Reviewed, UniProtKB/Swiss-Prot O65202 (ACOX1_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxisomal acyl-coenzyme A oxidase 1
      Short name=AOX 1
    EC=1.3.3.6
Alternative name(s):
    Long-chain acyl-CoA oxidase
      Short name=AtCX1

Gene names

Name:	ACX1
Ordered Locus Names:	At4g16760
ORF Names:	dl4405c, FCAALL.119

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	664 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the desaturation of both long- and medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Most active with C14-CoA. Activity on long-chain mono-unsaturated substrates is 40% higher than with the corresponding saturated substrates. Seems to be an important factor in the general metabolism of root tips. May be involved in the biosynthesis of jasmonic acid.
Catalytic activity	Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer.
Subcellular location	Peroxisome Probable.
Tissue specificity	Expressed mainly in flowers and young seedlings. Lower expression in roots, leaves and bracts. Ref.1
Developmental stage	Induced by seed imbibition with a peak at day 2 and then declines to reach a basal level 4 days after sowing. Ref.1
Induction	Induced by dehydration, abscisic acid (ABA) and jasmonic acid (JA), and localy and systemically by wounding. Ref.5
Sequence similarities	Belongs to the acyl-CoA oxidase family.
Biophysicochemical properties	Kinetic parameters: KM=5.3 µM for C14-CoA
Sequence caution	The sequence CAB10450.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78718.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Ref.1 Inferred from direct assay. Source: TAIR long-chain fatty acid metabolic process Ref.1 Inferred from mutant phenotype. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR response to wounding Inferred from expression pattern. Source: TAIR
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 Ref.1 Inferred from direct assay. 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

Chain

1 – 664

664

Peroxisomal acyl-coenzyme A oxidase 1

PRO_0000204689

Regions

Nucleotide binding

399 – 404

6

FAD

Motif

662 – 664

3

Microbody targeting signal

Sites

Active site

424

1

Proton acceptor By similarity

Binding site

138

1

FAD By similarity

Binding site

177

1

FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond

467 ↔ 576

Secondary structure

1

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664

Helix Strand Turn

Details...

Helix

8 – 11

4

Helix

18 – 26

9

Helix

29 – 43

15

Helix

46 – 48

3

Turn

51 – 54

4

Helix

58 – 78

21

Helix

83 – 93

11

Helix

98 – 104

7

Helix

106 – 113

8

Helix

116 – 127

12

Beta strand

133 – 136

4

Beta strand

142 – 144

3

Helix

146 – 148

3

Beta strand

152 – 155

4

Turn

157 – 159

3

Beta strand

160 – 165

6

Helix

169 – 171

3

Beta strand

172 – 174

3

Turn

177 – 182

6

Beta strand

184 – 194

11

Beta strand

197 – 207

11

Turn

211 – 213

3

Beta strand

220 – 224

5

Beta strand

228 – 232

5

Helix

233 – 236

4

Beta strand

240 – 250

11

Helix

251 – 253

3

Beta strand

257 – 261

5

Beta strand

267 – 269

3

Helix

274 – 276

3

Turn

278 – 282

5

Helix

283 – 309

27

Helix

324 – 326

3

Helix

328 – 361

34

Turn

362 – 365

4

Helix

370 – 397

28

Helix

398 – 404

7

Helix

406 – 408

3

Helix

410 – 417

8

Helix

418 – 421

4

Turn

422 – 424

3

Helix

427 – 442

16

Turn

443 – 447

5

Helix

453 – 460

8

Helix

461 – 464

4

Helix

474 – 478

5

Helix

480 – 502

23

Beta strand

505 – 507

3

Helix

508 – 514

7

Helix

516 – 538

23

Helix

548 – 566

19

Helix

568 – 573

6

Helix

579 – 596

18

Helix

597 – 599

3

Helix

600 – 605

6

Helix

611 – 614

4

Helix

626 – 635

10

Helix

637 – 640

4

Helix

647 – 650

4

Helix

652 – 655

4

Sequences

	Sequence		Length	Mass (Da)
	O65202-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 44AFD139D5434636	FASTA	664	74,302
	10 20 30 40 50 60 MEGIDHLADE RNKAEFDVED MKIVWAGSRH AFEVSDRIAR LVASDPVFEK SNRARLSRKE 70 80 90 100 110 120 LFKSTLRKCA HAFKRIIELR LNEEEAGRLR HFIDQPAYVD LHWGMFVPAI KGQGTEEQQK 130 140 150 160 170 180 KWLSLANKMQ IIGCYAQTEL GHGSNVQGLE TTATFDPKTD EFVIHTPTQT ASKWWPGGLG 190 200 210 220 230 240 KVSTHAVVYA RLITNGKDYG IHGFIVQLRS LEDHSPLPNI TVGDIGTKMG NGAYNSMDNG 250 260 270 280 290 300 FLMFDHVRIP RDQMLMRLSK VTREGEYVPS DVPKQLVYGT MVYVRQTIVA DASNALSRAV 310 320 330 340 350 360 CIATRYSAVR RQFGAHNGGI ETQVIDYKTQ QNRLFPLLAS AYAFRFVGEW LKWLYTDVTE 370 380 390 400 410 420 RLAASDFATL PEAHACTAGL KSLTTTATAD GIEECRKLCG GHGYLWCSGL PELFAVYVPA 430 440 450 460 470 480 CTYEGDNVVL QLQVARFLMK TVAQLGSGKV PVGTTAYMGR AAHLLQCRSG VQKAEDWLNP 490 500 510 520 530 540 DVVLEAFEAR ALRMAVTCAK NLSKFENQEQ GFQELLADLV EAAIAHCQLI VVSKFIAKLE 550 560 570 580 590 600 QDIGGKGVKK QLNNLCYIYA LYLLHKHLGD FLSTNCITPK QASLANDQLR SLYTQVRPNA 610 620 630 640 650 660 VALVDAFNYT DHYLNSVLGR YDGNVYPKLF EEALKDPLND SVVPDGYQEY LRPVLQQQLR TARL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Long-chain acyl-CoA oxidases of Arabidopsis." Hooks M.A., Kellas F., Graham I.A. Plant J. 20:1-13(1999) [PubMed: 10571860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, CHARACTERIZATION. Strain: cv. Columbia. Tissue: Seedling hypocotyl.
[2]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [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]	"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.
[6]	"Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism." Pedersen L., Henriksen A. J. Mol. Biol. 345:487-500(2005) [PubMed: 15581893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-659 OF MUTANT LEU-155.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF057044 mRNA. Translation: AAC13498.1.
Z97341 Genomic DNA. Translation: CAB10450.1. Sequence problems.
AL161544 Genomic DNA. Translation: CAB78718.1. Sequence problems.
AY058849 mRNA. Translation: AAL24237.1.
BT001067 mRNA. Translation: AAN46824.1.

IPI

IPI00534569.

PIR

H71434.
T52121.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W07	X-ray	2.00	A/B	1-659	[»]

ModBase

Search...

Proteomic databases

PRIDE

O65202.

Genome annotation databases

GenomeReviews

Gene locus AT4G16760 in contig CT486007_GR.

Organism-specific databases

TAIR

At4g16760.

Enzyme and pathway databases

BRENDA

1.3.3.6. 302.

Gene expression databases

GermOnline

AT4G16760. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR006091. 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]

Gene3D

G3DSA: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.

PANTHER

PTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.

Pfam

PF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]

PIRSF

PIRSF000168. Acyl-CoA_oxidase. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ACOX1_ARATH

Accession

Primary (citable) accession number: O65202
Secondary accession number(s): O23518

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)