Reviewed, UniProtKB/Swiss-Prot Q96329 (ACOX4_ARATH)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A oxidase 4, peroxisomal
      Short name=AOX 4
    EC=1.3.3.6
Alternative name(s):
    Short-chain acyl-CoA oxidase
      Short name=SAOX
      Short name=AtCX4
      Short name=AtG6
    G6p

Gene names

Name:	ACX4
Synonyms:	G6
Ordered Locus Names:	At3g51840

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	436 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 short-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Has no activity as acyl-CoA dehydrogenase or on crotonyl-CoA (an unsaturated C4:1 carbocyclic ester) or glutaryl-CoA (a dicarboxylic ester).
Catalytic activity	Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
Cofactor	FAD.
Subunit structure	Homotetramer.
Subcellular location	Glyoxysome. Peroxisome.
Tissue specificity	Particularly abundant in etiolated cotyledons. Also present in flowers, roots and siliques, but not detected in green cotyledons, rosette leaves and stems. Ref.2
Developmental stage	Induced by seed imbibition with a peak at day 5 to 7. Decreases after illumination but still detectable 5 days after illumination.
Induction	Induced by dehydration and abscisic acid (ABA). Ref.7
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=8.3 µM for hexanoyl-CoA pH dependence: Optimum pH is 8.5-9.0.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Glyoxysome Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	embryonic development ending in seed dormancy Inferred from genetic interaction. Source: TAIR fatty acid beta-oxidation Ref.2 Inferred from direct assay. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW short-chain fatty acid metabolic process Traceable author statement. Source: TAIR
Cellular component	glyoxysome 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.2 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 – 436

436

Acyl-coenzyme A oxidase 4, peroxisomal

PRO_0000201211

Regions

Nucleotide binding

172 – 175

4

FAD

Nucleotide binding

205 – 207

3

FAD

Nucleotide binding

324 – 326

3

FAD

Nucleotide binding

381 – 385

5

FAD

Nucleotide binding

410 – 412

3

FAD

Region

181 – 184

4

Substrate binding

Motif

434 – 436

3

Microbody targeting signal Potential

Sites

Binding site

181

1

FAD

Binding site

288

1

Substrate

Binding site

313

1

FAD

Binding site

409

1

Substrate; via amide nitrogen

Binding site

420

1

Substrate

Binding site

428

1

FAD; via carbonyl oxygen

Secondary structure

1

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436

Helix Strand Turn

Details...

Beta strand

19 – 23

5

Helix

28 – 31

4

Helix

51 – 54

4

Helix

57 – 73

17

Helix

75 – 84

10

Helix

89 – 91

3

Helix

92 – 96

5

Turn

97 – 99

3

Turn

101 – 104

4

Helix

115 – 128

14

Helix

130 – 140

11

Helix

143 – 150

8

Helix

153 – 164

12

Beta strand

170 – 173

4

Beta strand

179 – 181

3

Helix

183 – 185

3

Beta strand

189 – 193

5

Beta strand

196 – 207

12

Turn

208 – 211

4

Beta strand

213 – 221

9

Turn

222 – 224

3

Beta strand

225 – 233

9

Beta strand

239 – 243

5

Beta strand

247 – 250

4

Beta strand

255 – 266

12

Helix

267 – 269

3

Helix

277 – 312

36

Helix

320 – 322

3

Helix

324 – 352

29

Helix

358 – 382

25

Helix

383 – 388

6

Helix

390 – 392

3

Helix

394 – 406

13

Beta strand

407 – 409

3

Helix

411 – 423

13

Sequences

	Sequence		Length	Mass (Da)
	Q96329-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: B6050262D9482C6D	FASTA	436	47,557
	10 20 30 40 50 60 MAVLSSADRA SNEKKVKSSY FDLPPMEMSV AFPQATPAST FPPCTSDYYH FNDLLTPEEQ 70 80 90 100 110 120 AIRKKVRECM EKEVAPIMTE YWEKAEFPFH ITPKLGAMGV AGGSIKGYGC PGLSITANAI 130 140 150 160 170 180 ATAEIARVDA SCSTFILVHS SLGMLTIALC GSEAQKEKYL PSLAQLNTVA CWALTEPDNG 190 200 210 220 230 240 SDASGLGTTA TKVEGGWKIN GQKRWIGNST FADLLIIFAR NTTTNQINGF IVKKDAPGLK 250 260 270 280 290 300 ATKIPNKIGL RMVQNGDILL QNVFVPDEDR LPGVNSFQDT SKVLAVSRVM VAWQPIGISM 310 320 330 340 350 360 GIYDMCHRYL KERKQFGAPL AAFQLNQQKL VQMLGNVQAM FLMGWRLCKL YETGQMTPGQ 370 380 390 400 410 420 ASLGKAWISS KARETASLGR ELLGGNGILA DFLVAKAFCD LEPIYTYEGT YDINTLVTGR 430 EVTGIASFKP ATRSRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the Arabidopsis thaliana Em1 locus." Grellet F., Gaubier P., Wu H.-J., Laudie M., Berger C., Delseny M. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes." Hayashi H., De Bellis L., Ciurli A., Kondo M., Hayashi M., Nishimura M. J. Biol. Chem. 274:12715-12721(1999) [PubMed: 10212254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY. Strain: cv. Columbia.
[3]	"Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1 locus on chromosome III." Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M., Grellet F. Plant Mol. Biol. 41:687-700(1999) [PubMed: 10645728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"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.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"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.
[8]	"Controlling electron transfer in acyl-CoA oxidases and dehydrogenases: a structural view." Mackenzie J., Pedersen L., Arent S., Henriksen A. J. Biol. Chem. 281:31012-31020(2006) [PubMed: 16887802] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NAD AND ACYL-COA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U72505 mRNA. Translation: AAB18129.1.
AB017643 mRNA. Translation: BAA82478.1.
AF049236 Genomic DNA. Translation: AAC14411.1.
AY094441 mRNA. Translation: AAM19813.1.
AY125536 mRNA. Translation: AAM78046.1.
AY087793 mRNA. Translation: AAM65329.1.

IPI

IPI00544713.

PIR

T46895.

RefSeq

NP_190752.1.

UniGene

At.21620

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IX5	X-ray	2.70	A/B/C/D	1-436	[»]
2IX6	X-ray	3.90	A/B/C/D/E/F	1-436	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q96329.

Proteomic databases

PRIDE

Q96329.

ProMEX

Q96329.

Genome annotation databases

GeneID

824347.

GenomeReviews

Gene locus AT3G51840 in contig BA000014_GR.

KEGG

ath:AT3G51840.

NMPDR

fig|3702.1.peg.16441.

Organism-specific databases

GeneFarm

4887.

TAIR

At3g51840.

Phylogenomic databases

OMA

INDYWER.

Enzyme and pathway databases

BRENDA

1.3.3.6. 302.

Gene expression databases

Genevestigator

Q96329.

GermOnline

AT3G51840. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_M.
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. 1 hit.

Pfam

PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]

PROSITE

PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACOX4_ARATH

Accession

Primary (citable) accession number: Q96329

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	February 1, 1997
Last modified:	November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)