Acyl-coenzyme A oxidase 4 - Candida tropicalis (Yeast)

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Reviewed, UniProtKB/Swiss-Prot P06598 (ACOX4_CANTR)

Last modified June 16, 2009. Version 77. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A oxidase 4
      Short name=Acyl-CoA oxidase 4
    EC=1.3.3.6
Alternative name(s):
    Peroxisomal fatty acyl-CoA oxidase
    PXP-4

Gene names

Name:	POX4
Synonyms:	AOX

Organism

Candida tropicalis (Yeast)

Taxonomic identifier

5482 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length	709 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

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

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Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro 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 Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 709

708

Acyl-coenzyme A oxidase 4

PRO_0000204696

Experimental info

Sequence conflict

217

Q → E in CAA68660. Ref.4

Sequence conflict

246

P → A Ref.3

Sequence conflict

246

P → A Ref.4

Sequence conflict

336

N → K in AAA34362. Ref.3

Sequence conflict

359 – 394

FVPPM…TTPRL → LAAAYVISAGALKVEDTIHN TLAELDAAVEKNDTKA Ref.3

Sequence conflict

359 – 394

FVPPM…TTPRL → LAAAYVISAGALKVEDTIHN TLAELDAAVEKNDTKA Ref.4

Sequence conflict

436

H → Y in AAA34362. Ref.3

Sequence conflict

463

G → A in AAA34362. Ref.3

Sequence conflict

496

E → S Ref.3

Sequence conflict

577 – 579

ELA → DLV in AAA34362. Ref.3

Sequence conflict

698

Q → E Ref.3

Sequence conflict

698

Q → E Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P06598-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0D60580353F5D927
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FASTA

709

79,094

        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

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References

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

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Cross-references

Sequence databases
	M16193 Genomic DNA. Translation: AAA34322.2. M12160 Genomic DNA. Translation: AAA34362.1. Y00623 mRNA. Translation: CAA68660.1. Y00623 mRNA. Translation: CAA68661.1. Different initiation. Y00623 mRNA. Translation: CAA68662.1. Different initiation.
PIR	OXCKX4. A25123. OXCKAX. A28584. OXCKX. A29047.
3D structure databases
HSSP	HSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.3.6. 1242.
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...

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Entry information

Entry name

ACOX4_CANTR

Accession

Primary (citable) accession number: P06598
Secondary accession number(s): P11355

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents