Reviewed, UniProtKB/Swiss-Prot Q9LLH9 (ACOX3_ARATH)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A oxidase 3, peroxisomal
      Short name=AOX 3
    EC=1.3.3.6
Alternative name(s):
    Medium-chain acyl-CoA oxidase
      Short name=AtCX3

Gene names

Name:	ACX3
Ordered Locus Names:	At1g06290, At1g06300
ORF Names:	F9P14_11, F9P14.15, T2D23.1, F3E22.17, T8E24.15

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	675 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the desaturation of medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on C8:0- to C14:0-CoA with a maximal activity on C12:0-CoA.
Catalytic activity	Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
Cofactor	FAD.
Subcellular location	Peroxisome. Ref.2
Tissue specificity	Most abundant in flowers and senescing rosette leaves. Lower expression in hypocotyls, stems, young rosette leaves, cotyledons, cauline leaves and root tip of young seedlings. Ref.2 Ref.1
Developmental stage	Induced by seed imbibition with a peak at day 2 and then declines steadily until day 7. Not detected in developing seeds. Constitutive expression in root axis. Ref.1
Induction	Not induced by dehydration or abscisic acid (ABA). Ref.6
Sequence similarities	Belongs to the acyl-CoA oxidase family.
Biophysicochemical properties	Kinetic parameters: KM=3.7 µM for lauroyl-CoA pH dependence: Optimum pH is 8.5-9.0.
Sequence caution	The sequence AAF63829.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAG50996.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Traceable author statement. Source: TAIR medium-chain fatty acid metabolic process Traceable author statement. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro acyl-CoA oxidase activity Traceable author statement. Source: TAIR electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 34	34	Peroxisome Potential
	Chain	35 – 675	641	Acyl-coenzyme A oxidase 3, peroxisomal		PRO_0000000557
Regions
	Nucleotide binding	442 – 457	16	FAD Potential
Experimental info
	Sequence conflict	33	1	L → V in AAF73843. Ref.1
	Sequence conflict	578	1	I → M in AAG50996. Ref.3
	Sequence conflict	671	1	A → T in AAG50996. Ref.3
	Sequence conflict	671	1	A → T in AAF63829. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9LLH9-1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: FABBCBA01C5FC103	FASTA	675	75,676
	10 20 30 40 50 60 MSDNRALRRA HVLANHILQS NPPSSNPSLS RELCLQYSPP ELNESYGFDV KEMRKLLDGH 70 80 90 100 110 120 NVVDRDWIYG LMMQSNLFNR KERGGKIFVS PDYNQTMEQQ REITMKRIWY LLENGVFKGW 130 140 150 160 170 180 LTETGPEAEL RKLALLEVCG IYDHSVSIKV GVHFFLWGNA VKFFGTKRHH EKWLKNTEDY 190 200 210 220 230 240 VVKGCFAMTE LGHGSNVRGI ETVTTYDPKT EEFVINTPCE SAQKYWIGGA ANHATHTIVF 250 260 270 280 290 300 SQLHINGTNQ GVHAFIAQIR DQDGSICPNI RIADCGHKIG LNGVDNGRIW FDNLRIPREN 310 320 330 340 350 360 LLNAVADVSS DGKYVSSIKD PDQRFGAFMA PLTSGRVTIA SSAIYSAKVG LSIAIRYSLS 370 380 390 400 410 420 RRAFSVTANG PEVLLLDYPS HQRRLLPLLA KTYAMSFAAN ELKMIYVKRT PETNKAIHVV 430 440 450 460 470 480 SSGFKAVLTW HNMHTLQECR EAVGGQGVKT ENLVGQLKGE FDVQTTFEGD NNVLMQQVSK 490 500 510 520 530 540 ALFAEYVSCK KRNKPFKGLG LEHMNSPRPV LPTQLTSSTL RCSQFQTNVF CLRERDLLEQ 550 560 570 580 590 600 FTSEVAQLQG RGESREFSFL LSHQLAEDLG KAFTEKAILQ TILDAEAKLP TGSVKDVLGL 610 620 630 640 650 660 VRSMYALISL EEDPSLLRYG YLSQDNVGDV RREVSKLCGE LRPHALALVT SFGIPDSFLS 670 PIAFNWVEAN AWSSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis." Froman B.E., Edwards P.C., Bursch A.G., Dehesh K. Plant Physiol. 123:733-742(2000) [PubMed: 10859203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: cv. No-0.
[2]	"Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during Arabidopsis seed germination." Eastmond P.J., Hooks M.A., Williams D., Lange P., Bechtold N., Sarrobert C., Nussaume L., Graham I.A. J. Biol. Chem. 275:34375-34381(2000) [PubMed: 10918060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: cv. Columbia. Tissue: Hypocotyl.
[3]	"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. , 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.
[4]	"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. , 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.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"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: INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF207994 mRNA. Translation: AAF73843.1. AF253474 mRNA. Translation: AAF76137.1. AC068143 Genomic DNA. Translation: AAF82159.1. AC036106 Genomic DNA. Translation: AAG50996.1. Sequence problems. AC023912 Genomic DNA. Translation: AAF63829.1. Sequence problems. AY099579 mRNA. Translation: AAM20431.1. BT008413 mRNA. Translation: AAP37772.1. AK176257 mRNA. Translation: BAD44020.1.
IPI	IPI00524206.
PIR	G86198.
RefSeq	NP_172119.1.
UniGene	At.14938 At.53206
3D structure databases
HSSP	HSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBase	Search...
Proteomic databases
PRIDE	Q9LLH9.
Genome annotation databases
GeneID	837140.
GenomeReviews	Gene locus AT1G06290 in contig CT485782_GR.
KEGG	ath:AT1G06290.
NMPDR	fig|3702.1.peg.805.
Organism-specific databases
TAIR	At1g06290.
Phylogenomic databases
OMA	Q9LLH9. RRAFSIT.
Enzyme and pathway databases
BRENDA	1.3.3.6. 302.
Gene expression databases
GermOnline	AT1G06290. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl-CoA_oxidase_C. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
PANTHER	PTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
Pfam	PF01756. ACOX. 1 hit. PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACOX3_ARATH

Accession

Primary (citable) accession number: Q9LLH9
Secondary accession number(s): Q9C839 , Q9LKX5, Q9LMI8, Q9M7X6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	June 16, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)