ACOX4_CANTR
ID ACOX4_CANTR Reviewed; 709 AA.
AC P06598; P11355;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acyl-coenzyme A oxidase 4;
DE Short=Acyl-CoA oxidase 4;
DE EC=1.3.3.6;
DE AltName: Full=PXP-4;
DE AltName: Full=Peroxisomal fatty acyl-CoA oxidase;
GN Name=POX4; Synonyms=AOX;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX PubMed=3596241; DOI=10.1016/0378-1119(87)90300-3;
RA Murray W.W., Rachubinski R.A.;
RT "The primary structure of a peroxisomal fatty acyl-CoA oxidase from the
RT yeast Candida tropicalis pK233.";
RL Gene 51:119-128(1987).
RN [2]
RP SEQUENCE REVISION TO 367; 381 AND 385.
RA Murray W.W., Rachubinski R.A.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX PubMed=3456583; DOI=10.1073/pnas.83.5.1232;
RA Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.;
RT "Two acyl-coenzyme A oxidases in peroxisomes of the yeast Candida
RT tropicalis: primary structures deduced from genomic DNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1232-1236(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-709.
RC STRAIN=RR1;
RX PubMed=3611187; DOI=10.1083/jcb.105.1.247;
RA Small G.M., Lazarow P.B.;
RT "Import of the carboxy-terminal portion of acyl-CoA oxidase into
RT peroxisomes of Candida tropicalis.";
RL J. Cell Biol. 105:247-250(1987).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC -!- SUBUNIT: Homooctamer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68661.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA68662.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M16193; AAA34322.2; -; Genomic_DNA.
DR EMBL; M12160; AAA34362.1; -; Genomic_DNA.
DR EMBL; Y00623; CAA68660.1; -; mRNA.
DR EMBL; Y00623; CAA68661.1; ALT_INIT; mRNA.
DR EMBL; Y00623; CAA68662.1; ALT_INIT; mRNA.
DR PIR; A25123; OXCKX4.
DR PIR; A28584; OXCKAX.
DR PIR; A29047; OXCKX.
DR AlphaFoldDB; P06598; -.
DR SMR; P06598; -.
DR PRIDE; P06598; -.
DR VEuPathDB; FungiDB:CTMYA2_049290; -.
DR VEuPathDB; FungiDB:CTRG_02377; -.
DR SABIO-RK; P06598; -.
DR UniPathway; UPA00661; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR029320; Acyl-CoA_ox_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 2: Evidence at transcript level;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..709
FT /note="Acyl-coenzyme A oxidase 4"
FT /id="PRO_0000204696"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 217
FT /note="Q -> E (in Ref. 4; CAA68660)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="P -> A (in Ref. 3; AAA34362 and 4; CAA68660)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="N -> K (in Ref. 3; AAA34362)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..394
FT /note="FVPPMSSPSVPSRLNTPSRPPWSNWTSPLKRTTPRL -> LAAAYVISAGAL
FT KVEDTIHNTLAELDAAVEKNDTKA (in Ref. 3; AAA34362 and 4;
FT CAA68660/CAA68661)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="H -> Y (in Ref. 3; AAA34362)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="G -> A (in Ref. 3; AAA34362)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="E -> D (in Ref. 3; AAA34362)"
FT /evidence="ECO:0000305"
FT CONFLICT 577..579
FT /note="ELA -> DLV (in Ref. 3; AAA34362)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="Q -> E (in Ref. 3; AAA34362 and 4; CAA68660/
FT CAA68661/CAA68662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 79094 MW; 0D60580353F5D927 CRC64;
MTFTKKNVSV SQGPDPRSSI QKERDSSKWN PQQMNYFLEG SVERSELMKA LAQQMERDPI
LFTDGSYYDL TKDQQRELTA VKINRIARYR EQESIDTFNK RLSLIGIFDP QVGTRIGVNL
GLFLSCIRGN GTTSQLNYWA NEKETADVKG IYGCFGMTEL AHGSNVAGLE TTATFDKESD
EFVINTPHIG ATKWWIGGAA HSATHCSVYA RLIVDGQDYG VKTFVVPLRD SNHDLMPGVT
VGDIGPKMGR DGIDNGWIQF SNVRIPRFFM LQKFCKVSAE GEVTLPPLEQ LSYSALLGGR
VMMVLDSYRM LARMSTIALR YAIGRRQFKG DNVDPNDPNA LETQLIDYPL HQKRLFPYFV
PPMSSPSVPS RLNTPSRPPW SNWTSPLKRT TPRLIFKSID DMKSLFVDSG SLKSTATWLG
AEAIDQCRQA CGGHGHSSYN GFGKAYNDWV VQCTWEGDNN VLGMSVGKPI VKQVISIEDA
GKTVRGSTAF LNQLKEYTGS NSSKVVLNTV ADLDDIKTVI KAIEVAIIRL SQEAASIVKK
ESFDYVGAEL VQLSKLKAHH YLLTEYIRRI DTFDQKELAP YLITLGKLYA ATIVLDRFAG
VFLTFNVAST EAITALASVQ IPKLCAEVRP NVVAYTDSFQ QSDMIVNSAI GRYDGDIYEN
YFDLVKLQNP PSKTKAPYSD ALEAMLNRPT LDERERFQKS DETAAILSK
