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UniProtKB/Swiss-Prot entry P08790

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACOX5_CANTR
Primary accession number P08790
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Acyl-coenzyme A oxidase 5
Synonyms Acyl-CoA oxidase 5
EC 1.3.3.6
PXP-5
Gene name
Name: POX5
From
Candida tropicalis (Yeast) [TaxID: 5482] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
[2]
 SEQUENCE REVISION TO 265.
Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
Comments
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
M12161; AAA34363.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B25123; OXCKX5.
3D structure databases
HSSP P07872; 1IS2. [HSSP ENTRY / PDB]
ModBase P08790.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from InterPro).
GO:0003995; Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997; Molecular function: acyl-CoA oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635; Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
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.
ProtoNet P08790.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   662  661     Acyl-coenzyme A oxidase 5. PRO_0000204697
Sequence information
Length: 662 AA [This is the length of the unprocessed precursor] Molecular weight: 74238 Da [This is the MW of the unprocessed precursor] CRC64: 6746A72B6AD1986C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPTELQKERE LTKFNPKELN YFLEGSQERS EIISNMVEQM QKDPILKVDA SYYNLTKDQQ 

        70         80         90        100        110        120 
REVTAKKIAR LSRYFEHEYP DQQAQRLSIL GVFDPQVFTR IGVNLGLFVS CVRGNGTNSQ 

       130        140        150        160        170        180 
FFYWTINKGI DKLRGIYGCF GMTELAHGSN VQGIETTATF DEDTDEFVIN TPHIGATKWW 

       190        200        210        220        230        240 
IGGAAHSATH CSVYARLKVK GKDYGVKTFV VPLRDSNHDL EPGVTVGDIG AKMGRDGIDN 

       250        260        270        280        290        300 
GWIQFSNVRI PRFFMLQKYC KVSRSGEVTM PPSEQLSYSA LIGGRVTMMM DSYRMTSRFI 

       310        320        330        340        350        360 
TIALRYAIHR RQFKKKDTDT IETKLIDYPL HQKRLFPFLA AAYLFSQGAL YLEQTMNATN 

       370        380        390        400        410        420 
DKLDEAVSAG EKEAIDAAIV ESKKLFVASG CLKSTCTWLT AEAIDEARQA CGGHGYSSYN 

       430        440        450        460        470        480 
GFGKAYSDWV VQCTWEGDNN ILAMNVAKPM VRDLLKEPEQ KGLVLSSVAD LDDPAKLVKA 

       490        500        510        520        530        540 
FDHALSGLAR DIGAVAEDKG FDITGPSLVL VSKLNAHRFL IDGFFKRITP EWSEVLRPLG 

       550        560        570        580        590        600 
FLYADWILTN FGATFLQYGI ITPDVSRKIS SEHFPALCAK VRPNVVGLTD GFNLTDMMTN 

       610        620        630        640        650        660 
AAIGRYDGNV YEHYFETVKA LNPPENTKAP YSKALEDMLN RPDLEVRERG EKSEEAAEIL 


SS
P08790 in FASTA format

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