ID A0A1Q4DTI1_9PSEU Unreviewed; 651 AA.
AC A0A1Q4DTI1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:OJY47661.1};
GN ORFNames=BGP03_33590 {ECO:0000313|EMBL:OJY47661.1};
OS Pseudonocardia sp. 73-21.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY47661.1, ECO:0000313|Proteomes:UP000186163};
RN [1] {ECO:0000313|EMBL:OJY47661.1, ECO:0000313|Proteomes:UP000186163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-21 {ECO:0000313|EMBL:OJY47661.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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 oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288}.
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:OJY47661.1}.
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DR EMBL; MKVV01000044; OJY47661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4DTI1; -.
DR STRING; 1895809.BGP03_33590; -.
DR Proteomes; UP000186163; Unassembled WGS sequence.
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; 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 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 125..234
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 374..441
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 499..627
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 651 AA; 69816 MW; A0AC3F4461DE426D CRC64;
MSSVLQTVLD GRWAAVRDEV RAQMGEVQTD PSLPTEQYRA QIAGYVAELA KTGRPHQGFD
PAYGGGGDVG GVVAAFQMLG HGDLSLLVKA GVQWGLFGGA LQNLGTARHH DRYLRDMMDG
TLLGCFAMTE TGHGSDVQHL RTTATYDAAT QEFVIDTPEP GARKDYIGGA ARDARMAAVF
AQLITGGTSH GVHCFLVPIR SDAGDALPGV TITDCGEKAG LNGVDNGRLV FDGVRVPREA
LLNRYADVAE DGTYSSSIEN ETRRFFTMLG TLVRGRISVA GGAGTATQKA LTLAVRYGAT
RRQFSDPATG EEVVVLDYLA HQRKLLPALA TSYALHFAQE DLVGRMHDLQ KFSEGPLAGP
SSDTAPVQDE QLQRDLETRA AGIKALGTWH ATATIQACRE AAGGAGYLSE NLLPQLKADT
DVFTTFEGDN TVLLQLVAKT LLSDYARKVG KLDLLGKVRF AADLVGGEVA ERTGARSLLR
RGDVRDRAHQ RRLLVAREEH LLGSLARRMR AALKPGVDQF AIFNAAQDHL LEAARAHVDR
IVFDAFADAV DRAPSTVRGL LELVLTLHGL SVLESRRAWF LEHGYLTVSG SKALASGVNE
LCAALRPHAR DLVDGFGIPE QWLACPLLDG EQQLTTEAPA EEAPADLKAV G
//
