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Q9LMI7 (ACO32_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

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

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.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

acyl-CoA oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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

Sequences

Sequence LengthMass (Da)Tools
Q9LMI7 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC068143 Genomic DNA. Translation: AAF82160.1.
CP002684 Genomic DNA. Translation: AEE27973.1.
PIRH86198.
RefSeqNP_172120.2. NM_100512.2.
UniGeneAt.51502.

3D structure databases

ProteinModelPortalQ9LMI7.
SMRQ9LMI7. Positions 114-662.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G06310.1-P.

Proteomic databases

PaxDbQ9LMI7.
PRIDEQ9LMI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G06310.1; AT1G06310.1; AT1G06310.
GeneID837141.
KEGGath:AT1G06310.

Organism-specific databases

TAIRAT1G06310.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000245077.
InParanoidQ9LMI7.
KOK00232.
OMAHVFIAQI.
PhylomeDBQ9LMI7.

Enzyme and pathway databases

BioCycARA:AT1G06310-MONOMER.

Gene expression databases

GenevestigatorQ9LMI7.

Family and domain databases

Gene3D2.40.110.10. 1 hit.
InterProIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
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.
SUPFAMSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
ProtoNetSearch...

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: June 11, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names