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Database: UniProt
Entry: A0A2S4Y2L8_9ACTN
LinkDB: A0A2S4Y2L8_9ACTN
Original site: A0A2S4Y2L8_9ACTN 
ID   A0A2S4Y2L8_9ACTN        Unreviewed;       409 AA.
AC   A0A2S4Y2L8;
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:POX43028.1};
GN   ORFNames=C3486_02065 {ECO:0000313|EMBL:POX43028.1};
OS   Streptomyces sp. Ru73.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080748 {ECO:0000313|EMBL:POX43028.1, ECO:0000313|Proteomes:UP000236956};
RN   [1] {ECO:0000313|EMBL:POX43028.1, ECO:0000313|Proteomes:UP000236956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru73 {ECO:0000313|EMBL:POX43028.1,
RC   ECO:0000313|Proteomes:UP000236956};
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:POX43028.1}.
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DR   EMBL; PQSQ01000003; POX43028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4Y2L8; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000236956; 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   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:UP000236956}.
FT   DOMAIN          8..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          227..373
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   409 AA;  44414 MW;  995FAC2F075ECFE4 CRC64;
     MSAPYLTGDH EDLRQHVRDF AETEITAHVA RMESSRSVEE DLATRIAQQG WLGATIHPAF
     GGMGAGHMAK TIIIEEISRV SGAMGAMVQA SQLGTAKIIH FGSEEQRKTW LPQIAAGTCL
     PTIAVTEEGC GGHVLAMRAT ARRDGDNYIL NGRKTYVGNS HIGHLHGVVA RTGHGTKGLS
     AFLVEADRSG VILPDHPQSM GLHGFSFGEI VFDNCRIPAA NRLGQEGQGL DVAYSSSILY
     GRPNLGAVAL GIHQAIMEQT RKFVTERQRY GGPLAKLPAI QQKLGEMQSH LMTARLTAYH
     AAHLLDHGQP CDAELINAKH VNVRAARDSA RLAMDIHAAA GLFTTHPLER FFRDVEHLYA
     PAGTGEIQQH RLSEISLGTY RSQWSVRLAA VTSLRGTTGR ELHHHRISA
//
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