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Q00922 (ALOX_CANBO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. 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:AOD1
OrganismCandida boidinii (Yeast)
Taxonomic identifier5477 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
   Technical termDirect protein sequencing
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 – 663663Alcohol oxidase
PRO_0000205580

Regions

Nucleotide binding8 – 3932FAD By similarity
Motif661 – 6633Microbody targeting signal By similarity

Sites

Active site5671 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q00922 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: BC2E2F595B326AA6

FASTA66374,082
        10         20         30         40         50         60 
MAIPEEFDVI VCGGGSTGCV IAGRLANVDE NLKVLLIENG ENNLNNPWVY LPGIYPRNMR 

        70         80         90        100        110        120 
LDSKTATFYN SRPSKHLNGR RAIVPQANIL GGGSSINFMM YTRASASDYD DWESEGWTTD 

       130        140        150        160        170        180 
ELLPLMKKFE TYQRPCNNRD VHGFDGPIKV SFGNYTYPQC QDFLRACETQ GIPYVDDLED 

       190        200        210        220        230        240 
LKTSHGAEQW LKWINRDFGR RSDTAHAFIH STMRNKENLF LMTNTKVDKV IIEDGRAVAV 

       250        260        270        280        290        300 
RTVPSKPIGD SKVSRTFKAR KQIVVSCGTV SSPMVLQRSG IGEPSKLRAA GVKPIVELPG 

       310        320        330        340        350        360 
VGRNFQDHFC YFVPYRIKQD SESFDAFVSG DKEAQKSAFD QWYATGAGPL ATNGIEAGVK 

       370        380        390        400        410        420 
IRPTEAELAT ADKAFQQGWE SYFENKPDKP LMHYSVISGF FGDHTRLPPG KYMTMFHFLE 

       430        440        450        460        470        480 
YPFSRGWLHI SSDDPYAAPD FDPGFMNDDR DMWPMVWAFK KSRETARRME CFAGEPTAFH 

       490        500        510        520        530        540 
PHYKVDSPAR ALEQSAEDTK KVAGPLHLTA NLYHGSWSTP IGEADKHDPN HVTSSHINVY 

       550        560        570        580        590        600 
SKDIQYTKED DEAIENYIKE HAETTWHCLG TNSMAPREGN KNAPEGGVLD PRLNVHGVKG 

       610        620        630        640        650        660 
LKVADLSVCP DNVGCNTFST ALTIGEKAAV LVAEDLGYSG SELDMEVPQH KLKTYEQTGA 


ARY 

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References

[1]"Cloning and sequencing of the alcohol oxidase-encoding gene (AOD1) from the formaldehyde-producing asporogeneous methylotrophic yeast, Candida boidinii S2."
Sakai Y., Tani Y.
Gene 114:67-73(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11; 13-18 AND 20-35.
Strain: S2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81702 Genomic DNA. Translation: AAA34321.1.
PIRJC1117.

3D structure databases

ProteinModelPortalQ00922.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13165.
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_CANBO
AccessionPrimary (citable) accession number: Q00922
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 3, 2013
This is version 64 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