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Database: UniProt
Entry: A0A2A3HTA0_9ACTN
LinkDB: A0A2A3HTA0_9ACTN
Original site: A0A2A3HTA0_9ACTN 
ID   A0A2A3HTA0_9ACTN        Unreviewed;       380 AA.
AC   A0A2A3HTA0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:PBC71687.1};
GN   ORFNames=BX265_6299 {ECO:0000313|EMBL:PBC71687.1};
OS   Streptomyces sp. TLI_235.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC71687.1, ECO:0000313|Proteomes:UP000218662};
RN   [1] {ECO:0000313|EMBL:PBC71687.1, ECO:0000313|Proteomes:UP000218662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TLI_235 {ECO:0000313|EMBL:PBC71687.1,
RC   ECO:0000313|Proteomes:UP000218662};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2017) 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:PBC71687.1}.
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DR   EMBL; NSGV01000002; PBC71687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3HTA0; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000218662; 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.
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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218662}.
FT   DOMAIN          7..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          230..379
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41855 MW;  1839BC52968AA82A CRC64;
     MQREIYTEEH EAFRETVRAF LAKEVLPHQE RWEQAGIVDR EAWLAAGRHG LLGLAVPEEY
     GGGGTADFRF PAVLAEEFTR AGVSGLALGL HNDIIGPYLT SLATEEQKER WLPGFCSGDI
     VTAIAMTEPG AGSDLQGIRT TAVDEGDHYL LNGSKTFISN GIISDLVVVV ARTTPEGGAH
     GLSLLVVERG MPGFERGRNL DKIGQKAQDT AELFFDDVRV PKANLLGEEN QGFVYLMRNL
     AQERLTIAVS AIAGAEHLLE LTTRYVQQRT AFGKPLAKLQ HVRFEIAELA TECAVTRTFV
     DRCITEHNRY ALTPVDASMA KWWATELQKR TADRCLQLHG GYGYMAEYPV AKAFTDGRIQ
     TIYGGTTEIM KEIIGRSLLG
//
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