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Database: UniProt
Entry: A0A1R1SBK3_9ACTN
LinkDB: A0A1R1SBK3_9ACTN
Original site: A0A1R1SBK3_9ACTN 
ID   A0A1R1SBK3_9ACTN        Unreviewed;       408 AA.
AC   A0A1R1SBK3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Type 2 domain-containing Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OMI35602.1};
GN   ORFNames=SPAR_30571 {ECO:0000313|EMBL:OMI35602.1};
OS   Streptomyces sparsogenes DSM 40356.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI35602.1, ECO:0000313|Proteomes:UP000186168};
RN   [1] {ECO:0000313|EMBL:OMI35602.1, ECO:0000313|Proteomes:UP000186168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI35602.1,
RC   ECO:0000313|Proteomes:UP000186168};
RA   Coyne S., Seebeck F.P.;
RT   "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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:OMI35602.1}.
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DR   EMBL; ASQP01000392; OMI35602.1; -; Genomic_DNA.
DR   RefSeq; WP_076971406.1; NZ_ASQP01000392.1.
DR   AlphaFoldDB; A0A1R1SBK3; -.
DR   Proteomes; UP000186168; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; 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; 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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186168}.
FT   DOMAIN          21..99
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          242..380
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   408 AA;  43088 MW;  E56D73139B327061 CRC64;
     MTTVDEAIDA GTGHDHWLRI AREIADDLAT DAVDREQAGK APFDEVARLR EAGLLTLPAP
     AGHGAGDAGG ADWRTAYAVV RTISAADGAI GYLLGCHYFL SSSARFFAGP ALATRVEHES
     AARQWWWGGG LVSCEPTPRL TPTARGYVLD GRQSCVTGVG IADRLVVRAT RSGSGDPLAV
     LVDPAHPGVV YVDDDTFGQR LAAGGSVEFD SVPVAADDVF GSLSSDEGAL PPFAGLAAPT
     ARLVSVQFCL GVAEGLLAEV REYSRVVNSS WQPSAQQPWP GSPSRDPYVL SVYGELTVAA
     RSASALADQA VEALVRGFAH GEDLDDDECA EIAVLASVAE SAASRAALEI TTRALDVIGA
     RAAFLRHGFD RFWRNARTHT LREPVADRLR EVGDYFLNGA HPPFTIPS
//
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