ACOX_DEBHA
ID ACOX_DEBHA Reviewed; 706 AA.
AC Q6BRD5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Acyl-coenzyme A oxidase;
DE Short=Acyl-CoA oxidase;
DE EC=1.3.3.6;
GN Name=POX1; OrderedLocusNames=DEHA2D17248g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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).
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 -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; CR382136; CAG87407.2; -; Genomic_DNA.
DR RefSeq; XP_459235.2; XM_459235.1.
DR AlphaFoldDB; Q6BRD5; -.
DR SMR; Q6BRD5; -.
DR STRING; 4959.XP_459235.2; -.
DR PRIDE; Q6BRD5; -.
DR EnsemblFungi; CAG87407; CAG87407; DEHA2D17248g.
DR GeneID; 2901799; -.
DR KEGG; dha:DEHA2D17248g; -.
DR VEuPathDB; FungiDB:DEHA2D17248g; -.
DR eggNOG; KOG0136; Eukaryota.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; Q6BRD5; -.
DR OMA; PMMRGKL; -.
DR OrthoDB; 416859at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000000599; Chromosome D.
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; 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 3: Inferred from homology;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..706
FT /note="Acyl-coenzyme A oxidase"
FT /id="PRO_0000204698"
FT REGION 682..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 78487 MW; D3B95C9C5ADE2F62 CRC64;
MVSATNTVNS GVPPNPAASI QAERAASKFD PKEMHYFLEG GEERAEKFKQ MMQQMERDPI
LSANFQYYDL TKDQQRELTA LRIDRLTRYI ENESFDDFNK RMSLMGVFDP QLSTRLGINL
GLFVSCLKGN GTAEQVKYWA MDKSAVYMRG IYGCFGMTEL AHGSNVAGLE TTATFDDEND
EFIINTPHIG ATKWWIGGAA HSATHCSVYA RLIVGGQDYG VKTFVVPLRD SNHDTMPGVT
VGDIGAKMGR DGIDNGWIQF SNVRIPRYFM LQKFCKVSSE GDVQLPPLEQ LSYSALLGGR
VMMVLDSFRV SARFSTVALR YAIGRRQFKA GSASDDKNAL ECQLLDYPLH QRRLLPYLAL
SYIISASAVK IETTIESTLE NLDKAVEADD MGAIMKSIDS MKSLFVDSGS LKSTCTWLAA
EVIDQCRQAC GGHGYSAYSG FGKAYNDWVV MCTWEGDNNV LAMSVGKQII KHILGVLDGK
KVKGSADFLN NTEQYLNEEP VLRSVDDLKD LKKVLLAIEV AIIRVAYQAS QTLKENKGDF
DTVGAEMVTL SKLNAHHFML SEFLDRMDSF ESKQLVPYLE SVAKLYSATI VLEKFAGDFL
AQGVFPPKLN GELNSKHIPE LCKEIRPNVI ALTDSFQQSD MMINSAIGSY DGNIYENYFG
VVKANNPPSK TKAPYSGALE AMLNRPSKEE RERFEKSTET AKILSK
