ACOX3_YARLI
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 03-AUG-2022, entry version 125.
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 (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX PubMed=9848229;
RX DOI=10.1002/(sici)1097-0061(199811)14:15<1373::aid-yea332>3.0.co;2-1;
RA Wang H., Le Clainche A., le Dall M.-T., Wache Y., Pagot Y., Belin J.M.,
RA Gaillardin C., Nicaud J.-M.;
RT "Cloning and characterization of the peroxisomal acyl CoA oxidase ACO3 gene
RT 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., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP CHARACTERIZATION.
RX 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 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-containing
RT complex into peroxisomes of Yarrowia lipolytica.";
RL J. Cell Biol. 156:481-494(2002).
CC -!- FUNCTION: Oxidizes aliphatic acyl-CoA substrates of different chain
CC lengths such as hexanoyl-CoA, decanoyl-CoA and myristoyl-CoA as well as
CC aromatic/heterocyclic ring-substituted chromogenic substrates, such as
CC furylpropionyl-CoA. Of the above substrates, the efficiency of the
CC enzyme, exhibits the following order: decanoyl-CoA > myristoyl-CoA >
CC hexanoyl-CoA > furyl-propionyl-CoA.
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; Evidence={ECO:0000250};
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 {ECO:0000269|PubMed:11815635}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11815635}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; AJ001301; CAA04661.1; -; Genomic_DNA.
DR EMBL; CR382130; CAG81448.1; -; Genomic_DNA.
DR RefSeq; XP_503244.1; XM_503244.1.
DR PDB; 5YS9; X-ray; 2.50 A; A/B=1-700.
DR PDBsum; 5YS9; -.
DR AlphaFoldDB; O74936; -.
DR SMR; O74936; -.
DR STRING; 4952.CAG81448; -.
DR EnsemblFungi; CAG81448; CAG81448; YALI0_D24750g.
DR GeneID; 2910308; -.
DR KEGG; yli:YALI0D24750g; -.
DR VEuPathDB; FungiDB:YALI0_D24750g; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; O74936; -.
DR OMA; PMMRGKL; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
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; IPR009075; AcylCo_DH/oxidase_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; PF00441; Acyl-CoA_dh_1; 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 1: Evidence at protein level;
KW 3D-structure; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..700
FT /note="Acyl-coenzyme A oxidase 3"
FT /id="PRO_0000204703"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 148..153
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 300..330
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 349..385
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 391..428
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 429..435
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 441..448
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:5YS9"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 458..477
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 484..490
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 507..534
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 539..545
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 547..573
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 579..596
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 598..603
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 609..628
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 630..635
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 641..644
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 655..666
FT /evidence="ECO:0007829|PDB:5YS9"
FT TURN 675..680
FT /evidence="ECO:0007829|PDB:5YS9"
FT HELIX 681..685
FT /evidence="ECO:0007829|PDB:5YS9"
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
