Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alcohol oxidase

Gene

MOX

Organism
Pichia angusta (Yeast) (Hansenula polymorpha)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts.1 Publication

Catalytic activityi

A primary alcohol + O2 = an aldehyde + H2O2.

Cofactori

FAD2 PublicationsNote: May possess two different forms of flavin adenine dinucleotide, classical FAD and so-called modified FAD (mFAD), a stereochemical FAD analog, in which the C2 carbon of the ribityl chain has changed from the R to the S configuration. Conversion of FAD into mFAD was observed both in purified preparations of the enzyme and in cells grown in batch and continuous culture. The relative amount of mFAD in the enzyme varied from 5 to 95%, depending on the growth or storage conditions. The presence of mFAD led to a slight decrease in Vmax and a significant decrease in the KM of alcohol oxidase with respect to methanol.2 Publications

Pathwayi: methane degradation

This protein is involved in the pathway methane degradation, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway methane degradation and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei568 – 5681Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3932FADCuratedAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.3.13. 2587.
UniPathwayiUPA00147.

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol oxidase (EC:1.1.3.13)
Short name:
AO
Short name:
AOX
Alternative name(s):
Methanol oxidase
Short name:
MOX
Gene namesi
Name:MOX
OrganismiPichia angusta (Yeast) (Hansenula polymorpha)
Taxonomic identifieri870730 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataea

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 664663Alcohol oxidasePRO_0000205581Add
BLAST

Expressioni

Inductioni

Induced by methanol. Subject to strong carbon catabolite repression (By similarity).By similarity

Interactioni

Subunit structurei

Homooctamer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP04841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi662 – 6643Microbody targeting signalSequence analysis

Domaini

The C-terminal peroxisomal targeting signal (PTS) is essential for the efficient targeting and import of AOX into peroxisomes via the PTS1 pathway.By similarity

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Phylogenomic databases

PhylomeDBiP04841.

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04841-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIPDEFDII VVGGGSTGCC IAGRLANLDD QNLTVALIEG GENNINNPWV
60 70 80 90 100
YLPGVYPRNM RLDSKTATFY SSRPSKALNG RRAIVPCANI LGGGSSINFL
110 120 130 140 150
MYTRASASDY DDWESEGWST DELLPLIKKI ETYQRPCNNR DLHGFDGPIK
160 170 180 190 200
VSFGNYTYPT CQDFLRAAES QGIPVVDDLE DFKTSHGAEH WLKWINRDLG
210 220 230 240 250
RRSDSAHAYV HPTMRNKQSL FLITSTKCDK VIIEDGKAVA VRTVPMKPLN
260 270 280 290 300
PKKPVSRTFR ARKQIVISCG TISSPLVLQR SGIGAAHHLR SVGVKPIVDL
310 320 330 340 350
PGVGENFQDH YCFFTPYYVK PDVPTFDDFV RGDPVAQKAA FDQWYSNKDG
360 370 380 390 400
PLTTNGIEAG VKIRPTEEEL ATADEDFRRG YAEYFENKPD KPLMHYSVIS
410 420 430 440 450
GFFGDHTKIP NGKFMTMFHF LEYPFSRGFV RITSANPYDA PDFDPGFLND
460 470 480 490 500
ERDLWPMVWA YKKSRETARR MESFAGEVTS HHPLFKVDSP ARARDLDLET
510 520 530 540 550
CSAYAGPKHL TANLYHGSWT VPIDKPTPKN DFHVTSNQVQ LHSDIEYTEE
560 570 580 590 600
DDEAIVNYIK EHTETTWHCL GTCSMAPREG SKIAPKGGVL DARLNVYGVQ
610 620 630 640 650
NLKVADLSVC PDNVGCNTYS TALTIGEKAA TLVAEDLGYS GSDLDMTIPN
660
FRLGTYEETG LARF
Length:664
Mass (Da):74,089
Last modified:August 13, 1987 - v1
Checksum:i6A4E3AFD6688BD5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02425 Genomic DNA. Translation: CAA26278.1.
PIRiA23010. OXHQAP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02425 Genomic DNA. Translation: CAA26278.1.
PIRiA23010. OXHQAP.

3D structure databases

ProteinModelPortaliP04841.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

PhylomeDBiP04841.

Enzyme and pathway databases

UniPathwayiUPA00147.
BRENDAi1.1.3.13. 2587.

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALOX_PICAN
AccessioniPrimary (citable) accession number: P04841
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 7, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.