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Database: UniProt
Entry: A0A0M2GVX2_9ACTN
LinkDB: A0A0M2GVX2_9ACTN
Original site: A0A0M2GVX2_9ACTN 
ID   A0A0M2GVX2_9ACTN        Unreviewed;       393 AA.
AC   A0A0M2GVX2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KJK39746.1};
GN   ORFNames=UK15_11100 {ECO:0000313|EMBL:KJK39746.1};
OS   Streptomyces variegatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK39746.1, ECO:0000313|Proteomes:UP000034786};
RN   [1] {ECO:0000313|Proteomes:UP000034786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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:KJK39746.1}.
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DR   EMBL; JYJH01000006; KJK39746.1; -; Genomic_DNA.
DR   RefSeq; WP_031134595.1; NZ_JYJH01000006.1.
DR   AlphaFoldDB; A0A0M2GVX2; -.
DR   STRING; 284040.UK15_11100; -.
DR   PATRIC; fig|284040.3.peg.6645; -.
DR   Proteomes; UP000034786; 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:SF22; BLR3437 PROTEIN; 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|RuleBase:RU362125}.
FT   DOMAIN          8..109
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          114..210
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          237..386
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   393 AA;  41377 MW;  71D57AFCADAC51E2 CRC64;
     MTAFSLEPEQ LSWCAELRTL AAERLRPLAD KGEPGHVNRP LVAELGGLGL LGRLFTSGAL
     DLCLMRESLA YACTEAETAL ALQGLGAHPV HTHGTRAQRT RWLPGVTDGT VIAAFALSEP
     GAGSDAAALE LRAEPDAAQG GRASAGTALT AAPDGTARWR LTGEKCWISN APEADFYTVF
     ARTTPGAGAR GVTAFLVPAD RPGLTGRALD MLSPHPIGAL GFDAVPVTAD DVLGEVDRGF
     RVAMGTLNLF RPSVGAFAVG MAQAALDATL AHTAGRDAFG GKLRDLQAVA HQVAEMALRT
     EAARLMVHAA ASAYDADSPE VPRRSAMAKL LATETAQYVV DTAVQLHGAR ALQRGHLLEH
     LYREVRAPRI YEGASEVQRG IIAKELYARQ EAP
//
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