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Database: UniProt
Entry: G2GLG1_9ACTN
LinkDB: G2GLG1_9ACTN
Original site: G2GLG1_9ACTN 
ID   G2GLG1_9ACTN            Unreviewed;       395 AA.
AC   G2GLG1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EGX55659.1};
GN   ORFNames=SZN_31784 {ECO:0000313|EMBL:EGX55659.1};
OS   Streptomyces zinciresistens K42.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX55659.1, ECO:0000313|Proteomes:UP000004217};
RN   [1] {ECO:0000313|EMBL:EGX55659.1, ECO:0000313|Proteomes:UP000004217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K42 {ECO:0000313|EMBL:EGX55659.1,
RC   ECO:0000313|Proteomes:UP000004217};
RA   Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL   Submitted (AUG-2011) 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:EGX55659.1}.
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DR   EMBL; AGBF01000205; EGX55659.1; -; Genomic_DNA.
DR   RefSeq; WP_007502906.1; NZ_AGBF01000205.1.
DR   AlphaFoldDB; G2GLG1; -.
DR   PATRIC; fig|700597.3.peg.6224; -.
DR   OrthoDB; 3964153at2; -.
DR   Proteomes; UP000004217; 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; 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.
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:UP000004217}.
FT   DOMAIN          29..108
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          112..207
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          219..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   395 AA;  43287 MW;  1FE36A583FE88622 CRC64;
     MTGDAAGLRR RTAALLAAHP PAGTGRLDFL RARFDAGLAW VHFPEGLGGL GLPRSLQAVV
     DAELEAAGAP GNDPRRIGIG LGMAAPTILA YGTEEQKRRH LRPLWTGEEV WCQLFSEPGA
     GSDLAALGTR AVREDGGDWV VNGQKVWTSS AHLARWAILI ARTDPDAPKH AGITYFLCDM
     SDPGVEVRPL RQITGEAEFN EVFLTDVRIP DSRRLGGIGD GWKVARTTLD NERVAIGGMR
     LPREGGMIGP VARTWRERPE LRTHELHQRL LTLWVEAEVS RLTAERLRQQ LVAGQPGPEG
     AGMKLAFARL NQEISGLEVE LRGEEGLLYD DWTMRRPELV DFTGRDAGYR YLRAKGNSIE
     GGTSEVLLNV VAERVLGLPA EPRTDKDVAW KDLAR
//
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