ID A0A2T7UWE2_9RHOB Unreviewed; 527 AA.
AC A0A2T7UWE2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:PVE49002.1};
GN ORFNames=DDE23_00920 {ECO:0000313|EMBL:PVE49002.1};
OS Pararhodobacter aggregans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=404875 {ECO:0000313|EMBL:PVE49002.1, ECO:0000313|Proteomes:UP000244810};
RN [1] {ECO:0000313|EMBL:PVE49002.1, ECO:0000313|Proteomes:UP000244810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-19 {ECO:0000313|EMBL:PVE49002.1,
RC ECO:0000313|Proteomes:UP000244810};
RX PubMed=21959289; DOI=10.1016/j.syapm.2011.08.006;
RA Foesel B.U., Drake H.L., Schramm A.;
RT "Defluviimonas denitrificans gen. nov., sp. nov., and Pararhodobacter
RT aggregans gen. nov., sp. nov., non-phototrophic Rhodobacteraceae from the
RT biofilter of a marine aquaculture.";
RL Syst. Appl. Microbiol. 34:498-502(2011).
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:PVE49002.1}.
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DR EMBL; QDDR01000001; PVE49002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7UWE2; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000244810; 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:UP000244810}.
FT DOMAIN 20..163
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 177..270
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 280..431
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 527 AA; 56888 MW; 93A3FD86272383B3 CRC64;
MTASEPRGQL RTHEVFNQPA IPGRDPWAED PTLRRILGAD PGLAAFGAAL ASDEIREAAR
DAQTQLPQLR SFDRNGRRLD EVHFHPGYHR LMALGLEAGY AATAWDGTGS HLRHAAINYL
LSQVEPGVCC PMTMTYAGIP ALNADPGLAA LWQPKLAAAA YDPRSIPVDR KRAATLGMAM
TEKQGGSDVR ANATVAVRDG EFYRLTGHKW FCSAPMCDGF LTLAQLDGAI TCFLVPRWLP
DGTRNAFTLL RLKDKLGNKA NASSEIEYDG TLAHLLGEPG RGVQTIIEMV HHTRLDTAIA
PAGLMRAALG EALSWARGRS AFQKRLIDQP LMRAVLADLG LEAEAALLLA LDVARAFDDP
ARRPYARIAV ALAKFVSNKA APGMIYECME ALGGMGYVEE TPLPMLYREA PLNSIWEGSG
NVICLDILRT LMKEPEAGAQ LTARLEAARG LDPRYDAALA AHRERWPALP TEAEARWFAE
SLGVLLTGAV MLAESPLAGE WLATRLGPRG RVAGAVAIDA DKVLAAL
//
