[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 20336 / pK233 / NCYC 997; DOI=10.1016/0378-1119(87)90300-3; PubMed=3596241 [NCBI, ExPASy, EBI, Israel, Japan] Murray W.W., Rachubinski R.A.; "The primary structure of a peroxisomal fatty acyl-CoA oxidase from the yeast Candida tropicalis pK233."; Gene 51:119-128(1987).
[2]	SEQUENCE REVISION TO 367; 381 AND 385. Murray W.W., Rachubinski R.A.; Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 20336 / pK233 / NCYC 997; PubMed=3456583 [NCBI, ExPASy, EBI, Israel, Japan] Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.; "Two acyl-coenzyme A oxidases in peroxisomes of the yeast Candida tropicalis: primary structures deduced from genomic DNA sequence."; Proc. Natl. Acad. Sci. U.S.A. 83:1232-1236(1986).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 208-709. STRAIN=RR1; DOI=10.1083/jcb.105.1.247; PubMed=3611187 [NCBI, ExPASy, EBI, Israel, Japan] Small G.M., Lazarow P.B.; "Import of the carboxy-terminal portion of acyl-CoA oxidase into peroxisomes of Candida tropicalis."; J. Cell Biol. 105:247-250(1987).

Comments

CATALYTIC ACTIVITY: Acyl-CoA + O₂ = trans-2,3-dehydroacyl-CoA + H₂O₂.
COFACTOR: FAD.
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation .
SUBUNIT: Homooctamer.
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the acyl-CoA oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M16193; AAA34322.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12160; AAA34362.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00623; CAA68660.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00623; CAA68661.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00623; CAA68662.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25123; OXCKX4.
A28584; OXCKAX.
A29047; OXCKX.

3D structure databases

HSSP

P07872; 1IS2. [HSSP ENTRY / PDB]

ModBase

P06598.

Ontologies

GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR012258; Acyl-CoA_oxidase.
IPR002655; Acyl_CoA_ox_C.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.

PANTHER

PTHR10909:SF11; Acyl-CoA_oxidase; 1.

Pfam

PF01756; ACOX; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000168; Acyl-CoA_oxidase; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 709`	`708`	`Acyl-coenzyme A oxidase 4.`	`PRO_0000204696`
`CONFLICT`	`217 217`		`Q -> E (in Ref. 4; CAA68660).`
`CONFLICT`	`246 246`		`P -> A (in Ref. 3 and 4).`
`CONFLICT`	`336 336`		`N -> K (in Ref. 3; AAA34362).`
`CONFLICT`	`359 394`		`FVPPMSSPSVPSRLNTPSRPPWSNWTSPLKRTTPRL -> LAAAYVISAGALKVEDTIHNTLAELDAAVEKNDTKA (in Ref. 3 and 4).`
`CONFLICT`	`436 436`		`H -> Y (in Ref. 3; AAA34362).`
`CONFLICT`	`463 463`		`G -> A (in Ref. 3; AAA34362).`
`CONFLICT`	`496 496`		`E -> S (in Ref. 3).`
`CONFLICT`	`577 579`		`ELA -> DLV (in Ref. 3; AAA34362).`
`CONFLICT`	`698 698`		`Q -> E (in Ref. 3 and 4).`

Sequence information

Length: 709 AA [This is the length of the unprocessed precursor]

Molecular weight: 79094 Da [This is the MW of the unprocessed precursor]

CRC64: 0D60580353F5D927 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTFTKKNVSV SQGPDPRSSI QKERDSSKWN PQQMNYFLEG SVERSELMKA LAQQMERDPI 

        70         80         90        100        110        120 
LFTDGSYYDL TKDQQRELTA VKINRIARYR EQESIDTFNK RLSLIGIFDP QVGTRIGVNL 

       130        140        150        160        170        180 
GLFLSCIRGN GTTSQLNYWA NEKETADVKG IYGCFGMTEL AHGSNVAGLE TTATFDKESD 

       190        200        210        220        230        240 
EFVINTPHIG ATKWWIGGAA HSATHCSVYA RLIVDGQDYG VKTFVVPLRD SNHDLMPGVT 

       250        260        270        280        290        300 
VGDIGPKMGR DGIDNGWIQF SNVRIPRFFM LQKFCKVSAE GEVTLPPLEQ LSYSALLGGR 

       310        320        330        340        350        360 
VMMVLDSYRM LARMSTIALR YAIGRRQFKG DNVDPNDPNA LETQLIDYPL HQKRLFPYFV 

       370        380        390        400        410        420 
PPMSSPSVPS RLNTPSRPPW SNWTSPLKRT TPRLIFKSID DMKSLFVDSG SLKSTATWLG 

       430        440        450        460        470        480 
AEAIDQCRQA CGGHGHSSYN GFGKAYNDWV VQCTWEGDNN VLGMSVGKPI VKQVISIEDA 

       490        500        510        520        530        540 
GKTVRGSTAF LNQLKEYTGS NSSKVVLNTV ADLDDIKTVI KAIEVAIIRL SQEAASIVKK 

       550        560        570        580        590        600 
ESFDYVGAEL VQLSKLKAHH YLLTEYIRRI DTFDQKELAP YLITLGKLYA ATIVLDRFAG 

       610        620        630        640        650        660 
VFLTFNVAST EAITALASVQ IPKLCAEVRP NVVAYTDSFQ QSDMIVNSAI GRYDGDIYEN 

       670        680        690        700 
YFDLVKLQNP PSKTKAPYSD ALEAMLNRPT LDERERFQKS DETAAILSK

P06598 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools