ID A0A1C4QUF7_9ACTN Unreviewed; 626 AA.
AC A0A1C4QUF7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-coenzyme A oxidase {ECO:0000313|EMBL:SCE26297.1};
GN ORFNames=GA0115242_12749 {ECO:0000313|EMBL:SCE26297.1};
OS Streptomyces sp. SolWspMP-5a-2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCE26297.1, ECO:0000313|Proteomes:UP000199131};
RN [1] {ECO:0000313|EMBL:SCE26297.1, ECO:0000313|Proteomes:UP000199131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCE26297.1,
RC ECO:0000313|Proteomes:UP000199131};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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DR EMBL; FMCI01000256; SCE26297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4QUF7; -.
DR Proteomes; UP000199131; 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; 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; 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; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909:SF382; ACYL-COENZYME A OXIDASE; 1.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 2.
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:ARBA00022827}.
FT DOMAIN 294..433
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 467..605
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 626 AA; 68652 MW; 29F73A16D72120D1 CRC64;
MISTAAVEIA RTEGDLHTDD MPLLPDPALA SRLTDVLFAG RFDELHRPWT ELLRREVFRY
RDGLSQEARS ELAYERLRIV NRDIESVEDL VTDTSRLVAL HEWLGVVDGS LTTLATVHYN
LFLGSLLGLD PLGKVDRTPF TTLDQYGTVL ITELGYGNNA ARLETTATHH PESDTFVLTT
PSRDAQKFMP NTGPVGGDKS GLVAARLVAR GQDHGVFLFL VPLRDERGPL PGIRIRPLSQ
TPGSAVDHAI TSFDHVRLDR TALLTGDHAD LDPDGTFHSA IRNRRQRFLR SIHRVTTGKL
CLAAAALSGA RATLTIAVRH AHRRHTSAPG SHSHVPVFAH RGHQSRLLAA TARAYAATLL
MREVVRRRSD PNDPRPTETE VLVPIVKGWA TWQARDIVTE CRERCGAQGL LSANRIVDLL
TPIEGAITAE GDNLVIWTKA AADLLTGRGY EPPRPPPAGP VDPADPEAVL DLLVHHELTC
LARAGDRLAE PADDPLERWN HAVDPALELV EAHVTRRAAE SFLAASRRPA DPATRALLAQ
TLHLFALEIL TPHTGPLLAD GHLTADAVRA LPRTVERLRT RLAPHALTLV EAFAVPDTIL
EAPIATDRYA RTYDDPHGPW QSKPSE
//