ACOX1_YARLI
ID ACOX1_YARLI Reviewed; 689 AA.
AC O74934; Q6C3Q9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Acyl-coenzyme A oxidase 1;
DE Short=Acyl-CoA oxidase 1;
DE EC=1.3.3.6;
GN Name=POX1; Synonyms=ACO1; OrderedLocusNames=YALI0E32835g;
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].
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RA Le Clainche A., Nicaud J.-M.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 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 -!- 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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG80307.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ001299; CAA04659.1; -; Genomic_DNA.
DR EMBL; CR382131; CAG80307.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_504703.1; XM_504703.1.
DR PDB; 5Y9D; X-ray; 2.50 A; A/B=1-689.
DR PDBsum; 5Y9D; -.
DR AlphaFoldDB; O74934; -.
DR SMR; O74934; -.
DR STRING; 4952.CAG80307; -.
DR GeneID; 2912003; -.
DR KEGG; yli:YALI0E32835g; -.
DR InParanoid; O74934; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000001300; Chromosome E.
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..689
FT /note="Acyl-coenzyme A oxidase 1"
FT /id="PRO_0000204701"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:5Y9D"
FT TURN 134..139
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5Y9D"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5Y9D"
FT TURN 188..193
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 208..218
FT /evidence="ECO:0007829|PDB:5Y9D"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 286..314
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 335..371
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 380..417
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 418..424
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 430..437
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:5Y9D"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 447..466
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 473..479
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 499..524
FT /evidence="ECO:0007829|PDB:5Y9D"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 538..561
FT /evidence="ECO:0007829|PDB:5Y9D"
FT TURN 566..568
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 569..586
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 588..593
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 599..617
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 645..656
FT /evidence="ECO:0007829|PDB:5Y9D"
FT TURN 665..670
FT /evidence="ECO:0007829|PDB:5Y9D"
FT HELIX 671..675
FT /evidence="ECO:0007829|PDB:5Y9D"
SQ SEQUENCE 689 AA; 77282 MW; 843D99D6DCEB4150 CRC64;
MTTNTFTDPP VEMAKERGKT QFTVRDVTNF LNGGEEETQI VEKIMSSIER DPVLSVTADY
DCNLQQARKQ TMERVAALSP YLVTDTEKLS LWRAQLHGMV DMSTRTRLSI HNNLFIGSIR
GSGTPEQFKY WVKKGAVAVK QFYGCFAMTE LGHGSNLKGL ETTATYDQDS DQFIINTPHI
GATKWWIGGA AHTSTHCVCF AKLIVHGKDY GTRNFVVPLR NVHDHSLKVG VSIGDIGKKM
GRDGVDNGWI QFTNVRIPRQ NMLMRYAKVS DTGVVTKPAL DQLTYGALIR GRVSMIADSF
HVSKRFLTIA LRYACVRRQF GTSGDTKETK IIDYPYHQRR LLPLLAYCYA MKMGADEAQK
TWIETTDRIL ALNPNDPAQK NDLEKAVTDT KELFAASAGM KAFTTWGCAK IIDECRQACG
GHGYSGYNGF GQGYADWVVQ CTWEGDNNVL CLSMGRGLVQ SALQILAGKH VGASIQYVGD
KSKISQNGQG TPREQLLSPE FLVEAFRTAS RNNILRTTDK YQELVKTLNP DQAFEELSQQ
RFQCARIHTR QHLISSFYAR IATAKDDIKP HLLKLANLFA LWSIEEDTGI FLRENILTPG
DIDLINSLVD ELCVAVRDQV IGLTDAFGLS DFFINAPIGS YDGNVYEKYF AKVNQQNPAT
NPRPPYYEST LKPFLFREEE DDEICDLDE
