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Database: UniProt
Entry: A0A3E0HE51_9PSEU
LinkDB: A0A3E0HE51_9PSEU
Original site: A0A3E0HE51_9PSEU 
ID   A0A3E0HE51_9PSEU        Unreviewed;       380 AA.
AC   A0A3E0HE51;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:REH43544.1};
GN   ORFNames=BCF44_10987 {ECO:0000313|EMBL:REH43544.1};
OS   Kutzneria buriramensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1045776 {ECO:0000313|EMBL:REH43544.1, ECO:0000313|Proteomes:UP000256269};
RN   [1] {ECO:0000313|EMBL:REH43544.1, ECO:0000313|Proteomes:UP000256269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45791 {ECO:0000313|EMBL:REH43544.1,
RC   ECO:0000313|Proteomes:UP000256269};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (AUG-2018) 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:REH43544.1}.
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DR   EMBL; QUNO01000009; REH43544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0HE51; -.
DR   OrthoDB; 5241155at2; -.
DR   Proteomes; UP000256269; 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; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          5..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..216
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41371 MW;  2152247DD7834D0F CRC64;
     MREWTDDQRA LREHYAGVVA AWGEDHIRRD QDGEFPQEIW KLVAESGLLG LPFDPEWGGQ
     GQDLLTVMHV LEELGLSCRD GGLNFSIATH LVSTGIPLQR FGSSQLKARY LTRICDGSAI
     GAHAITEPRG GSDVAGMVTT ARQDGDAFVL SGQKSFVSCG PVADLFVVYA RTQQGAGPFG
     ITAFLVERAT PGLTVGPSAD KMGLRTSPFG ELLLDGCVVP RQNVLGQVGN GFFVLDYVMK
     WEILCSFVIT LGAMRNRLAR CVEYARTRTQ FGRKIGGYQL VADMIVDMKI GVETSSRWLY
     DTAERFLAGA SVMQEIAITK LLVSEANLRS ATNAVRIFGG RGYLTEYGVE KELRDAVGGT
     IYSGTSEIQR DKIARMLGVA
//
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