ID A0A1B1B3B5_9ACTN Unreviewed; 553 AA.
AC A0A1B1B3B5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:ANP53232.1};
GN ORFNames=AVL59_30160 {ECO:0000313|EMBL:ANP53232.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP53232.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP53232.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP53232.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016279; ANP53232.1; -; Genomic_DNA.
DR RefSeq; WP_067310707.1; NZ_JAGGLP010000018.1.
DR AlphaFoldDB; A0A1B1B3B5; -.
DR STRING; 68214.AVL59_30160; -.
DR KEGG; sgs:AVL59_30160; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000092659; Chromosome.
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; PS00073; ACYL_COA_DH_2; 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 19..173
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 187..282
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 294..448
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 59424 MW; DBB4B49FD1A268E8 CRC64;
MVSIPAQSPP QSATHDVTNQ APPLAPYDAS EDHALLEGLR REGAGWAEEG IRALGVRAGG
EEAQEWGEQA NRHEPELRTH DRYGHRIDEV DFHPSWHHLM RTAVAEGLAG APWADDRSGA
HVARTAGGLV WGHTEAGHGC PTSMTYAAVP ALRAEPDLAK IYEPLLTSRV YEPGLRVPTE
KPGLLAGMGM TEKQGGSDVR TNTTTATPTG EPGVYTLRGH KWFTSAPMCD VFLVLAQAPG
GLTCFLVPRI LPDGSRNTFR VQRLKDKLGN RSNASSEPEF DRTVAWRVGP EGLGVKTIIE
MVNCTRLDCV MSSATLMRKT LVEAGHHACH RSAFGARLID QPLMRNVLAD LALESEAATT
LTLRLAGAAD RAVRGDAGER AFRRIATAVG KYWVTKRGPA FTAEALECLG GNGYVEDSGM
PRHYREAPLL SIWEGSGNVN ALDVLRALGR EPDTAEALFA ELALARGADA RLDAAVVSLR
QQLAETDQVG ARRLVERMAL ALQASLLVRH APHPVADAFC ATRLGGDWGH AFGTLPAGVG
LDAILERALP GRN
//
