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Reviewed, UniProtKB/Swiss-Prot P04841 (ALOX_PICAN)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alcohol oxidase
      Short name=AOX
    EC=1.1.3.13
Alternative name(s):
    Methanol oxidase
      Short name=MOX
Gene names
Name: MOX
OrganismPichia angusta (Yeast) (Hansenula polymorpha)
Taxonomic identifier4905 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaePichia

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

A primary alcohol + O2 = an aldehyde + H2O2.

Cofactor

FAD.

Pathway

Energy metabolism; methane degradation.

Subunit structure

Homooctamer.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
   Biological processMethanol utilization
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processmethanol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

alcohol oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 664664Alcohol oxidase
PRO_0000205581

Regions

Nucleotide binding8 – 3932FAD Probable
Motif662 – 6643Microbody targeting signal Potential

Sites

Active site5681 By similarity

Sequences

Sequence LengthMass (Da)Tools
P04841-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 6A4E3AFD6688BD5D

FASTA66474,089
        10         20         30         40         50         60 
MAIPDEFDII VVGGGSTGCC IAGRLANLDD QNLTVALIEG GENNINNPWV YLPGVYPRNM 

        70         80         90        100        110        120 
RLDSKTATFY SSRPSKALNG RRAIVPCANI LGGGSSINFL MYTRASASDY DDWESEGWST 

       130        140        150        160        170        180 
DELLPLIKKI ETYQRPCNNR DLHGFDGPIK VSFGNYTYPT CQDFLRAAES QGIPVVDDLE 

       190        200        210        220        230        240 
DFKTSHGAEH WLKWINRDLG RRSDSAHAYV HPTMRNKQSL FLITSTKCDK VIIEDGKAVA 

       250        260        270        280        290        300 
VRTVPMKPLN PKKPVSRTFR ARKQIVISCG TISSPLVLQR SGIGAAHHLR SVGVKPIVDL 

       310        320        330        340        350        360 
PGVGENFQDH YCFFTPYYVK PDVPTFDDFV RGDPVAQKAA FDQWYSNKDG PLTTNGIEAG 

       370        380        390        400        410        420 
VKIRPTEEEL ATADEDFRRG YAEYFENKPD KPLMHYSVIS GFFGDHTKIP NGKFMTMFHF 

       430        440        450        460        470        480 
LEYPFSRGFV RITSANPYDA PDFDPGFLND ERDLWPMVWA YKKSRETARR MESFAGEVTS 

       490        500        510        520        530        540 
HHPLFKVDSP ARARDLDLET CSAYAGPKHL TANLYHGSWT VPIDKPTPKN DFHVTSNQVQ 

       550        560        570        580        590        600 
LHSDIEYTEE DDEAIVNYIK EHTETTWHCL GTCSMAPREG SKIAPKGGVL DARLNVYGVQ 

       610        620        630        640        650        660 
NLKVADLSVC PDNVGCNTYS TALTIGEKAA TLVAEDLGYS GSDLDMTIPN FRLGTYEETG 


LARF 

« Hide

References

[1]"Molecular cloning and characterization of a gene coding for methanol oxidase in Hansenula polymorpha."
Ledeboer A.M., Edens L., Maat J., Visser C., Bos J.W., Verrips C.T.
Nucleic Acids Res. 13:3063-3082(1985) [PubMed: 2582370] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Drosophila glucose dehydrogenase and yeast alcohol oxidase are homologous and share N-terminal homology with other flavoenzymes."
Cavener D.R., Krasney P.
Mol. Biol. Evol. 8:144-150(1991) [PubMed: 2002763] [Abstract]
Cited for: SIMILARITY TO DROSOPHILA GLUCOSE DEHYDROGENASE.
[3]"Biosynthesis and assembly of alcohol oxidase, a peroxisomal matrix protein in methylotrophic yeasts: a review."
van der Klei I.J., Harder W., Veenhuis M.
Yeast 7:195-209(1991) [PubMed: 1882546] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

X02425 Genomic DNA. Translation: CAA26278.1.
PIROXHQAP. A23010.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.3.13. 276392.

Family and domain databases

InterProIPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFPIRSF000137. Alcohol_oxidase. 1 hit.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALOX_PICAN
AccessionPrimary (citable) accession number: P04841
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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) · Sequences · References · Cross-references · Entry information · Relevant documents