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Database: UniProt
Entry: A0A0G3UI38_9ACTN
LinkDB: A0A0G3UI38_9ACTN
Original site: A0A0G3UI38_9ACTN 
ID   A0A0G3UI38_9ACTN        Unreviewed;       419 AA.
AC   A0A0G3UI38;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AKL65478.1};
GN   ORFNames=M444_08785 {ECO:0000313|EMBL:AKL65478.1};
OS   Streptomyces sp. Mg1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL65478.1, ECO:0000313|Proteomes:UP000035653};
RN   [1] {ECO:0000313|EMBL:AKL65478.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL65478.1,
RC   ECO:0000313|Proteomes:UP000035653};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT   Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP011664; AKL65478.1; -; Genomic_DNA.
DR   RefSeq; WP_037797291.1; NZ_CP011664.1.
DR   AlphaFoldDB; A0A0G3UI38; -.
DR   KEGG; strm:M444_08785; -.
DR   PATRIC; fig|465541.12.peg.1954; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000035653; Chromosome.
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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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:UP000035653}.
FT   DOMAIN          10..140
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          144..247
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          261..410
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   419 AA;  45606 MW;  A1DCCD496C9823C0 CRC64;
     MDFAFDARTE ELRERLLAFM DEYVYPAEPV AAEQRARLAS PWDTPAVFGE LKAEARRQGL
     WNLFFVDEHG SPGAGQGSGP GAGLTNLQYA PLAEITGRSP HLAPMATNCA APDTGNMELL
     AQFGSEEQKK QWLEPLLAGE IRSAFAMTEP EVASSDATNI ETRVERSADG DAYVVTGRKW
     FISGAMNPDC KVFIVMGKTD PEGADPRRQQ SMILVPRDTP GVEVRRAMTV YGFEDHEHGG
     HAEVVFDGAR VPAANLIGEE GAGFAIAQAR LGPGRIHHCM RLIGMAERAI ELMCRRAIGR
     TAFGKELAAQ GVVQNWIADA RVTVEQLRLL VLKTAWLMDT VGNRGAHTEI QAIKIATPRA
     VVGILDQAVQ LHGAGGVSQD FPLAELWAAA RTLRLADGPD EVHQRSLAHR ELKKYAGLR
//
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