ID E8NGL3_MICTS Unreviewed; 700 AA.
AC E8NGL3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAJ74096.1};
GN OrderedLocusNames=MTES_1132 {ECO:0000313|EMBL:BAJ74096.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ74096.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ74096.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ74096.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288}.
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DR EMBL; AP012052; BAJ74096.1; -; Genomic_DNA.
DR RefSeq; WP_013584223.1; NC_015125.1.
DR AlphaFoldDB; E8NGL3; -.
DR STRING; 979556.MTES_1132; -.
DR KEGG; mts:MTES_1132; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_014629_4_0_11; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000008975; 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; 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; 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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 87..159
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 164..273
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 528..663
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 76023 MW; CF4EC9D8D9AB9832 CRC64;
MTDAAVRPTT PATSTRTPVG GAPSAPHSAA EAAEARIDID RVTDLLLGTW GDTRRQAREM
LKDPALWRDD SLGMDAHRER TLSQLHLLVQ NNAVHRAFPK RFGGEENNGA NIAGFEELVA
ADPSLQIKSG VQWGLFGSAV LQLGTAEHHD KWLPGIMSLE IPGAFAMTET GHGSDVAAIG
TTATYDPETE EFVIHTPFRG AWKDYLGNAA LHGKAATVFA QLITNGVNHG VHCFYVPLRD
EDGTFLPGIG GEDDGLKGGL NGIDNGRLHF DHVRIPRTNL LNRYGDVAAD GTYSSDIASP
GRRFFTMLGT LVQGRVSLDG AAAWASAIGL IIAITYGNQR RQFDSGSGTP EVTLLDYGKH
QRRLLPRLAT TYAEIFAHDE FLQKFDGVFS GALDTDADRE DLETLAAALK PLSTWHALDT
LQEAREACGG QGFLFENRLV GLRADLDIFV TFEGDNNILL QLVGKRLLAD YARQFKGKDA
KALAAFAVGQ TAGKLFHGAG LRQLGQAVTD LGSTARSVER GLRADQQHEL LAGRVQQMIA
DIAGRLRPAS KLSREDAAAL FNANQSELIE AARAHGELLQ WEAFTDAINR IEDRGTLQVM
TWLRDLFGLQ LIEKHLAWHL INGRLSTQRA AAVSSYIDRL CARLRPHAQD LVDAFGYGPE
HVRASIATGV EDDRQNEAAA YYAELRASGN APVPEKKPAK
//
