ID A0A0X3VBY0_9ACTN Unreviewed; 557 AA.
AC A0A0X3VBY0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=DNA alkylation response protein {ECO:0000313|EMBL:KUL40806.1};
GN ORFNames=ADL12_12735 {ECO:0000313|EMBL:KUL40806.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL40806.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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}.
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:KUL40806.1}.
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DR EMBL; LLZG01000073; KUL40806.1; -; Genomic_DNA.
DR RefSeq; WP_062701687.1; NZ_LLZG01000073.1.
DR AlphaFoldDB; A0A0X3VBY0; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000053923; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053923}.
FT DOMAIN 20..174
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 188..283
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 293..452
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 59782 MW; 87F3EB4B556378F2 CRC64;
MVSIPAQELS GQYATHDVTN QPSPLAPYDA SEDTALLEGL RREGAGWAEE GIRRLGLRAG
SAEAQEWGEQ ANRHEPELRT HDRYGHRVDE VEFHPSWHHL MRVAVAEGLA AAPWADERPG
AHVARTAGGL VWGHTEAGHG CPTSMTYAAV PVLRRQPELA KVYEPLLTSR EYDPELRVPT
EKRGLLAGMG MTEKQGGSDV RTNTTTATPT AEPGVYTLRG HKWFTSAPMC DVFLVLAQAP
GGLSCFLVPR VLPDGSRNTF RIQRLKDKLG NRSNASSEPE FDGTVAWLVG PEGRGVKTII
EMVNCTRLDC VMSSATLMRK TLVEAGHHVR HRSAFGAPLI DQPLMRNVLA DLALESEAAT
TLTLRLAGAA DRAVRGDDVD GAETAFRRIA TAVGKYWVTK RGPAFTAEAL ECLGGNGYVE
ESGMPRHYRE APLLSIWEGS GNVNALDVLR ALSREPGTAE TLFAELALAQ GADARLDAAI
TRLKGLLTAG SEAGARRLVE LMALTLQASL LVRHAPTAVA DTFCASRLGG DWGHAFGTLP
DAADVDAILG RALPGGA
//
