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Database: UniProt
Entry: A0A2S4Z2A1_9ACTN
LinkDB: A0A2S4Z2A1_9ACTN
Original site: A0A2S4Z2A1_9ACTN 
ID   A0A2S4Z2A1_9ACTN        Unreviewed;       385 AA.
AC   A0A2S4Z2A1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:POX55104.1};
GN   ORFNames=C3489_12390 {ECO:0000313|EMBL:POX55104.1};
OS   Streptomyces sp. Ru71.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX55104.1, ECO:0000313|Proteomes:UP000237414};
RN   [1] {ECO:0000313|EMBL:POX55104.1, ECO:0000313|Proteomes:UP000237414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru71 {ECO:0000313|EMBL:POX55104.1,
RC   ECO:0000313|Proteomes:UP000237414};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-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:POX55104.1}.
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DR   EMBL; PQSS01000015; POX55104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4Z2A1; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000237414; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; 2.
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, 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:UP000237414}.
FT   DOMAIN          13..122
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          130..225
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          237..385
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   385 AA;  42417 MW;  642C4AEC51494AC6 CRC64;
     MSELPTELVP LSREQRDIID LTRSFAQEEI RPRARAVDEA DTETPWDLWR KAAKVGITGF
     MLPAEYGGGG FTDVFTQVLV QEELCVGDLG IGNLLCSNGF FADPLLELGT EEQKRTWLTP
     LTGPDTPMTA LATTEPGAGS DAASITTTAT RTTGGYRLNG QKAWISNAGE ADQYVVFAKT
     DPTQRSRGVT AFLLRKGTAG MEFGEPMRKM GQRAIVCREI FLNDVLVPEE DRLGEEGRGF
     HGLMRTFDIS RTVLGAAATG VARAAYEYAR DYAKNRVQFG KPVIEHQAVA FRLADMRTRI
     EQARLMTWRA AKRLDAGLDA TAQAAMAKLT ASETAAHCTW AAVQTLGGWG YSREYPVEQW
     MRDAKLEEIE EGTSDIMRLV ISRSM
//
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