ID D9T0A0_MICAI Unreviewed; 663 AA.
AC D9T0A0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Acyl-CoA oxidase domain-containing protein {ECO:0000313|EMBL:ADL47336.1};
GN OrderedLocusNames=Micau_3812 {ECO:0000313|EMBL:ADL47336.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL47336.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL47336.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) 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; CP002162; ADL47336.1; -; Genomic_DNA.
DR RefSeq; WP_013286960.1; NC_014391.1.
DR AlphaFoldDB; D9T0A0; -.
DR STRING; 644283.Micau_3812; -.
DR KEGG; mau:Micau_3812; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_014629_4_0_11; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000001908; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908}.
FT DOMAIN 24..130
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 135..244
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 278..440
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 500..638
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 663 AA; 72468 MW; FE08D7A4ACFC2F62 CRC64;
MLDHASRRID IARLQETLDG PWAEVRQAHR KHLDERFLPV YGETGDQARE RITRLLGELP
VELGIAAGFP PEYGGRSDIG ASIVATEMLA QVDLSLMVKA GVQWGLFGGA VAALGTKRHH
DAYLRDIVEG RIFGCFAMTE TGHGSDVQQL RTTCVYDPQT RTFDLHTPHE AARKDYIGNA
ARDGRMAVVF AQLISGGRRH GVHAWLVPIR DEHGNPMPGV TIGDAGPKAG LLGVDNGRLS
FDHVRVPRDM LLDRYAQVAE DGTYSSAIEN DSRRFFTMLG TLVRGRVSVG GAASAATKAA
LAIAVRYGDI RRQFSDAEGD REVLLNDYLA HQRKLLPALA TTYALHFAQT ELVAALDEIQ
GGDGPVDEHR QRELESRAAG LKAAQTWHAT RTIQACREAC GGAGYLSENR LPSLKADTDV
FTTFEGDNTV LLQLVAKGLL TGYRDEFGSL DGWGRASFVA EQVREMVLER TAARALIARL
VGAVPGRDDE VAVTDRGWQL KVFEDREEHL LDSAVRRLRG GASTKKDRPF DIFNDVQDHV
LAVAAAHVDR VTLEAFVAGI DATADPAVKE LLSRVCDLYA LSVIEANKGW LMEHGRLTPA
RSKAITGVVN GLLKELRPYM RTLVDGFAIP DAWLHAAILR EEPARQETMA AHDAATDPRS
APV
//
