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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) (Pichia pastoris)
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)DescriptionActionsGraphical viewLength
Active sitei567Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi8 – 38FADBy similarityAdd BLAST31

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) (Pichia pastoris)
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00004257152 – 663Alcohol oxidase 1Add BLAST662

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homooctamer.1 Publication

Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Helixi16 – 26Combined sources11
Beta strandi34 – 37Combined sources4
Beta strandi39 – 41Combined sources3
Helixi47 – 50Combined sources4
Helixi52 – 59Combined sources8
Beta strandi64 – 69Combined sources6
Helixi75 – 77Combined sources3
Beta strandi84 – 87Combined sources4
Helixi92 – 95Combined sources4
Helixi106 – 110Combined sources5
Helixi119 – 129Combined sources11
Beta strandi130 – 132Combined sources3
Helixi139 – 141Combined sources3
Beta strandi147 – 151Combined sources5
Helixi159 – 168Combined sources10
Turni169 – 171Combined sources3
Beta strandi180 – 182Combined sources3
Beta strandi185 – 189Combined sources5
Beta strandi192 – 195Combined sources4
Turni196 – 199Combined sources4
Helixi204 – 208Combined sources5
Helixi210 – 213Combined sources4
Beta strandi217 – 222Combined sources6
Beta strandi224 – 233Combined sources10
Beta strandi236 – 246Combined sources11
Beta strandi256 – 266Combined sources11
Helixi269 – 279Combined sources11
Helixi285 – 290Combined sources6
Turni300 – 303Combined sources4
Beta strandi305 – 307Combined sources3
Beta strandi310 – 318Combined sources9
Helixi326 – 330Combined sources5
Helixi333 – 346Combined sources14
Helixi350 – 352Combined sources3
Beta strandi355 – 362Combined sources8
Helixi366 – 369Combined sources4
Helixi374 – 383Combined sources10
Turni384 – 386Combined sources3
Beta strandi392 – 400Combined sources9
Helixi405 – 407Combined sources3
Beta strandi413 – 422Combined sources10
Beta strandi427 – 430Combined sources4
Beta strandi432 – 434Combined sources3
Beta strandi441 – 443Combined sources3
Helixi450 – 452Combined sources3
Helixi453 – 468Combined sources16
Beta strandi473 – 476Combined sources4
Helixi478 – 480Combined sources3
Helixi497 – 504Combined sources8
Helixi534 – 536Combined sources3
Helixi548 – 561Combined sources14
Beta strandi599 – 603Combined sources5
Helixi606 – 608Combined sources3
Helixi618 – 635Combined sources18
Helixi640 – 644Combined sources5
Helixi655 – 658Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HSAX-ray2.35A/B/C/D/E/F/G/H1-663[»]
ProteinModelPortaliF2QY27.
SMRiF2QY27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi661 – 663Microbody targeting signalSequence analysis3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HSAX-ray2.35A/B/C/D/E/F/G/H1-663[»]
ProteinModelPortaliF2QY27.
SMRiF2QY27.
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: November 2, 2016
This is version 32 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.