ACOX3_ARATH
ID ACOX3_ARATH Reviewed; 675 AA.
AC P0CZ23; Q9C839; Q9LKX5; Q9LLH9; Q9LMI8; Q9M7X6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Acyl-coenzyme A oxidase 3, peroxisomal;
DE Short=AOX 3;
DE Short=Acyl-CoA oxidase 3;
DE EC=1.3.3.6;
DE AltName: Full=Medium-chain acyl-CoA oxidase;
DE Short=AtCX3;
DE Flags: Precursor;
GN Name=ACX3; OrderedLocusNames=At1g06290;
GN ORFNames=F9P14.15, F9P14_11, T2D23.1;
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], CHARACTERIZATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. No-0;
RX PubMed=10859203; DOI=10.1104/pp.123.2.733;
RA Froman B.E., Edwards P.C., Bursch A.G., Dehesh K.;
RT "ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis.";
RL Plant Physiol. 123:733-742(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RX PubMed=10918060; DOI=10.1074/jbc.m004945200;
RA Eastmond P.J., Hooks M.A., Williams D., Lange P., Bechtold N.,
RA Sarrobert C., Nussaume L., Graham I.A.;
RT "Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is
RT induced transcriptionally during Arabidopsis seed germination.";
RL J. Biol. Chem. 275:34375-34381(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 medium-chain acyl-CoAs to 2-
CC trans-enoyl-CoAs. Active on C8:0- to C14:0-CoA with a maximal activity
CC on C12:0-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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for lauroyl-CoA;
CC pH dependence:
CC Optimum pH is 8.5-9.0.;
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10918060}.
CC -!- TISSUE SPECIFICITY: Most abundant in flowers and senescing rosette
CC leaves. Lower expression in hypocotyls, stems, young rosette leaves,
CC cotyledons, cauline leaves and root tip of young seedlings.
CC {ECO:0000269|PubMed:10859203, ECO:0000269|PubMed:10918060}.
CC -!- DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak at day 2
CC and then declines steadily until day 7. Not detected in developing
CC seeds. Constitutive expression in root axis.
CC {ECO:0000269|PubMed:10859203}.
CC -!- INDUCTION: Not induced by dehydration or 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; AF207994; AAF73843.1; -; mRNA.
DR EMBL; AF253474; AAF76137.1; -; mRNA.
DR EMBL; AC068143; AAF82159.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27972.1; -; Genomic_DNA.
DR EMBL; AY099579; AAM20431.1; -; mRNA.
DR EMBL; BT008413; AAP37772.1; -; mRNA.
DR EMBL; AK176257; BAD44020.1; -; mRNA.
DR PIR; G86198; G86198.
DR RefSeq; NP_172119.1; NM_100511.3.
DR AlphaFoldDB; P0CZ23; -.
DR SMR; P0CZ23; -.
DR BioGRID; 22381; 2.
DR IntAct; P0CZ23; 1.
DR STRING; 3702.AT1G06290.1; -.
DR PaxDb; P0CZ23; -.
DR PRIDE; P0CZ23; -.
DR ProteomicsDB; 244385; -.
DR EnsemblPlants; AT1G06290.1; AT1G06290.1; AT1G06290.
DR GeneID; 837140; -.
DR Gramene; AT1G06290.1; AT1G06290.1; AT1G06290.
DR KEGG; ath:AT1G06290; -.
DR Araport; AT1G06290; -.
DR TAIR; locus:2038540; AT1G06290.
DR eggNOG; KOG0135; Eukaryota.
DR HOGENOM; CLU_014629_4_0_1; -.
DR InParanoid; P0CZ23; -.
DR OMA; VMPNIQI; -.
DR OrthoDB; 226134at2759; -.
DR PhylomeDB; P0CZ23; -.
DR BioCyc; ARA:AT1G06290-MON; -.
DR BioCyc; MetaCyc:AT1G06290-MON; -.
DR BRENDA; 1.3.3.6; 399.
DR UniPathway; UPA00661; -.
DR PRO; PR:P0CZ23; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0CZ23; baseline and differential.
DR Genevisible; P0CZ23; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
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:0006635; P:fatty acid beta-oxidation; TAS: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:0051791; P:medium-chain fatty acid metabolic process; TAS:TAIR.
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 1: Evidence at protein level;
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:0000255"
FT CHAIN 35..675
FT /note="Acyl-coenzyme A oxidase 3, peroxisomal"
FT /id="PRO_0000000557"
FT BINDING 442..457
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 33
FT /note="L -> V (in Ref. 1; AAF73843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 75676 MW; FABBCBA01C5FC103 CRC64;
MSDNRALRRA HVLANHILQS NPPSSNPSLS RELCLQYSPP ELNESYGFDV KEMRKLLDGH
NVVDRDWIYG LMMQSNLFNR KERGGKIFVS PDYNQTMEQQ REITMKRIWY LLENGVFKGW
LTETGPEAEL RKLALLEVCG IYDHSVSIKV GVHFFLWGNA VKFFGTKRHH EKWLKNTEDY
VVKGCFAMTE LGHGSNVRGI ETVTTYDPKT EEFVINTPCE SAQKYWIGGA ANHATHTIVF
SQLHINGTNQ GVHAFIAQIR DQDGSICPNI RIADCGHKIG LNGVDNGRIW FDNLRIPREN
LLNAVADVSS DGKYVSSIKD PDQRFGAFMA PLTSGRVTIA SSAIYSAKVG LSIAIRYSLS
RRAFSVTANG PEVLLLDYPS HQRRLLPLLA KTYAMSFAAN ELKMIYVKRT PETNKAIHVV
SSGFKAVLTW HNMHTLQECR EAVGGQGVKT ENLVGQLKGE FDVQTTFEGD NNVLMQQVSK
ALFAEYVSCK KRNKPFKGLG LEHMNSPRPV LPTQLTSSTL RCSQFQTNVF CLRERDLLEQ
FTSEVAQLQG RGESREFSFL LSHQLAEDLG KAFTEKAILQ TILDAEAKLP TGSVKDVLGL
VRSMYALISL EEDPSLLRYG YLSQDNVGDV RREVSKLCGE LRPHALALVT SFGIPDSFLS
PIAFNWVEAN AWSSV
