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Database: UniProt
Entry: A0A367BAF2_9ACTN
LinkDB: A0A367BAF2_9ACTN
Original site: A0A367BAF2_9ACTN 
ID   A0A367BAF2_9ACTN        Unreviewed;       386 AA.
AC   A0A367BAF2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RBY97977.1};
GN   ORFNames=DQ237_03530 {ECO:0000313|EMBL:RBY97977.1};
OS   Blastococcus sp. TF02-8.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY97977.1, ECO:0000313|Proteomes:UP000252403};
RN   [1] {ECO:0000313|EMBL:RBY97977.1, ECO:0000313|Proteomes:UP000252403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02-8 {ECO:0000313|EMBL:RBY97977.1,
RC   ECO:0000313|Proteomes:UP000252403};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Blastococcus sp. TF02-8.";
RL   Submitted (JUL-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:RBY97977.1}.
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DR   EMBL; QOHK01000001; RBY97977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367BAF2; -.
DR   OrthoDB; 2769798at2; -.
DR   Proteomes; UP000252403; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252403}.
FT   DOMAIN          14..127
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          132..228
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          284..383
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  41927 MW;  81553A75AE4E8F23 CRC64;
     MSNSLVLAPA PRSEAAERVR AEVREFLAAE LAAGSFRTHV DTWLSGVDPE FSRKLGERGW
     LGMTWPKKYG GHERTAMERY AVTEELLAAG APVAAHWIAD RQSGPNLLRY GTEKQREEIL
     PRIVRGECFF VIGMSEPDSG SDLASIRTRA SRNESGDWVV NGAKVWTSNA HASHYGIVLV
     RTSPADPANR HAGLSQLLVD LSLPGITVNP IRILDGGHHF NEVVFEDVVV PGDMLLGTEG
     DGWHQVTAEL AFERSGPERF LSTYPLIAEF GRRVVDTGDA AQLAALGRLS ARVLALRQMS
     LRIAAALDRG ELPNIPAALV KDVGTTFEAD VIEEVRRVVD VTPSLDSPDT LARALAEAQL
     HQPGFTLRGG TNEILRGIVA RGLGLR
//
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