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Database: UniProt
Entry: A0A0X3XNZ3_9ACTN
LinkDB: A0A0X3XNZ3_9ACTN
Original site: A0A0X3XNZ3_9ACTN 
ID   A0A0X3XNZ3_9ACTN        Unreviewed;       386 AA.
AC   A0A0X3XNZ3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KUL73448.1};
GN   ORFNames=ADL34_20025 {ECO:0000313|EMBL:KUL73448.1};
OS   Streptomyces sp. NRRL WC-3605.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL73448.1, ECO:0000313|Proteomes:UP000052945};
RN   [1] {ECO:0000313|EMBL:KUL73448.1, ECO:0000313|Proteomes:UP000052945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL73448.1,
RC   ECO:0000313|Proteomes:UP000052945};
RA   Gilbert D.G.;
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:KUL73448.1}.
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DR   EMBL; LLZN01000062; KUL73448.1; -; Genomic_DNA.
DR   RefSeq; WP_062670219.1; NZ_LLZN01000062.1.
DR   AlphaFoldDB; A0A0X3XNZ3; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000052945; 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   PIRSF; PIRSF016578; HsaA; 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:UP000052945}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..222
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          234..382
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  41702 MW;  CC2462DA153F7435 CRC64;
     MDHRLSPELE DLRRTVEEFA HDVVAPKIGD FYERHEFPYE IVREMGRMGL FGLPFPEEHG
     GMGGDYLALG IALEELARVD SSVAITLEAG VSLGAMPIHL FGTEEQKRTW LPKLCSGEIL
     GAFGLTEPDG GSDAGATRTT ARLDESTGEW VINGTKCFIT NSGTDITGLV TVTAVTGRKP
     DGKPLISSII VPSGTPGFTV AAPYSKVGWN ASDTRELSFV DVRVPAANLL GQEGRGYAQF
     LRILDEGRIA IAALATGLAQ GCVDESVKYA KERHAFGRPI GSNQAIQFKI ADMEMKAHTA
     RLAWRDAASR LVAGEPFKKE AALAKLYSST VAVDNARDAT QVHGGYGFMN EYPVARMWRD
     SKILEIGEGT SEVQRMLIAR ELGLAG
//
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