ID   ACO32_ARATH             Reviewed;         675 AA.
AC   Q9LMI7;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Putative acyl-coenzyme A oxidase 3.2, peroxisomal;
DE            EC=1.3.3.6;
DE   Flags: Precursor;
GN   Name=ACX3.2; OrderedLocusNames=At1g06310; ORFNames=T2D23.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=15141068; DOI=10.1104/pp.104.039925;
RA   Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.;
RT   "Gene-specific involvement of beta-oxidation in wound-activated responses
RT   in Arabidopsis.";
RL   Plant Physiol. 135:85-94(2004).
CC   -!- FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-
CC       CoAs. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; AC068143; AAF82160.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27973.1; -; Genomic_DNA.
DR   PIR; H86198; H86198.
DR   RefSeq; NP_172120.2; NM_100512.3.
DR   AlphaFoldDB; Q9LMI7; -.
DR   SMR; Q9LMI7; -.
DR   STRING; 3702.AT1G06310.1; -.
DR   iPTMnet; Q9LMI7; -.
DR   PaxDb; Q9LMI7; -.
DR   PRIDE; Q9LMI7; -.
DR   ProteomicsDB; 244690; -.
DR   EnsemblPlants; AT1G06310.1; AT1G06310.1; AT1G06310.
DR   GeneID; 837141; -.
DR   Gramene; AT1G06310.1; AT1G06310.1; AT1G06310.
DR   KEGG; ath:AT1G06310; -.
DR   Araport; AT1G06310; -.
DR   TAIR; locus:2202275; AT1G06310.
DR   eggNOG; KOG0135; Eukaryota.
DR   HOGENOM; CLU_014629_4_0_1; -.
DR   InParanoid; Q9LMI7; -.
DR   OMA; ITWSARD; -.
DR   OrthoDB; 226134at2759; -.
DR   PhylomeDB; Q9LMI7; -.
DR   BioCyc; ARA:AT1G06310-MON; -.
DR   PRO; PR:Q9LMI7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LMI7; baseline and differential.
DR   Genevisible; Q9LMI7; AT.
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; 2.40.110.10; -; 1.
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; 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   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; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Peroxisome"
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..675
FT                   /note="Putative acyl-coenzyme A oxidase 3.2, peroxisomal"
FT                   /id="PRO_0000000558"
FT   BINDING         442..457
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   675 AA;  75900 MW;  317D2FE5162F1534 CRC64;
     MSENVELRRA HILANHILRS PRPSSNPSLT PEVCFQYSPP ELNESYGFEV KEMRKLLDGH
     NLEERDWLYG LMMQSNLFNP KQRGGQIFVS PDYNQTMEQQ RQISMKRIFY LLEKGVFQGW
     LTETGPEAEL KKFALYEVCG IYDYSLSAKL GVHFLLWGNA VKFFGTKRHH EKWLKDTEDY
     VVKGCFAMTE LGHGTNVRGI ETVTTYDPTT EEFVINTPCE SAQKYWIGEA ANHANHAIVI
     SQLSMNGTNQ GIHVFIAQIR DHDGNTCPNV RIADCGHKIG LNGVDNGRIW FDNLRIPREN
     LLNSVADVLA DGKYVSSIKD PDQRFGAFLA PLTSGRVTIA SSAIYSAKLG LAVAIRYSLS
     RRAFSVAANG PEVLLLDYPS HQRRLLPLLA KTYAMSFAVN DLKMIYVKRT PETNKAIHVV
     SSGFKAVLTW HNMRTLQECR EAVGGQGLKT ENRVGHLKGE YDVQTTFEGD NNVLMQLVSK
     ALFAEYVSCK KRNKPFKGLG LEHMNSPRPV LPTQLTSSTL RCSQFQKSVF CLRERDLLER
     FTSEVAELQG RGESREFLFL LNHQLSEDLS KAFTEKAILQ TVLDAEAKLP PGSVKDVLGL
     VRSMYALISL EEDPSLLRYG HLSRDNVGDV RKEVSKLCGE LRPHALALVA SFGIPDAFLS
     PIAFNWVEAN AWSSL