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Protein

Alcohol oxidase 1

Gene

AOX1

Organism
Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Major isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts.2 Publications

Catalytic activityi

A primary alcohol + O2 = an aldehyde + H2O2.

Cofactori

FADBy similarity

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 sitei567 – 5671Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3831FADBy similarityAdd
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. 4827.
UniPathwayiUPA00147.

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol oxidase 1 (EC:1.1.3.13)
Short name:
AO 1
Short name:
AOX 1
Alternative name(s):
Methanol oxidase 1
Short name:
MOX 1
Gene namesi
Name:AOX1
Ordered Locus Names:PP7435_Chr4-0130
OrganismiKomagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1) (Yeast)
Taxonomic identifieri981350 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeKomagataella
Proteomesi
  • UP000006853 Componenti: Chromosome 4

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 – 663662Alcohol oxidase 1PRO_0000425715Add
BLAST

Expressioni

Inductioni

Induced by methanol. Subject to strong carbon catabolite repression.1 Publication

Interactioni

Subunit structurei

Homooctamer.1 Publication

Structurei

Secondary structure

1
663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Helixi16 – 2611Combined sources
Beta strandi34 – 374Combined sources
Beta strandi39 – 413Combined sources
Helixi47 – 504Combined sources
Helixi52 – 598Combined sources
Beta strandi64 – 696Combined sources
Helixi75 – 773Combined sources
Beta strandi84 – 874Combined sources
Helixi92 – 954Combined sources
Helixi106 – 1105Combined sources
Helixi119 – 12911Combined sources
Beta strandi130 – 1323Combined sources
Helixi139 – 1413Combined sources
Beta strandi147 – 1515Combined sources
Helixi159 – 16810Combined sources
Turni169 – 1713Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi192 – 1954Combined sources
Turni196 – 1994Combined sources
Helixi204 – 2085Combined sources
Helixi210 – 2134Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi224 – 23310Combined sources
Beta strandi236 – 24611Combined sources
Beta strandi256 – 26611Combined sources
Helixi269 – 27911Combined sources
Helixi285 – 2906Combined sources
Turni300 – 3034Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi310 – 3189Combined sources
Helixi326 – 3305Combined sources
Helixi333 – 34614Combined sources
Helixi350 – 3523Combined sources
Beta strandi355 – 3628Combined sources
Helixi366 – 3694Combined sources
Helixi374 – 38310Combined sources
Turni384 – 3863Combined sources
Beta strandi392 – 4009Combined sources
Helixi405 – 4073Combined sources
Beta strandi413 – 42210Combined sources
Beta strandi427 – 4304Combined sources
Beta strandi432 – 4343Combined sources
Beta strandi441 – 4433Combined sources
Helixi450 – 4523Combined sources
Helixi453 – 46816Combined sources
Beta strandi473 – 4764Combined sources
Helixi478 – 4803Combined sources
Helixi497 – 5048Combined sources
Helixi534 – 5363Combined sources
Helixi548 – 56114Combined sources
Beta strandi599 – 6035Combined sources
Helixi606 – 6083Combined sources
Helixi618 – 63518Combined sources
Helixi640 – 6445Combined sources
Helixi655 – 6584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5HSAX-ray2.35A/B/C/D/E/F/G/H1-663[»]
ProteinModelPortaliF2QY27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi661 – 6633Microbody 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

OrthoDBiEOG092C10SH.

Family and domain databases

Gene3Di3.50.50.60. 3 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

F2QY27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIPEEFDIL VLGGGSSGSC IAGRLANLDH SLKVGLIEAG ENNLNNPWVY
60 70 80 90 100
LPGIYPRNMK LDSKTASFYT SNPSPHLNGR RAIVPCANVL GGGSSINFMM
110 120 130 140 150
YTRGSASDYD DFQAEGWKTK DLLPLMKKTE TYQRACNNPD IHGFEGPIKV
160 170 180 190 200
SFGNYTYPVC QDFLRASESQ GIPYVDDLED LVTAHGAEHW LKWINRDTGR
210 220 230 240 250
RSDSAHAFVH STMRNHDNLY LICNTKVDKI IVEDGRAAAV RTVPSKPLNP
260 270 280 290 300
KKPSHKIYRA RKQIVLSCGT ISSPLVLQRS GFGDPIKLRA AGVKPLVNLP
310 320 330 340 350
GVGRNFQDHY CFFSPYRIKP QYESFDDFVR GDAEIQKRVF DQWYANGTGP
360 370 380 390 400
LATNGIEAGV KIRPTPEELS QMDESFQEGY REYFEDKPDK PVMHYSIIAG
410 420 430 440 450
FFGDHTKIPP GKYMTMFHFL EYPFSRGSIH ITSPDPYAAP DFDPGFMNDE
460 470 480 490 500
RDMAPMVWAY KKSRETARRM DHFAGEVTSH HPLFPYSSEA RALEMDLETS
510 520 530 540 550
NAYGGPLNLS AGLAHGSWTQ PLKKPTAKNE GHVTSNQVEL HPDIEYDEED
560 570 580 590 600
DKAIENYIRE HTETTWHCLG TCSIGPREGS KIVKWGGVLD HRSNVYGVKG
610 620 630 640 650
LKVGDLSVCP DNVGCNTYTT ALLIGEKTAT LVGEDLGYSG EALDMTVPQF
660
KLGTYEKTGL ARF
Length:663
Mass (Da):73,898
Last modified:May 31, 2011 - v1
Checksum:i2206F9319CDC96ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96967 Genomic DNA. Translation: AAB57849.1.
FR839631 Genomic DNA. Translation: CCA40305.1.

Genome annotation databases

EnsemblFungiiCCA40305; CCA40305; PP7435_Chr4-0130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96967 Genomic DNA. Translation: AAB57849.1.
FR839631 Genomic DNA. Translation: CCA40305.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5HSAX-ray2.35A/B/C/D/E/F/G/H1-663[»]
ProteinModelPortaliF2QY27.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCCA40305; CCA40305; PP7435_Chr4-0130.

Phylogenomic databases

OrthoDBiEOG092C10SH.

Enzyme and pathway databases

UniPathwayiUPA00147.
BRENDAi1.1.3.13. 4827.

Family and domain databases

Gene3Di3.50.50.60. 3 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALOX1_KOMPC
AccessioniPrimary (citable) accession number: F2QY27
Secondary accession number(s): Q9URI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: May 31, 2011
Last modified: September 7, 2016
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.