Q6BRD5 (ACOX_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A oxidase
Short name=Acyl-CoA oxidase
EC=1.3.3.6

Gene names

Name:	POX1
Ordered Locus Names:	DEHA2D17248g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length	706 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
Cofactor	FAD By similarity.
Pathway	Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Subcellular location	Peroxisome By similarity.
Sequence similarities	Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro acyl-CoA oxidase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding 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 – 706	706	Acyl-coenzyme A oxidase		PRO_0000204698

Sequences

	Sequence		Length	Mass (Da)
	Q6BRD5 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: D3B95C9C5ADE2F62	FASTA	706	78,487
	10 20 30 40 50 60 MVSATNTVNS GVPPNPAASI QAERAASKFD PKEMHYFLEG GEERAEKFKQ MMQQMERDPI 70 80 90 100 110 120 LSANFQYYDL TKDQQRELTA LRIDRLTRYI ENESFDDFNK RMSLMGVFDP QLSTRLGINL 130 140 150 160 170 180 GLFVSCLKGN GTAEQVKYWA MDKSAVYMRG IYGCFGMTEL AHGSNVAGLE TTATFDDEND 190 200 210 220 230 240 EFIINTPHIG ATKWWIGGAA HSATHCSVYA RLIVGGQDYG VKTFVVPLRD SNHDTMPGVT 250 260 270 280 290 300 VGDIGAKMGR DGIDNGWIQF SNVRIPRYFM LQKFCKVSSE GDVQLPPLEQ LSYSALLGGR 310 320 330 340 350 360 VMMVLDSFRV SARFSTVALR YAIGRRQFKA GSASDDKNAL ECQLLDYPLH QRRLLPYLAL 370 380 390 400 410 420 SYIISASAVK IETTIESTLE NLDKAVEADD MGAIMKSIDS MKSLFVDSGS LKSTCTWLAA 430 440 450 460 470 480 EVIDQCRQAC GGHGYSAYSG FGKAYNDWVV MCTWEGDNNV LAMSVGKQII KHILGVLDGK 490 500 510 520 530 540 KVKGSADFLN NTEQYLNEEP VLRSVDDLKD LKKVLLAIEV AIIRVAYQAS QTLKENKGDF 550 560 570 580 590 600 DTVGAEMVTL SKLNAHHFML SEFLDRMDSF ESKQLVPYLE SVAKLYSATI VLEKFAGDFL 610 620 630 640 650 660 AQGVFPPKLN GELNSKHIPE LCKEIRPNVI ALTDSFQQSD MMINSAIGSY DGNIYENYFG 670 680 690 700 VVKANNPPSK TKAPYSGALE AMLNRPSKEE RERFEKSTET AKILSK

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382136 Genomic DNA. Translation: CAG87407.2.
RefSeq	XP_459235.2. XM_459235.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2901799.
GenomeReviews	Gene locus DEHA2D17248g in contig CR382136_GR.
KEGG	dha:DEHA2D17248g.
Phylogenomic databases
eggNOG	fuNOG06313.
HOGENOM	HBG737904.
OMA	MLMKHSK.
OrthoDB	EOG4ZGSMP.
Family and domain databases
InterPro	IPR006090. 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. [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.
KO	K00232.
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.
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNet	Search...

Entry information

Entry name

ACOX_DEBHA

Accession

Primary (citable) accession number: Q6BRD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	December 16, 2008
Last modified:	November 16, 2011
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program