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Q00468 (ACOX2_CANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acyl-coenzyme A oxidase 2
Short name=AOX 2
Short name=Acyl-CoA oxidase 2
EC=1.3.3.6
Gene names
Name:POX2
OrganismCandida maltosa (Yeast)
Taxonomic identifier5479 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactor

FAD.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processfatty acid beta-oxidation

Inferred from electronic annotation. Source: InterPro

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyl-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Acyl-coenzyme A oxidase 2
PRO_0000204693

Sequences

Sequence LengthMass (Da)Tools
Q00468 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6081C636926CEFC1

FASTA72482,274
        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

« Hide

References

[1]"Cloning and characterization of the POX2 gene in Candida maltosa."
Masuda Y., Park S.M., Ohta A., Takagi M.
Gene 167:157-161(1995) [PubMed: 8566769] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D21228 Genomic DNA. Translation: BAA04761.1.
PIRJC4563.

3D structure databases

ProteinModelPortalQ00468.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR006091. 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]
Gene3DG3DSA: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.
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNetSearch...

Entry information

Entry nameACOX2_CANMA
AccessionPrimary (citable) accession number: Q00468
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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