ID   ACOX3_YARLI             Reviewed;         700 AA.
AC   O74936; Q6C7W8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Acyl-coenzyme A oxidase 3;
DE            Short=Acyl-CoA oxidase 3;
DE            EC=1.3.3.6;
GN   Name=POX3; Synonyms=ACO3; OrderedLocusNames=YALI0D24750g;
OS   Yarrowia lipolytica (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=4952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX   MEDLINE=99064695; PubMed=9848229;
RX   DOI=10.1002/(SICI)1097-0061(199811)14:15<1373::AID-YEA332>3.3.CO;2-T;
RA   Wang H., Le Clainche A., le Dall M.-T., Wache Y., Pagot Y.,
RA   Belin J.M., Gaillardin C., Nicaud J.-M.;
RT   "Cloning and characterization of the peroxisomal acyl CoA oxidase ACO3
RT   gene from the alkane-utilizing yeast Yarrowia lipolytica.";
RL   Yeast 14:1373-1386(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=21023333; PubMed=11147819; DOI=10.1006/abbi.2000.2079;
RA   Luo Y.S., Wang H.J., Gopalan K.V., Srivastava D.K., Nicaud J.-M.,
RA   Chardot T.;
RT   "Purification and characterization of the recombinant form of Acyl CoA
RT   oxidase 3 from the yeast Yarrowia lipolytica.";
RL   Arch. Biochem. Biophys. 384:1-8(2000).
RN   [4]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21686203; PubMed=11815635; DOI=10.1083/jcb.200111075;
RA   Titorenko V.I., Nicaud J.-M., Wang H., Chan H., Rachubinski R.A.;
RT   "Acyl-CoA oxidase is imported as a heteropentameric, cofactor-
RT   containing complex into peroxisomes of Yarrowia lipolytica.";
RL   J. Cell Biol. 156:481-494(2002).
CC   -!- FUNCTION: Oxidizes aliphatic acyl-CoA substrates of different
CC       chain lengths such as hexanoyl-CoA, decanoyl-CoA and myristyl-CoA
CC       as well as aromatic/heterocyclic ring-substituted chromogenic
CC       substrates, such as furylpropionyl-CoA. Of the above substrates,
CC       the efficiency of the enzyme, exhibits the following order:
CC       decanoyl-CoA > myristyl-CoA > hexanoyl-CoA > furyl-propionyl-CoA.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA +
CC       H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.4;
CC       Temperature dependence:
CC         Optimum temperature is 23-38 degrees Celsius;
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC   -!- SUBUNIT: Heteropentamer composed of five different subunits.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
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DR   EMBL; AJ001301; CAA04661.1; -; Genomic_DNA.
DR   EMBL; CR382130; CAG81448.1; -; Genomic_DNA.
DR   RefSeq; XP_503244.1; -.
DR   HSSP; P07872; 1IS2.
DR   GeneID; 2910308; -.
DR   KEGG; yli:YALI0D24750g; -.
DR   HOGENOM; O74936; -.
DR   OMA; O74936; EYERANT.
DR   BRENDA; 1.3.3.6; 3602.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006090; Acyl-CoA_Oxase/DH_1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_M.
DR   InterPro; IPR012258; Acyl-CoA_oxidase.
DR   InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR013764; AcylCoA_oxidase/DH_1/2_C.
DR   Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
DR   Gene3D; G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
DR   Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.
DR   PANTHER; PTHR10909:SF11; Acyl-CoA_oxidase; 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.
PE   1: Evidence at protein level;
KW   Complete proteome; FAD; Fatty acid metabolism; Flavoprotein;
KW   Lipid metabolism; Oxidoreductase; Peroxisome.
FT   CHAIN         1    700       Acyl-coenzyme A oxidase 3.
FT                                /FTId=PRO_0000204703.
SQ   SEQUENCE   700 AA;  78010 MW;  864A89CF48161D5E CRC64;
     MISPNLTANV EIDGKQYNTF TEPPKALAGE RAKVKFPIKD MTEFLHGGEE NVTMIERLMT
     ELERDPVLNV SGDYDMPKEQ LRETAVARIA ALSGHWKKDT EKEALLRSQL HGIVDMGTRI
     RLGVHTGLFM GAIRGSGTKE QYDYWVRKGA ADVKGFYGCF AMTELGHGSN VAGLETTATY
     IQDTDEFIIN TPNTGATKWW IGGAAHSATH TACFARLLVD GKDYGVKIFV VQLRDVSSHS
     LMPGIALGDI GKKMGRDAID NGWIQFTNVR IPRQNMLMKY AKVSSTGKVS QPPLAQLTYG
     ALIGGRVTMI ADSFFVSQRF ITIALRYACV RRQFGTTPGQ PETKIIDYPY HQRRLLPLLA
     FTYAMKMAAD QSQIQYDQTT DLLQTIDPKD KGALGKAIVD LKELFASSAG LKAFTTWTCA
     NIIDQCRQAC GGHGYSGYNG FGQAYADWVV QCTWEGDNNV LCLSMGRGLI QSCLGHRKGK
     PLGSSVGYLA NKGLEQATLS GRDLKDPKVL IEAWEKVANG AIQRATDKFV ELTKGGLSPD
     QAFEELSQQR FQCAKIHTRK HLVTAFYERI NASAKADVKP YLINLANLFT LWSIEEDSGL
     FLREGFLQPK DIDQVTELVN HYCKEVRDQV AGYTDAFGLS DWFINAPIGN YDGDVYKHYF
     AKVNQQNPAQ NPRPPYYEST LRPFLFREDE DDDICELDEE
//