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Database: UniProt
Entry: A4FH69_SACEN
LinkDB: A4FH69_SACEN
Original site: A4FH69_SACEN 
ID   A4FH69_SACEN            Unreviewed;       406 AA.
AC   A4FH69;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CAM03394.1};
DE            EC=1.3.99.3 {ECO:0000313|EMBL:CAM03394.1};
GN   Name=fadE1 {ECO:0000313|EMBL:CAM03394.1};
GN   OrderedLocusNames=SACE_4125 {ECO:0000313|EMBL:CAM03394.1};
GN   ORFNames=A8924_4513 {ECO:0000313|EMBL:PFG97094.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM03394.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAM03394.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAM03394.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG97094.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG97094.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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}.
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DR   EMBL; AM420293; CAM03394.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG97094.1; -; Genomic_DNA.
DR   RefSeq; WP_009947026.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FH69; -.
DR   STRING; 405948.SACE_4125; -.
DR   KEGG; sen:SACE_4125; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_1_0_11; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; 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; 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   ECO:0000313|EMBL:CAM03394.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN          12..123
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          128..224
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          236..383
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   406 AA;  44279 MW;  CBC7CE475D396E8A CRC64;
     MTAEPNAPGR ARELARRVRE FVDTHVVPAE PEMFASREVC AELLVELQSK ARSQGLWGIG
     YPASLGGAGL PLTSYLLVAE QEGRSFYGPA VFGAETVVDV HMLDRFATPQ VRERFLLPTV
     RGEAVPSYGM TEPGKTGSEV SGFTTEVRFE PDRCTVRGRK WFISNADRAT FMTVMARSEG
     LGKHPKDAFS LVVVPTDATG FGIVRELPVL GHFTGQCEVE LRDVQVPHSH VVGERGAGLA
     VVQQRLGLAR TVRSMHWLGQ AQRGFDLMCR RLRSRRVQGG HLADKQLLGQ HVADSYAEIS
     AARALVRRAA ARIDQGRLHV DLGVAKLAAS RTAVAVLDRA VQVHGAEGLC DDTPLSVMYR
     AARSTRIYDG ADEVQISQMA PRILKTYADS DGFDFTDPVD DFAAPA
//
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