQLKT HSRVGERIDQ VEFHPSYHAL MREAVGAGLH GAAFGAAEQA SGNAHLRRAA GFMLFTELEP SVLCPISMSY AVTPALQDNA AIYRDWAPQL TSRDYDPALK LWRDKPGATM GMGMTEKQGG SDVRANTTRA EPAGRDGWGQ RFAVTGHKWF FSAPMCDAFL ILAQTASGLS CLFLPRVLPD GSLNAIRIQR LKDKLGNKAN ASSEVEFLGA TAWLVGEEGR GVPQILAMGT MTRLDCALGT SGLMRQALSI ALNHTTQRKA FGKFLIDQPL MKNVLADLAL ESEAATALAL RLARAFDRQH DPHEQVMARL LTPVAKFWIC KRGSHFAQEA MECLGGNGYV EEGGEGIMAR IYREMPLNSI WEGAGNIMAL DLLRAIRKAD AAAALAQELA PARGQHAALD HLAARLPLRV EEMATEMEAR RLAQDVALAV QAALLAQTAP AAVFNAFCDS RLGGHWGHSF GSLSAGTGVD AIIERAMPR //