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Reviewed, UniProtKB/Swiss-Prot Q9ZQP2 (ACO12_ARATH)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative peroxisomal acyl-coenzyme A oxidase 1.2
    EC=1.3.3.6
Gene names
Name: ACX1.2
Ordered Locus Names: At2g35690
ORF Names: T20F21.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs By similarity.

Catalytic activity

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactor

FAD By similarity.

Subcellular location

Peroxisome Probable.

Induction

Not induced by wounding. Ref.3

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 664664Putative peroxisomal acyl-coenzyme A oxidase 1.2
PRO_0000204690

Regions

Nucleotide binding399 – 4046FAD By similarity
Motif662 – 6643Microbody targeting signal Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZQP2-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E523BC625944A7AA

FASTA66474,298
        10         20         30         40         50         60 
MERVDHLADE RNKAEFNVDD MKIVWAGSRH AFDVSNRMSR LVANDPVFEK SKRAVMSRKE 

        70         80         90        100        110        120 
LFKNTLRKSV HAWKLINELR LSDEEGLKLR SFMDQPGFLD LHWGMFVPAI KGQGTEQQQQ 

       130        140        150        160        170        180 
KWLSLATKMQ IIGCYAQTEL GHGSNVQGLE TTATFDPKTD QFIIHSPTQT SSKWWPGGLG 

       190        200        210        220        230        240 
KVSTHAVIYA RLITNGKDHG VHGFIVQLRS LDDHSPLPGI TVGDIGMKFG NGAYNSMDNG 

       250        260        270        280        290        300 
FLMFDHFRIP RDQMLMRLSK VTREGKYVAS DVPRQLVYGT MVYVRQSIVS NASTALARAV 

       310        320        330        340        350        360 
CIATRYSAVR RQFGSHDGGI ETQVINYKTQ QNRLFPLLAS AYAFRFVGEW LKWLYTDVTK 

       370        380        390        400        410        420 
RLEASDFATL PEAHACTAGL KSMTTSATSD GIEECRKLCG GHGYLWCSGL PELFAVYVPA 

       430        440        450        460        470        480 
CTYEGDNVVL QLQVARFLMK TVSQLGSGKA PSGTTAYMGR AKHLLQCSSG VRNARDWLNP 

       490        500        510        520        530        540 
GMVLEAFEAR ALRMAVTCAN NLSKFENQEQ GFSELLADLV EAATAHCQLI VVSKFIAKVE 

       550        560        570        580        590        600 
GDIEGKGVKK QLKNLCYIYA LYLLHKHLGD FLSTNSVTPE QASLANQQLR SLYSQVRPNA 

       610        620        630        640        650        660 
VALVDAFDYT DQYLGSVLGR YDGNVYPKLF EEALKDPLND SVVPDGYREY IRPLIKQRFR 


SAKL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Gene-specific involvement of beta-oxidation in wound-activated responses in Arabidopsis."
Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.
Plant Physiol. 135:85-94(2004) [PubMed: 15141068] [Abstract]
Cited for: IDENTIFICATION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

AC006068 Genomic DNA. Translation: AAD15446.1.
AY074357 mRNA. Translation: AAL67053.1.
AY096691 mRNA. Translation: AAM20325.1.
IPIIPI00520398.
PIRG84771.
RefSeqNP_181112.1.
UniGeneAt.37640

3D structure databases

HSSPHSSP built from PDB template 1IS2 based on UniProtKB P07872.
SMRQ9ZQP2. Positions 2-659.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ZQP2.

Proteomic databases

PRIDEQ9ZQP2.

Genome annotation databases

GeneID818138.
GenomeReviewsGene locus AT2G35690 in contig CT485783_GR.
KEGGath:AT2G35690.
NMPDRfig|3702.1.peg.10667.

Organism-specific databases

TAIRAt2g35690.

Phylogenomic databases

OMAMVQIRLL.

Enzyme and pathway databases

BRENDA1.3.3.6. 302.

Gene expression databases

ArrayExpressQ9ZQP2.
GenevestigatorQ9ZQP2.
GermOnlineAT2G35690. Arabidopsis thaliana.

Family and domain databases

InterProIPR006091. Acyl-CoA_Oxase/DH_M.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
PANTHERPTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACO12_ARATH
AccessionPrimary (citable) accession number: Q9ZQP2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents