ID H0QYH9_9ACTN Unreviewed; 761 AA.
AC H0QYH9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative acyl-CoA oxidase {ECO:0000313|EMBL:GAB17880.1};
GN ORFNames=GOEFS_041_00340 {ECO:0000313|EMBL:GAB17880.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB17880.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB17880.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB17880.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) 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}.
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:GAB17880.1}.
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DR EMBL; BAEH01000041; GAB17880.1; -; Genomic_DNA.
DR AlphaFoldDB; H0QYH9; -.
DR STRING; 1077974.GOEFS_041_00340; -.
DR eggNOG; COG1960; Bacteria.
DR Proteomes; UP000035034; 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; 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:UP000035034}.
FT DOMAIN 164..238
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 244..358
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 392..559
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 618..756
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 94..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 82782 MW; 015133BF671B1693 CRC64;
MTGLRGRTPG YDDREGGEYH QLTSAHVPDG TEVTIRYART CKPLLTCAHF SNRHDDTAQL
DAARTPKGSL DLNFSWRGHT LAASRLRTVR AMAASADSAG PSTTISPDET PVPDDTVIED
GLRAALDGRW RATREDLRAG LDRADLLPDP SRTLAEARTN ILAEMRELSS LNFAAAGFRT
EHGGTGDVGA SISAIEMLGY ADLSLMVKSG VQWGLFGGAV ENLGTKRHHD RYVADLISLD
LLGCFAMTET GHGSNVQALE TTATYDAAAR EFVIHSPTPS ARKDYIGGAA EHARVAAVFA
QLITGGPGEE PTGHGVHCFI VPIRDENGAD LPGVTTGDCG YKGGLSAVDN GRISFDQVRI
PAENLLNKYG DVAADGTYSS PIENINRRFF TMLGTLIRGR VSVGATGGAA GRKALTLATR
YALLRKQFDA PGEEDEITIL DYRAHQRKLL PLIAKSYAIT FAQNDLTSEL HDVQTADLSI
AELTDEDAER QRHLEGWAAG LKAYATWHAS HAINVSREAC GGAGYLDENQ LPIIRGDIDV
FTTFEGDNTV LTQLVGKELL SAYSDDVRGL NAGGWVRFVA GMARDVVAEK TAVRQVIQTI
LDNSDEETED SALSERATQI RLFRNREDHL LRTCAQRLRR ATEDDADPFE VFNNAQDHLL
KVGQAHVERI VLESFISGIA ECDSRSAAEV LDKVCDLFVY SALEADLSWF LMHRHVSVER
AKAIRRGVND LCEDLRPHAR TLVDAFGIPE ALLRAPMLEH G
//
