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P04841 (ALOX_PICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. 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:
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 identifier870730 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetales incertae sedisOgataea

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
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_processmethane catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

methanol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalcohol oxidase activity

Inferred from electronic annotation. Source: EC

choline dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

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 – 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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL Y-5445.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02425 Genomic DNA. Translation: CAA26278.1.
PIROXHQAP. A23010.

3D structure databases

ProteinModelPortalP04841.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00147.

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: April 3, 2013
This is version 69 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