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UniProtKB/Swiss-Prot entry Q00468

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

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Entry information
Entry name ACOX2_CANMA
Primary accession number Q00468
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 50)
Name and origin of the protein
Protein name Acyl-coenzyme A oxidase 2
Synonyms Acyl-CoA oxidase 2
AOX 2
EC 1.3.3.6
Gene name
Name: POX2
From
Candida maltosa (Yeast) [TaxID: 5479] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / IFO 1977 / JCM 1504;
DOI=10.1016/0378-1119(95)00655-9; PubMed=8566769 [NCBI, ExPASy, EBI, Israel, Japan]
Masuda Y., Park S.M., Ohta A., Takagi M.;
"Cloning and characterization of the POX2 gene in Candida maltosa.";
Gene 167:157-161(1995).
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
D21228; BAA04761.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4563; JC4563.
3D structure databases
ModBase Q00468.
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 Q00468.
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
CHAIN   1   724  724     Acyl-coenzyme A oxidase 2. PRO_0000204693
Sequence information
Length: 724 AA [This is the length of the unprocessed precursor] Molecular weight: 82274 Da [This is the MW of the unprocessed precursor] CRC64: 6081C636926CEFC1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MALISNLKDE YDHPTKTDPD TNPKIVADII SSKEPPQPSQ DVAEERSRTD WDLKEMHEFL 

        70         80         90        100        110        120 
EGDEAKSEEI LRLYQSIERD PILQTRPEQF DYTKNEERES VALRINQMSK YLETEPYEKF 

       130        140        150        160        170        180 
RRRLQLMTVN DPSLGIRMLV NIGLFLNCIR GNGTQKQYDF WAKTKEAGKV KQLLRLFRYD 

       190        200        210        220        230        240 
ELGHGFNVAG CEIFATFDEK TDQFIIDTPH IGATKWWIGG AAHSATHTVC YARLIVKDID 

       250        260        270        280        290        300 
YGVKTFVVPL RDSTHNLLPG VAIGDIGPKL GRQGVDNGWI QFTEVRIPRF FMLQRWCKVD 

       310        320        330        340        350        360 
RQGNVTLPPL EQLSYISLLE GRVGMATDSY RIGARYTTIA LRYAVARRQF SKGDGQPETK 

       370        380        390        400        410        420 
LIDYTLHQRR LLPYLALTYL AALGTDKLER QHDQLLKNLD KALATNNKLL LKNTIQSTKS 

       430        440        450        460        470        480 
MFVDSGSLKS TLTWLASDLI NEARQSCGGH GYSAYNGFGK TYGDWAVQCT WEGDNNVLGM 

       490        500        510        520        530        540 
SAGKTIIKTV QQVLNGKQLK DSTLEFLNDA PALSSAKKAV IRIKSHVDDT DRVLKAIAGL 

       550        560        570        580        590        600 
ISKYAKDLIP VSYQSWDSIG PQRVVLSKFR CHYYLLETFN ERLNDRIKAK SPARPHLENI 

       610        620        630        640        650        660 
IKLYYVTNVL GPFIDEFLRF GVISPSVAKY ITTEYPQKLC AAIRPYVIGL TDSFQQPDNF 

       670        680        690        700        710        720 
INSLIGRYDG NVYTNYLTNV TNVNDPTNYK APYSEALEAM LNRASLEERE RFEKSKAVAA 


KLSQ
Q00468 in FASTA format

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