ACO12_ARATH
ID ACO12_ARATH Reviewed; 664 AA.
AC Q9ZQP2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative peroxisomal acyl-coenzyme A oxidase 1.2;
DE EC=1.3.3.6;
GN Name=ACX1.2; OrderedLocusNames=At2g35690; ORFNames=T20F21.12;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP IDENTIFICATION, AND 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 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 -!- INDUCTION: Not induced by wounding. {ECO:0000269|PubMed:15141068}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; AC006068; AAD15446.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09145.1; -; Genomic_DNA.
DR EMBL; AY074357; AAL67053.1; -; mRNA.
DR EMBL; AY096691; AAM20325.1; -; mRNA.
DR PIR; G84771; G84771.
DR RefSeq; NP_181112.1; NM_129124.4.
DR AlphaFoldDB; Q9ZQP2; -.
DR SMR; Q9ZQP2; -.
DR BioGRID; 3483; 17.
DR STRING; 3702.AT2G35690.1; -.
DR PaxDb; Q9ZQP2; -.
DR PRIDE; Q9ZQP2; -.
DR ProteomicsDB; 244384; -.
DR EnsemblPlants; AT2G35690.1; AT2G35690.1; AT2G35690.
DR GeneID; 818138; -.
DR Gramene; AT2G35690.1; AT2G35690.1; AT2G35690.
DR KEGG; ath:AT2G35690; -.
DR Araport; AT2G35690; -.
DR TAIR; locus:2058779; AT2G35690.
DR eggNOG; KOG0136; Eukaryota.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; Q9ZQP2; -.
DR OMA; TKWWIGA; -.
DR OrthoDB; 416859at2759; -.
DR PhylomeDB; Q9ZQP2; -.
DR BRENDA; 1.3.3.6; 399.
DR PRO; PR:Q9ZQP2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQP2; baseline and differential.
DR Genevisible; Q9ZQP2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0016401; F:palmitoyl-CoA oxidase activity; 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 GO; GO:0001676; P:long-chain fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; 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; 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; 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 2: Evidence at transcript level;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..664
FT /note="Putative peroxisomal acyl-coenzyme A oxidase 1.2"
FT /id="PRO_0000204690"
FT MOTIF 662..664
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 399..404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 664 AA; 74298 MW; E523BC625944A7AA CRC64;
MERVDHLADE RNKAEFNVDD MKIVWAGSRH AFDVSNRMSR LVANDPVFEK SKRAVMSRKE
LFKNTLRKSV HAWKLINELR LSDEEGLKLR SFMDQPGFLD LHWGMFVPAI KGQGTEQQQQ
KWLSLATKMQ IIGCYAQTEL GHGSNVQGLE TTATFDPKTD QFIIHSPTQT SSKWWPGGLG
KVSTHAVIYA RLITNGKDHG VHGFIVQLRS LDDHSPLPGI TVGDIGMKFG NGAYNSMDNG
FLMFDHFRIP RDQMLMRLSK VTREGKYVAS DVPRQLVYGT MVYVRQSIVS NASTALARAV
CIATRYSAVR RQFGSHDGGI ETQVINYKTQ QNRLFPLLAS AYAFRFVGEW LKWLYTDVTK
RLEASDFATL PEAHACTAGL KSMTTSATSD GIEECRKLCG GHGYLWCSGL PELFAVYVPA
CTYEGDNVVL QLQVARFLMK TVSQLGSGKA PSGTTAYMGR AKHLLQCSSG VRNARDWLNP
GMVLEAFEAR ALRMAVTCAN NLSKFENQEQ GFSELLADLV EAATAHCQLI VVSKFIAKVE
GDIEGKGVKK QLKNLCYIYA LYLLHKHLGD FLSTNSVTPE QASLANQQLR SLYSQVRPNA
VALVDAFDYT DQYLGSVLGR YDGNVYPKLF EEALKDPLND SVVPDGYREY IRPLIKQRFR
SAKL
