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Database: UniProt
Entry: A0A0U3PHE0_9MICC
LinkDB: A0A0U3PHE0_9MICC
Original site: A0A0U3PHE0_9MICC 
ID   A0A0U3PHE0_9MICC        Unreviewed;       691 AA.
AC   A0A0U3PHE0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ALV45008.1};
GN   ORFNames=MB46_05305 {ECO:0000313|EMBL:ALV45008.1};
OS   Arthrobacter alpinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=656366 {ECO:0000313|EMBL:ALV45008.1, ECO:0000313|Proteomes:UP000055883};
RN   [1] {ECO:0000313|EMBL:ALV45008.1, ECO:0000313|Proteomes:UP000055883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3 {ECO:0000313|EMBL:ALV45008.1,
RC   ECO:0000313|Proteomes:UP000055883};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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DR   EMBL; CP013745; ALV45008.1; -; Genomic_DNA.
DR   RefSeq; WP_044575831.1; NZ_CP013745.1.
DR   AlphaFoldDB; A0A0U3PHE0; -.
DR   STRING; 656366.AS189_11320; -.
DR   KEGG; arw:MB46_05305; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000055883; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; 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; 2.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR012258; Acyl-CoA_oxidase.
DR   InterPro; IPR002655; Acyl-CoA_oxidase_C.
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; PTHR10909:SF378; ACYL-COENZYME A OXIDASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 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; PIRSF000168; Acyl-CoA_oxidase; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          60..139
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          146..256
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          290..451
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          510..650
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   691 AA;  75659 MW;  F59CE909A8DF4A55 CRC64;
     MTNVLTPVSS AAQHDGATVD VAALGELLLG KWSQVRLAAR ELAGRPELHK IEGLSHTEHR
     RRVFEQLGIL VKQNGVHRAF PTRLGGSDDH GGNVAGFEEL VLADPSLQIK GGVQWGLFGS
     AVLHLGTEEH QNKWLPGIMN LDIPGCFAMT EIGHGSDVAS IATTATYDEA TQEFVINTPF
     RAAWKEFIGN AAVDGLAAVV FAQLITKGVN HGVHALYVEL RDPETKEFRP GIQGLDDNIK
     GGLNGIDNGR LAFDNVRVPR TNLLNRYGDV AADGTYSSTI SSPGRRFFTM LGTLVQGRVS
     LNGAAVAASK VALKIAIQYA TERRQFNAAS DTEEVVLLDY QRHQRRLLPF LATTYAAAFA
     HEELLVKFDG VFSGEHDTDE DRQDLETLAA ALKSLTTWHA LDTLQECREA CGGSGFMVEN
     RFTSLRADLD VYATFEGDNT VLLQLVAKRL LADYSKEFSN LDFGVLARFV VGQAADLTLN
     KTGLRQVVQA LADTGSAQKS AKALKDEDTQ RQLLADRVQT MVAETASALK EAAKLPKDKG
     AAIFNDNQNA LIEAARAHAE LLQWEAFTTA LARIEDAGTK RILTKLRDIF GLGLIEKHLD
     WYLMNGRISM QRARTLAPYI NRLLANMRPH ALDLVDAFGY GPEHLRATIA SGIERERQDE
     ARDYFRNLRA SSDGPVDEKI LIQRAKAAAK K
//
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