ACOX2_ARATH
ID ACOX2_ARATH Reviewed; 692 AA.
AC O65201; Q9FJQ4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Acyl-coenzyme A oxidase 2, peroxisomal {ECO:0000303|PubMed:10571860};
DE Short=AOX 2 {ECO:0000305};
DE EC=1.3.3.6 {ECO:0000269|PubMed:10571860};
DE AltName: Full=Long-chain acyl-CoA oxidase {ECO:0000305};
DE Short=AtCX2 {ECO:0000303|PubMed:10571860};
DE Flags: Precursor;
GN Name=ACX2 {ECO:0000303|PubMed:10571860};
GN OrderedLocusNames=At5g65110 {ECO:0000312|Araport:AT5G65110};
GN ORFNames=MQN23.4 {ECO:0000312|EMBL:BAB11647.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=10571860; DOI=10.1046/j.1365-313x.1999.00559.x;
RA Hooks M.A., Kellas F., Graham I.A.;
RT "Long-chain acyl-CoA oxidases of Arabidopsis.";
RL Plant J. 20:1-13(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
RP INDUCTION.
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 long-chain acyl-CoAs to 2-
CC trans-enoyl-CoAs. Active on substrates longer than C14 and mostly with
CC C18-CoA. Activity on long-chain mono-unsaturated substrates is double
CC than with the corresponding saturated substrates.
CC {ECO:0000269|PubMed:10571860}.
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 Evidence={ECO:0000269|PubMed:10571860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000269|PubMed:10571860};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O65202};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O65202};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for C18:1-CoA {ECO:0000269|PubMed:10571860};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O65202}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=O65201-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed mainly in flowers and young seedlings.
CC Lower expression in roots, leaves and bracts.
CC {ECO:0000269|PubMed:10571860}.
CC -!- DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak at day 2
CC and then declines steadily until day 8. {ECO:0000269|PubMed:10571860}.
CC -!- INDUCTION: Induced by dehydration and abscisic acid (ABA).
CC {ECO:0000269|PubMed:15141068}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; AF057043; AAC13497.1; -; mRNA.
DR EMBL; AB013395; BAB11647.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98003.1; -; Genomic_DNA.
DR PIR; T52120; T52120.
DR RefSeq; NP_201316.1; NM_125910.6. [O65201-1]
DR AlphaFoldDB; O65201; -.
DR SMR; O65201; -.
DR STRING; 3702.AT5G65110.1; -.
DR PaxDb; O65201; -.
DR PRIDE; O65201; -.
DR ProteomicsDB; 244361; -. [O65201-1]
DR EnsemblPlants; AT5G65110.1; AT5G65110.1; AT5G65110. [O65201-1]
DR GeneID; 836635; -.
DR Gramene; AT5G65110.1; AT5G65110.1; AT5G65110. [O65201-1]
DR KEGG; ath:AT5G65110; -.
DR Araport; AT5G65110; -.
DR TAIR; locus:2171825; AT5G65110.
DR eggNOG; KOG0135; Eukaryota.
DR HOGENOM; CLU_014629_4_3_1; -.
DR InParanoid; O65201; -.
DR OMA; YVTRAPI; -.
DR PhylomeDB; O65201; -.
DR BioCyc; ARA:AT5G65110-MON; -.
DR BioCyc; MetaCyc:AT5G65110-MON; -.
DR BRENDA; 1.3.3.6; 399.
DR PRO; PR:O65201; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65201; baseline and differential.
DR Genevisible; O65201; AT.
DR GO; GO:0005777; C:peroxisome; ISS:TAIR.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:TAIR.
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:0006635; P:fatty acid beta-oxidation; IDA:TAIR.
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 GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:TAIR.
DR CDD; cd01150; AXO; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR034171; ACO.
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 1: Evidence at protein level;
KW Alternative splicing; FAD; Fatty acid metabolism; Flavoprotein;
KW Lipid metabolism; Oxidoreductase; Peroxisome; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Peroxisome"
FT /evidence="ECO:0000255"
FT CHAIN 50..692
FT /note="Acyl-coenzyme A oxidase 2, peroxisomal"
FT /id="PRO_0000000555"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 192
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 384
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 452
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 473
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT BINDING 477
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O65202"
FT CONFLICT 37
FT /note="P -> L (in Ref. 1; AAC13497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 77480 MW; 43B29F0E8D3176D7 CRC64;
MESRREKNPM TEEESDGLIA ARRIQRLSLH LSPSLTPSPS LPLVQTETCS ARSKKLDVNG
EALSLYMRGK HIDIQEKIFD FFNSRPDLQT PIEISKDDHR ELCMNQLIGL VREAGVRPFR
YVADDPEKYF AIMEAVGSVD MSLGIKMGVQ YSLWGGSVIN LGTKKHRDKY FDGIDNLDYT
GCFAMTELHH GSNVQGLQTT ATFDPLKDEF VIDTPNDGAI KWWIGNAAVH GKFATVFARL
ILPTHDSKGV SDMGVHAFIV PIRDMKTHQT LPGVEIQDCG HKVGLNGVDN GALRFRSVRI
PRDNLLNRFG DVSRDGTYTS SLPTINKRFG ATLGELVGGR VGLAYASVGV LKISATIAIR
YSLLRQQFGP PKQPEVSILD YQSQQHKLMP MLASTYAYHF ATVYLVEKYS EMKKTHDEQL
VADVHALSAG LKSYVTSYTA KALSVCREAC GGHGYAAVNR FGSLRNDHDI FQTFEGDNTV
LLQQVAADLL KRYKEKFQGG TLTVTWSYLR ESMNTYLSQP NPVTARWEGE DHLRDPKFQL
DAFRYRTSRL LQNVAARLQK HSKTLGGFGA WNRCLNHLLT LAESHIETVI LAKFIEAVKN
CPDPSAKAAL KLACDLYALD RIWKDIGTYR NVDYVAPNKA KAIHKLTEYL SFQVRNVAKE
LVDAFELPDH VTRAPIAMQS DAYSQYTQVV GF
