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Reviewed, UniProtKB/Swiss-Prot Q9LMI7 (ACO32_ARATH)

Last modified February 9, 2010. Version 56. 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

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Names and origin

Protein namesRecommended name:
    Putative acyl-coenzyme A oxidase 3.2, peroxisomal
    EC=1.3.3.6
Gene names
Name: ACX3.2
Ordered Locus Names: At1g06310
ORF Names: T2D23.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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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.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid beta-oxidation

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

acyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

acyl-CoA oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Peroxisome By similarity
Chain35 – 675641Putative acyl-coenzyme A oxidase 3.2, peroxisomal
PRO_0000000558

Regions

Nucleotide binding442 – 45716FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9LMI7-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 317D2FE5162F1534

FASTA67575,900
        10         20         30         40         50         60 
MSENVELRRA HILANHILRS PRPSSNPSLT PEVCFQYSPP ELNESYGFEV KEMRKLLDGH 

        70         80         90        100        110        120 
NLEERDWLYG LMMQSNLFNP KQRGGQIFVS PDYNQTMEQQ RQISMKRIFY LLEKGVFQGW 

       130        140        150        160        170        180 
LTETGPEAEL KKFALYEVCG IYDYSLSAKL GVHFLLWGNA VKFFGTKRHH EKWLKDTEDY 

       190        200        210        220        230        240 
VVKGCFAMTE LGHGTNVRGI ETVTTYDPTT EEFVINTPCE SAQKYWIGEA ANHANHAIVI 

       250        260        270        280        290        300 
SQLSMNGTNQ GIHVFIAQIR DHDGNTCPNV RIADCGHKIG LNGVDNGRIW FDNLRIPREN 

       310        320        330        340        350        360 
LLNSVADVLA DGKYVSSIKD PDQRFGAFLA PLTSGRVTIA SSAIYSAKLG LAVAIRYSLS 

       370        380        390        400        410        420 
RRAFSVAANG PEVLLLDYPS HQRRLLPLLA KTYAMSFAVN DLKMIYVKRT PETNKAIHVV 

       430        440        450        460        470        480 
SSGFKAVLTW HNMRTLQECR EAVGGQGLKT ENRVGHLKGE YDVQTTFEGD NNVLMQLVSK 

       490        500        510        520        530        540 
ALFAEYVSCK KRNKPFKGLG LEHMNSPRPV LPTQLTSSTL RCSQFQKSVF CLRERDLLER 

       550        560        570        580        590        600 
FTSEVAELQG RGESREFLFL LNHQLSEDLS KAFTEKAILQ TVLDAEAKLP PGSVKDVLGL 

       610        620        630        640        650        660 
VRSMYALISL EEDPSLLRYG HLSRDNVGDV RKEVSKLCGE LRPHALALVA SFGIPDAFLS 

       670 
PIAFNWVEAN AWSSL

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC068143 Genomic DNA. Translation: AAF82160.1.
IPIIPI00537491.
PIRH86198.
RefSeqNP_172120.2.
UniGeneAt.51502

3D structure databases

SMRQ9LMI7. Positions 47-671.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9LMI7.

Proteomic databases

PRIDEQ9LMI7.

Genome annotation databases

GeneID837141.
GenomeReviewsGene locus AT1G06310 in contig CT485782_GR.
KEGGath:AT1G06310.
NMPDRfig|3702.1.peg.806.

Organism-specific databases

TAIRAt1g06310.

Phylogenomic databases

eggNOGKOG0135.
HOGENOMHBG506332.
InParanoidQ9LMI7.
PhylomeDBQ9LMI7.

Enzyme and pathway databases

BRENDA1.3.3.6. 302.

Gene expression databases

GenevestigatorQ9LMI7.
GermOnlineAT1G06310. Arabidopsis thaliana.

Family and domain databases

InterProIPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
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.
PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameACO32_ARATH
AccessionPrimary (citable) accession number: Q9LMI7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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